Login| Sign Up| Help| Contact|

Patent Searching and Data


Title:
CLEANING COMPOSITION COMPRISING ANIONIC SURFACTANT AND A POLYPEPTIDE HAVING RNASE ACTIVITY
Document Type and Number:
WIPO Patent Application WO/2020/070014
Kind Code:
A1
Abstract:
The present invention relates to cleaning compositions comprising at least one polypeptide having RNase activity, a method for cleaning an item and use of the cleaning composition according to the invention.

Inventors:
BALTSEN LILIAN (DK)
BARRIENTOS FABIAN (DK)
NISSEN DOROTA (DK)
SEGURA DOROTEA (DK)
SALOMON JESPER (DK)
OEHLENSCHLAEGER CHRISTIAN (DK)
Application Number:
PCT/EP2019/076239
Publication Date:
April 09, 2020
Filing Date:
September 27, 2019
Export Citation:
Click for automatic bibliography generation   Help
Assignee:
NOVOZYMES AS (DK)
International Classes:
C11D1/02; C11D3/386; C11D11/00; C12N9/22
Domestic Patent References:
WO1994000016A11994-01-06
WO2018185285A12018-10-11
WO2018178061A12018-10-04
WO2006031554A22006-03-23
WO2015155350A12015-10-15
WO2018178061A12018-10-04
WO2016176280A12016-11-03
WO2009102854A12009-08-20
WO1998017767A11998-04-30
WO2007087258A22007-08-02
WO2007087244A22007-08-02
WO2007087259A22007-08-02
WO2007087242A22007-08-02
WO1994026860A11994-11-24
WO1994026859A11994-11-24
WO2006130575A22006-12-07
WO2005003274A12005-01-13
WO2005003275A12005-01-13
WO2005003276A12005-01-13
WO2007087257A22007-08-02
WO2007087243A22007-08-02
WO1989009259A11989-10-05
WO1996011262A11996-04-18
WO1996029397A11996-09-26
WO1998008940A11998-03-05
WO1994007998A11994-04-14
WO1995024471A11995-09-14
WO1998012307A11998-03-26
WO1999001544A11999-01-14
WO2002099091A22002-12-12
WO2001062903A12001-08-30
WO1999064619A21999-12-16
WO1993024618A11993-12-09
WO1995010602A11995-04-20
WO1998015257A11998-04-16
WO1996013580A11996-05-09
WO1995006720A11995-03-09
WO1996027002A11996-09-06
WO1996012012A11996-04-25
WO2010065455A22010-06-10
WO2010107560A22010-09-23
WO2011084412A12011-07-14
WO2011084417A12011-07-14
WO2011084599A12011-07-14
WO2011150157A22011-12-01
WO2012137147A12012-10-11
WO1992005249A11992-04-02
WO1994001541A11994-01-20
WO1994025578A11994-11-10
WO1995014783A11995-06-01
WO1995030744A21995-11-16
WO1995035381A11995-12-28
WO1995022615A11995-08-24
WO1996000292A11996-01-04
WO1997004079A11997-02-06
WO1997007202A11997-02-27
WO2000034450A12000-06-15
WO2000060063A12000-10-12
WO2001092502A12001-12-06
WO2007087508A22007-08-02
WO2009109500A12009-09-11
WO2010111143A22010-09-30
WO2005056782A22005-06-23
WO2009067279A12009-05-28
WO2010100028A22010-09-10
WO1995010603A11995-04-20
WO1994002597A11994-02-03
WO1994018314A11994-08-18
WO1997043424A11997-11-20
WO1999019467A11999-04-22
WO2002010355A22002-02-07
WO2006066594A22006-06-29
WO1996023873A11996-08-08
WO2008153815A22008-12-18
WO2001066712A22001-09-13
WO2009061380A22009-05-14
WO2013184577A12013-12-12
WO2010104675A12010-09-16
WO2011098531A12011-08-18
WO2013001078A12013-01-03
WO2013001087A22013-01-03
WO2009021867A22009-02-19
WO1993018140A11993-09-16
WO2001016285A22001-03-08
WO2002016547A22002-02-28
WO1994025583A11994-11-10
WO2005040372A12005-05-06
WO2005052161A22005-06-09
WO2005052146A22005-06-09
WO1995023221A11995-08-31
WO1992021760A11992-12-10
WO2007044993A22007-04-19
WO1989006279A11989-07-13
WO1992019729A11992-11-12
WO1996034946A11996-11-07
WO1998020115A11998-05-14
WO1998020116A11998-05-14
WO1999011768A11999-03-11
WO2001044452A12001-06-21
WO2003006602A22003-01-23
WO2004003186A22004-01-08
WO2004041979A22004-05-21
WO2007006305A12007-01-18
WO2011036263A12011-03-31
WO2011036264A12011-03-31
WO2016001449A12016-01-07
WO2004067737A22004-08-12
WO1992001046A11992-01-23
WO1997008325A21997-03-06
WO1995033836A11995-12-14
WO2015155351A12015-10-15
WO2011098579A12011-08-18
WO2014087011A12014-06-12
WO2017060475A22017-04-13
WO2009087523A22009-07-16
WO2007138054A12007-12-06
WO2006108856A22006-10-19
WO2006113314A12006-10-26
WO2003040279A12003-05-15
WO2013188331A12013-12-19
WO2013184577A12013-12-12
Foreign References:
US20170355930A12017-12-14
US20160319227A12016-11-03
EP2018057746W2018-03-27
US5977053A1999-11-02
EP0624154A11994-11-17
EP1867708A12007-12-19
EP1876226A12008-01-09
US4435307A1984-03-06
US5648263A1997-07-15
US5691178A1997-11-25
US5776757A1998-07-07
EP0495257A11992-07-22
EP0531372A11993-03-17
EP0531315A11993-03-17
US5457046A1995-10-10
US5686593A1997-11-11
US5763254A1998-06-09
EP0258068A21988-03-02
EP0305216A11989-03-01
EP0218272A11987-04-15
EP0331376A21989-09-06
US5389536A1995-02-14
EP0407225A11991-01-09
GB1296839A1972-11-22
US7262042B22007-08-28
EP1921147A22008-05-14
EP1921148A22008-05-14
US5352604A1994-10-04
EP0179486A21986-04-30
JPH02238885A1990-09-21
EP1867808A12007-12-19
EP2169040A12010-03-31
US20090011970A12009-01-08
Other References:
NEEDLEMANWUNSCH, J. MOL. BIOL., vol. 48, 1970, pages 443 - 453
RICE ET AL.: "EMBOSS: The European Molecular Biology Open Software Suite", TRENDS GENET., vol. 16, 2000, pages 276 - 277, XP004200114, doi:10.1016/S0168-9525(00)02024-2
FINN, NUCLEIC ACIDS RESEARCH, 2016, pages D279 - D285
EDGAR, NUCLEIC ACIDS RESEARCH, vol. 32, no. 5, 2004, pages 1792 - 1797
PRICE ET AL., PLOS ONE, vol. 5, no. 3, 2010
LETUNICBORK: "2007", BIOINFORMATICS, vol. 23, no. 1, pages 127 - 128
SIEZEN ET AL., PROTEIN ENGNG., vol. 4, 1991, pages 719 - 737
SIEZEN ET AL., PROTEIN SCIENCE, vol. 6, 1997, pages 501 - 523
"Powdered Detergents, Surfactant science series", vol. 71, MARCEL DEKKER, INC.
Download PDF:
Claims:
CLAIMS

1 . A cleaning composition comprising one or more anionic surfactants, and at least one polypeptide having RNase activity.

2. The cleaning composition according to claim 1 , wherein the composition further comprises one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes.

3. The cleaning composition according to any of claims 1 -2, wherein the composition comprises from 0.5 to about 80 wt % of the anionic surfactant.

4. The cleaning composition according to claim 3, wherein the anionic surfactant is selected from linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2, 3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) including methyl ester sulfonate (MES), alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfo-succinic acid or salt of fatty acids (soap), and combinations thereof.

5. The cleaning composition according to any of the preceding claims, wherein the composition further comprises a non-ionic surfactant.

6. The cleaning composition according to claim 5, wherein the nonionic surfactant is selected from alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA) and combinations thereof.

7. The cleaning composition according to any of claims 5-6, wherein the weight ratio of anionic to non-ionic surfactant is from 10:1 to 1 :5.

8. The cleaning composition according to any of the preceding claims, wherein the composition further comprises from 0.5 to 65% by weight of a builder and/or a co-builder.

9. The cleaning composition according to any of the preceding claims, wherein the concentration of the polypeptide having RNase activity is 0.0002 wt% to 5 wt%.

10. A method of cleaning an item comprising the steps of:

(a) Exposing the item to water;

(b) Optionally remove excess of water;

(c) Exposing the item to a wash liquor comprising the cleaning composition of any of claims 1 -9 or at least one polypeptide having RNase activity;

(d) Completing at least one wash cycle; and

(e) Optionally rinsing the item;

wherein the item is a textile, a dish ware or a hard surface.

1 1 . The method according to claim 10, wherein the pH of the wash liquor is in the range 5.5 to 1 1 .

12. The method according to any of claims 10-1 1 , wherein the temperature of the wash liquor is in the range of 5°C to 95°C.

13. The method according to any of claims 10-12, wherein the concentration of the polypeptide having RNase activity in the wash liquor is in the range 0.0002 mg/L to 5 mg/L.

14. A method according to any of claims 10-13, wherein the item is exposed to water, and the excess of water is removed by dripping, wringing and/or centrifuging.

15. Use of a cleaning composition according to any of claims 1 -9 for cleaning an item by:

(a) preventing, reducing or removing stickiness of the item;

(b) preventing, reducing or removing RNA or RNA components from the item; (c) preventing, reducing or removing redeposition of soil during cleaning of the item;

(d) preventing, reducing or removing adherence of soil to the item;

(e) maintaining or improving whiteness of the item; or

(f) preventing, reducing or removing malodor from the item;

wherein the item is a textile, a hard surface or a dish ware.

16. Use according to claim 15, wherein the measured effect ratio of test panellists preferring fabrics washed with RNase vs test panellists preferring fabrics washed without RNase is at least 60:40, preferably at least 70:30, preferably at least 80:20 or preferably at least 90:10, when measured as described in Example 16.

17. Use according to claim 15, wherein the cleaning effect e.g. deep cleaning effect ratio of test panellists preferring fabrics washed with RNase vs test panellists preferring fabrics washed without RNase is at least 60:40, preferably at least 70:30, preferably at least 80:20 or preferably at least 90:10, when measured as described in Example 16.

Description:
CLEANING COMPOSITION COMPRISING ANIONIC SURFACTANT

AND A POLYPEPTIDE HAVING RNASE ACTIVITY

Reference to a Sequence Listing

This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference.

BACKGROUND OF THE INVENTION Field of the Invention

The present invention relates to cleaning compositions comprising at least one polypeptide having RNase activity, a method for cleaning an item and use of the cleaning composition according to the invention.

Description of the Related Art

Cleaning of different item can be a challenge, even though cleaning compositions specifically adapted for cleaning of laundry item, hard surfaces and dish ware are on the marked. Many of the commercially available cleaning compositions do not clean the items sufficiently, and some or all items do not appear clean, visually or sensorial.

Consumers experiencing for example that a white shirt that has become grey before being worn out may decide to discharge the shirt.

Many cleaning compositions contain enzymes that facilitate the removal of soil and cleaning of the item, e.g. proteases facilitating removal of protein soil. The item can become soiled with many different types of soiling, e.g. complex food stains. Another source of complex soil is body soil that adheres to the clothes, which soil will typically comprise bacteria and which may result in development of malodor.

Biofilm is an example of soiling and which may build up on items after being used, e.g. by body soil attaching to clothes. This may provide several disadvantages. Biofilm comprises an extracellular polymeric matrix, composed of e.g. polysaccharides, RNA, extracellular DNA and RNA (exDNA, exRNA), and proteins. The extracellular polymeric matrix may be sticky or gluing, which when present on an item, give rise to redeposition or backstaining of soil resulting in a greying of the item.

Another drawback is that malodor may be trapped within the organic structure or malodor may even develop from bacteria present in the biofilm. Biofilm is therefore not desirable on any items: laundry item, hard surfaces and dish ware or on surfaces associated with cleaning, such as the interior of washing machines, dishwashing machines etc. Further, the soil removed from the items during wash or originating from the washing or dishwashing machine, can redeposit on the items. As a result, hereof, some items may be more“soiled” after wash than before wash. One example is a new white T-shirt, which is washed with other laundry items, and become greyish after first wash, or a plate being more or differently soiled after wash.

WO 2006/031554 (Novozymes) describes methods for preventing, removing, reducing or disrupting biofilm on a surface. The methods disclosed use alpha-amylases, and no specific RNase and no effect of the use of RNase is disclosed.

As biofilm is a complex mixture of polysaccharides, proteins, RNA, DNA etc. Enzymes can facilitate removal of biofilm are already available. However, there is a need for cleaning compositions, which effectively remove or reduce components of organic soiling e.g. biofilm in cleaning processes such as laundry, dish wash and hard surface cleaning. The object of the present invention is to provide cleaning compositions, which effectively reduce or remove biofilm.

SUMMARY OF THE INVENTION

The present invention pertains to a cleaning composition comprising one or more anionic surfactants, and at least one polypeptide having RNase activity. The invention further relates to a method of cleaning an item comprising the steps of:

(a) Exposing the item to water;

(b) Optionally remove excess of water;

(c) Exposing the item to a wash liquor comprising the cleaning composition of the invention or at least one polypeptide having RNase activity;

(d) Completing at least one wash cycle; and

(e) Optionally rinsing the item;

wherein the item is a textile, a dish ware or a hard surface.

The invention further concerns the use of a cleaning composition according to the invention for for cleaning an item by:

(a) preventing, reducing or removing stickiness of the item;

(b) preventing, reducing or removing RNA or RNA components from the item;

(c) preventing, reducing or removing redeposition of soil during cleaning of the item;

(d) preventing, reducing or removing adherence of soil to the item;

(e) maintaining or improving whiteness of the item; or

(f) preventing, reducing or removing malodor from the item;

wherein the item is a textile, a hard surface or a dish ware.

Overview of sequences

SEQ ID NO 1 mature polypeptide obtained from Paenibacillus sp-18057

SEQ ID NO 2 mature polypeptide obtained from Paenibacillus sp-62770

SEQ ID NO 3 mature polypeptide obtained from Amycolatopsis azurea SEQ ID NO 4 mature polypeptide obtained from Environmental sample community E

SEQ ID NO 5 mature polypeptide obtained from Acremonium alcalophilum

SEQ ID NO 6 is the mature polypeptide obtained from Stenotrophomonas rhizophila.

SEQ ID NO 7 is the mature polypeptide obtained from Erwinia persicina.

SEQ ID NO 8 is the mature polypeptide obtained from Paenibacillus tundrae.

SEQ ID NO 9 is the mature polypeptide obtained from Saccharothrix sp-62935.

SEQ ID NO 10 s the mature polypeptide obtained from Saccharopolyspora endophytica. SEQ ID NO 1 1 s the mature polypeptide obtained from Amycolatopsis circi.

SEQ ID NO 12 s the mature polypeptide obtained from Paenibacillus sp-62770

SEQ ID NO 13 s the mature polypeptide obtained from Paenibacillus sp-18006.

SEQ ID NO 14 s the mature polypeptide obtained from Paenibacillus sp-62724.

SEQ ID NO 15 s the mature polypeptide obtained from Alkalimonas sp-62516.

SEQ ID NO 16 s the mature polypeptide obtained from Nonomuraea dietziae.

SEQ ID NO 17 s the mature polypeptide derived from Trichoderma harzianum.

SEQ ID NO 18 s the mature polypeptide derived from Fusarium solani.

SEQ ID NO 19 RNase from Streptomyces aureofaciens (public sequence SWISSPROT:P30289)

SEQ ID NO 20 RNase from Gibberella fujikuroi (public sequence SWISSPROT:A7M7A2)

SEQ ID NO 21 EYTV motif

SEQ ID NO 22 [YRF]E[AYFWC]D motif

SEQ ID NO 23 IGGD motif

SEQ ID NO 24 YPH motif

SEQ ID NO 25 HTGA motif

SEQ ID NO 26 DRV motif

SEQ ID NO 27 Bacillus amyloliquefaciens ribonuclease Barnase

SEQ ID NO 28 YXEYTVXTPXXXXRGXRR motif

SEQ ID NO 29 [WY][YRF]E[AYFWC]D[IV] motif

SEQ ID NO 30 GXXIGGDXFXN motif

SEQ ID NO 31 YPHX[YFA]X[ND]XE motif

SEQ ID NO 32 PGXDRV motif

SEQ ID NO 33 THTGA[SR]G motif

SEQ ID NO 34 is the mature polypeptide derived from Bacillus mojavensis

SEQ ID NO 35 is the mature polypeptide derived from Bacillus subtilis Definitions

The term“RNase” is an abbreviation of the term ribonuclease, which means a nuclease or a polypeptide having RNase activity (EC 3.1 .2.7) that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases; the present invention relates to e.g. endoribonucleases. For purposes of the present invention, RNase activity is determined according to the procedure in Assay I. In one aspect, the polypeptides of the present invention have at least 20%, e.g., at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or at least 100% of the RNase activity of the any of the mature polypeptides shown in SEQ ID NOs: 1 , 2, 3, 4,5, 6, 7, 8, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19, 20, 27, 34 or 35.

The term“biofilm” means a film produced by any group of microorganisms in which cells stick to each other or stick to a surface, such as a textile, dishware or hard surface or another kind of surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS). Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins, and polysaccharides. Biofilms may form on living or non-living surfaces. The microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single-cells that may float or swim in a liquid medium. Bacteria living in a biofilm usually have significantly different properties from planktonic bacteria of the same species, as the dense and protected environment of the film allows them to cooperate and interact in various ways. One benefit of this environment for the microorganisms is increased resistance to detergents and antibiotics, as the dense extracellular matrix and the outer layer of cells protect the interior of the community. On laundry biofilm producing bacteria can be found among species including Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, and Stenotrophomonas sp. On hard surfaces biofilm producing bacteria can be found among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, Staphylococcus aureus and Stenotrophomonas sp.

The term “deep cleaning” means in this context disruption, reduction or removal of organic components such as polysaccharides, proteins, RNA, DNA, soil or other components present in organic matter e.g. biofilm.

Cleaning component: The cleaning component e.g. a detergent ingredient is different to the polypeptides of this invention. The precise nature of these additional cleaning components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the operation for which it is to be used. Suitable cleaning components include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric huing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.

Cleaning Composition: The term cleaning composition includes“detergent composition” and refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles, dish ware and hard surfaces. The detergent composition may be used to e.g. clean textiles for both household cleaning and industrial cleaning. The terms encompass any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre-spotters/pretreatment).

In addition to containing the RNase of the invention, the cleaning composition may contain one or more additional enzymes (such as DNases, proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidaes, haloperoxygenases, catalases, galactanase, mannanases, or any mixture thereof), and/or cleaning components such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.

Dishware: The term dish ware is intended to mean any form of kitchen utensil, dinner set, tableware or crockery made of any kind of suitable material. Dish ware includes, but is not limited to plates, cups, glasses, bowls, all forms of cutlery such as spoons, knives, forks and serving utensils, cooking utensils and the like. They can be made of any kind of suitable material such as ceramics, plastics, metals, china, glass and acrylics.

Dish wash: The term "dish wash" refers to all forms of washing dishes, e.g. by hand (MDW) or automatic dish wash (ADW).

Enzyme Detergency benefit: The term“enzyme detergency benefit” is defined herein as the advantageous effect an enzyme may add to a detergent compared to the same detergent without the enzyme. Important detergency benefits which can be provided by enzymes are stain removal with no or very little visible soils after washing and/or cleaning, prevention or reduction of redeposition of soils released in the washing process (an effect that also is termed anti- redeposition), restoring fully or partly the whiteness of textiles which originally were white but after repeated use and wash have obtained a greyish or yellowish appearance (an effect that also is termed whitening). Textile care benefits, which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits. Examples of such textile care benefits are prevention or reduction of dye transfer from one fabric to another fabric or another part of the same fabric (an effect that is also termed dye transfer inhibition or anti-backstaining), removal of protruding or broken fibers from a fabric surface to decrease pilling tendencies or remove already existing pills or fuzz (an effect that also is termed anti-pilling), improvement of the fabric-softness, colour clarification of the fabric and removal of particulate soils which are trapped in the fibers of the fabric or garment. Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides.

Hard surface cleaning: The term "Hard surface cleaning" is defined herein as cleaning of hard surfaces wherein hard surfaces may include floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dish wash).

HQ-tag: A“His-tag” refers to a polyhistidine tag typically comprising at least 6 histidine residues, that may be added to the N- or C-terminal. His-tags are known in the art for use in e.g. protein purification but may also be used for improving solubility at low pH values. Similarly, an “HQ-tag”, i.e. a histidine-glutamine tag, may also be used for the purpose of purification as is known in the art.

Improved wash performance: The term“improved wash performance” is defined herein as an enzyme displaying an increased wash performance in a detergent composition relative to the wash performance of same detergent composition without the enzyme e.g. by increased stain removal or less re-deposition. The term “improved wash performance” includes wash performance in laundry, hard surface and dish washing.

The term“laundering” relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention. The laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand.

By the term’’malodor” is meant an odor which is not desired on clean items. The cleaned item should smell fresh and clean without malodors adhered to the item. One example of malodor is compounds with an unpleasant smell which may be produced by microorganisms and trapped within a biofilm or stick to the“glue” of a biofilm. Other examples of unpleasant smells are sweat or body odor adhered to an item which has been in contact with a human or animal. Other examples of malodor are odors from spices which stick to items, for example curry or other exotic spices with a strong smell. The term“mature polypeptide” means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc.

Nomenclature: For purposes of the present invention, the nomenclature [E/Q] or [EQ] means that the amino acid at this position may be a glutamic acid (Glu, E) or a glutamine (Gin, Q). Likewise, the nomenclature [V/G/A/l] or [VGAI] means that the amino acid at this position may be a valine (Val, V), glycine (Gly, G), alanine (Ala, A) or isoleucine (lie, I), and so forth for other combinations as described herein. Unless otherwise limited further, the amino acid X is defined such that it may be any of the 20 natural amino acids.

Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter“sequence identity”.

For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 5.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled“longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:

(Identical Residues x 100)/(Length of Alignment - Total Number of Gaps in Alignment)

The term“variant” means a polypeptide having RNase activity comprising an alteration, / ' .e., a substitution, insertion, and/or deletion, at one or more (e.g., several) positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.

Textile: The term "textile" means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles). The textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and towelling. The textile may be cellulose based such as natural cellulosics, including cotton, flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g. originating from wood pulp) including viscose/rayon, cellulose acetate fibers (tricell), lyocell or blends thereof. The textile or fabric may also be non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non-cellulose based fibers. Examples of blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fiber (e.g. polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber), and/or cellulose-containing fiber (e.g. rayon/viscose, ramie, flax/linen, jute, cellulose acetate fiber, lyocell). Fabric may be conventional washable laundry, for example stained household laundry. When the term fabric or garment is used it is intended to include the broader term textiles as well.

Wash cycle: The term“wash cycle” is defined herein as a washing operation wherein one or more items are exposed to a wash liquor, and the items and wash liquor are subjected to interaction e.g. by applying is mechanical action of some kind to the wash liquor and/or to the item, or by spraying the washing liquor on to the items, in order to release stains and to facilitate flow of wash liquor in or around the items, and finally the superfluous wash liquor is removed. After one or more wash cycles, the items are generally rinsed and dried.

Wash liquor: The term“wash liquor” is defined herein as the solution or mixture of water and a cleaning composition.

DETAILED DESCRIPTION OF THE INVENTION

The present invention relates to cleaning composition comprising one or more anionic surfactants and a polypeptides having RNase activity, i.e. RNases.

The advantage of the present cleaning composition is that it is useful in cleaning items such as textiles, which may comprise body soiling such as cell debris, dead cells, sebum, sweat and other organic staining.

The polypeptide having RNase activity is useful in cleaning surfaces comprising RNA stains and when provided in a cleaning composition together with one or more anionic surfactants, the cleaning effect is even better, as the surfactant facilitates the polypeptides access to the stain. Actually, the cleaning composition of the invention does not only clean the surface of a soiled item. The cleaning composition is effective in deep cleaning of surfaces, e.g. textiles.

Organic stains such as cell debris, sebum and biofilm may be sticky or gluing and may attract soil components to stick to the biofilm. Thus, an item soiled with organic stains may look grey or dirty, as different kinds of soil stick to the stains e.g. stains related to body soil or biofilm. The cleaning composition of the present invention is effective in preventing, removing or reducing the stickiness of an item and is also effective in removing or reducing the greying of the item and maintaining or improving the whiteness of the item.

During wash, dead cells or other body soiling may be released or removed from the item and can redeposit on same or other items, which may result in greying of the item. One example is laundering of a new white t-shirt together with clothes that have been worn and washed several times. The stains from the worn clothes may stick to the new t-shirt and result in greying of the t-shirt. The cleaning composition of the present invention is effective in preventing, reducing or removing redeposition of soil to an item.

Another drawback is that body soiling is that it often causes malodor. The cleaning composition of the invention is therefore useful for prevention, reduction or removal of malodor. Such unsatisfactory cleaning result may result in the consumer buying a new item instead of the cleaned item. This has huge impact on the environment and the cleaning composition of the invention may thus help protecting our environment by causing less damage to the environment, e.g. by reducing waste.

The cleaning composition of the invention may further comprise one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes. The cleaning compositions of the invention show improved wash performance. The cleaning composition components are described in more details in the below paragraphs, e.g. paragraphs“builders and Co-builders”,“bleaching systems” etc.

The cleaning composition of the invention comprises from 0.5 to about 80 wt % of anionic surfactant. The presence of one or more anionic surfactants in the cleaning composition ensures an effective cleaning of items soiled with organic stains e.g. body soils.

In one embodiment of the invention the cleaning composition comprises from about 1 wt % to about 60 wt %, such as from about 5 wt % to about 50 wt %, from about 5 wt % to about 40 wt %, from about 5 wt % to about 30 wt %, from about 5 wt % to about 20 wt %, from about 5 wt % to about 10 wt % of the anionic surfactant.

The anionic surfactant contributes to the release of the stains by easing access of the polypeptide having RNase activity to the surface of the textile and to the soiling. The anionic surfactants, which can be used in the inventive cleaning composition, are described in the paragraph “surfactants” below. However in one preferred embodiment of the invention the anionic surfactant is selected from the group consisting of linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha- olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2, 3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) including methyl ester sulfonate (MES), alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfo- succinic acid or salt of fatty acids (soap), and combinations thereof.

In one embodiment of the invention the cleaning composition comprises

(a) at least one polypeptide having RNase activity; (b) from 0.5 % to 15 % by weight of a linear alkylbenzenesulfonate and optionally further anionic surfactants; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes.

In one embodiment of the invention the cleaning composition comprises

(a) at least one polypeptide having RNase activity;

(b) from 5 % to 15 % by weight of a linear alkylbenzenesulfonate and optionally further anionic surfactants; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes.

In one embodiment of the invention the cleaning composition comprises

(a) at least one polypeptide having RNase activity;

(b) from 5 % to 10 % by weight of a linear alkylbenzenesulfonate and optionally further anionic surfactants; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes.

The cleaning composition may further comprise a non-ionic surfactant. The choice of non-ionic surfactant is described in the paragraph“surfactants” below, however in one preferred embodiment of the invention the cleaning composition comprises a nonionic surfactant selected from the group consisting of alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N- acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA) and combinations thereof.

When the cleaning composition comprises one or more anionic surfactants and one or more non-ionic surfactants, the amounts of the anionic surfactants relative to amount of non- ionic surfactants is important. In one embodiment the weight ratio of anionic to non-ionic surfactant is from 10:1 to 1 :5. In a preferred embodiment of the invention the weight ratio of anionic to non-ionic surfactant is from 7:1 to 1 :4, or more preferred from 6:1 to 1 :3, or even more preferred from 5:1 to 1 :2.5 orfrom 4:1 to 1 :2.2. The most preferred weight ratio of anionic to non- ionic surfactant is from 3:1 to 1 :2 or from 2:1 to 1 :1. The cleaning composition may further comprise a builder. The builder softens the water and thereby contributes to the cleaning of the item to be cleaned. In one embodiment of the invention the cleaning composition comprises from 0.5 to 65% by weight of a builder and/or a co-builder, such as from 5 to 50% by weight or from 40 to 65% by weight or from 50 to 65% by weight. The cleaning composition can comprise the builder described below in the paragraph “builders and co-builders”. In a preferred embodiment of the invention the builder is selected from the group consisting of zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates, ethanolamines such as 2-aminoethan-1 -ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1 -ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1 -ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

In one embodiment of the invention the cleaning composition further comprises a co- builder, which can be selected from the group consisting of homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA PMA), citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid, 2,2’,2”-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N’-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1 -hydroxyethane-1 ,1 -diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis(methylenephosphonic acid) (DTMPA or DTPMPA), N-(2- hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid- N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)-aspartic acid (SMAS), N-(2-sulfoethyl)-aspartic acid (SEAS), N-(2- sulfomethyl)-glutamic acid (SMGL), N-(2-sulfoethyl)-glutamic acid (SEGL), N- methyliminodiacetic acid (MIDA), oalanine-N,N-diacetic acid (a-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA) , taurine-N,N- diacetic acid (TUDA) and sulfomethyl-N,N-diacetic acid (SMDA), N-(2- hydroxyethyl)ethylenediamine-N,N’,N”-triacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof.

In a particularly preferred embodiment of the invention the cleaning composition comprises a builder selected from the group consisting of sodium alumino silicate, soluble silicates such as sodium metasilicate, layered silicates, citric acid, methylglycine-N,N-diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA) and mixtures thereof. The silicate builders can comprise sodium alumino silicate, which in one embodiment of the invention may be present in an amount of 0.01 to 1 % by weight. In a preferred embodiment of the invention the cleaning composition comprises sodium alumino silicate in an amount of 0.01 to 1 % by weight and at least 80% by weight alkyl benzene sulphonate surfactant, preferably at least 85 % by weight linear alkyl benzene sulphonate (LAS). In one embodiment of the invention such cleaning composition can be used for pre-treatment of very soiled item, e.g. by applying the composition directly on the soiled textile.

An even better cleaning can be achieved when the cleaning composition of the invention further comprise one or more enzymes. In one embodiment of the invention the one or more enzymes selected from the group consisting of DNases, proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidaes, haloperoxygenases, catalases, galactanase, mannanases, or any mixture thereof. The enzymes are described in further details in the below paragraph on enzymes.

The cleaning composition of the invention can be formulated as described in the paragraph“formulation of detergent products” below. In a preferred embodiment of the invention the cleaning composition is in the form of a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, a regular liquid, a compact liquid or concentrated liquid. In a more preferred embodiment the cleaning composition is in the form of a regular or compact powder. In another more preferred embodiment the cleaning composition is in the form of a regular liquid, a compact liquid or concentrated liquid.

When the cleaning composition is formulated as a liquid detergent composition, it may be advantageous to encapsulate the enzymes present in the composition in a microcapsule.

In one embodiment of the invention the liquid detergent composition comprises an anionic surfactant and a detergent builder in a total concentration of at least 3% by weight, and a microcapsule containing a polypeptide having RNase activity, wherein the membrane of the microcapsule is produced by cross-linking of a polybranched polyamine having a molecular weight of more than 1 kDa. The encapsulation of the polypeptide having RNase activity can be done as describe in WO2015/155350 on pages 15-20. The encapsulation of the enzyme has the advantage that the enzyme will be separated for incompatible components in the cleaning composition.

The cleaning composition of the invention comprises polypeptides having RNase activity. In one embodiment of the invention the polypeptides having RNase activity comprise a domain from the RNase Barnase (Swiss Prot P00648 (SEQ ID NO 27)), PF00545 family) as well as the clusters such as the clades. A clade is a grouping that has a shared phylogeny and includes a common ancestor and all the descendants (living and extinct) of that ancestor (http://evolution.berkeley.edu/evolibrary/article/0_0_0/evo_ 06). Thus, in the present context a clade refers to a subgroup of closely related RNases. The polypeptides are further described in international patent application number PCT/EP2018/057746 (Novozymes A/S), which is hereby incorporated by reference.

A phylogenetic tree was constructed of polypeptide sequences containing a Barnase domain, as defined in PFAM (PF000545, Pfam version 30.0 Finn (2016). Nucleic Acids Research, Database Issue 44 D279-D285). The phylogenetic tree was constructed from a multiple alignment of mature polypeptide sequences containing at least one Barnase domain. The sequences were aligned using the MUSCLE algorithm version 3.8.31 (Edgar, 2004. Nucleic Acids Research 32(5): 1792-1797), and the trees were constructed using FastTree version 2.1 .8 (Price et al., 2010, PloS one 5(3)) and visualized using iTOL (Letunic & Bork, 2007. Bioinformatics 23(1 ): 127-128). The polypeptides comprising the Barnase domain can be separated into multiple distinct sub-clusters, or clades, where we denoted the clades listed below. Distinct motifs for each clade are described in Example 10 of international patent application number PCT/EP2018/057746 (published as WO2018/178061 ). Examples 1 -5 of PCT/EP2018/057746 describes one way of producing the polypeptides having RNA activity.

In one embodiment of the invention the RNases of the invention belong to a specific subgroup or clade comprising one or more motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), YPH (SEQ ID NO: 24), HTGA (SEQ ID NO: 25) or DRV (SEQ ID NO:26).

In one aspect, the polypeptide of the invention having RNase activity belongs to the EYTV clade and comprises the motif EYTV (SEQ ID NO: 21 ). In one embodiment of this aspect, the polypeptide comprises the extended motif YXEYTVXTPXXXXRGXRR (SEQ ID NO: 28), wherein each X independently may be any naturally occurring amino acid.

In one aspect, the polypeptide of the invention having RNase activity belongs to the EAD clade and comprises one or more of the motif(s) [YRF]E[AYFWC]D (SEQ ID NO: 22) or IGGD (SEQ ID NO: 23). In one embodiment of this aspect, the polypeptide comprises the extended motif [WY][YRF]E[AYFWC]D[IV] (SEQ ID NO: 29). In another embodiment, the polypeptide comprises the extended motif GXXIGGDXFXN (SEQ ID NO: 30), wherein each X independently may be any naturally occurring amino acid.

In one aspect, the polypeptide of the invention having RNase activity belongs to the YPH clade and comprises one or more of the motif(s) YPH (SEQ ID NO: 24), HTGA (SEQ ID NO: 25) or DRV (SEQ ID NO:26). In one embodiment of this aspect, the polypeptide comprises the extended motif YPHX[YFA]X[ND]XE (SEQ ID NO: 31 ), wherein each X independently may be any naturally occurring amino acid. In another embodiment, the polypeptide comprises the extended motif PGXDRV (SEQ ID NO: 32), wherein X may be any naturally occurring amino acid. In another embodiment, the polypeptide comprises the extended motif THTGA[SR]G (SEQ ID NO: 33).

In one embodiment of the invention the cleaning composition according to any of the preceding claims, wherein the polypeptide having RNase activity, preferably is a polypeptide of the clades EYTV, EAD or YPH, selected from the group consisting of:

(a) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97% at least 98% 100% sequence identity to the polypeptide of SEQ ID NO: 1 ;

(b) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 2;

(c) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 3;

(d) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 4;

(e) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 5;

(f) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 6;

(g) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 7;

(h) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 8;

(i) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 9;

(j) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 10; (k) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 1 1 ;

(L) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 12;

(m)a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 13;

(n) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 14;

(o) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 15;

(p) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 16;

(q) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 17;

(r) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 18;

(s) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 19;

(t) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 20;

(u) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 27;

(v) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 34; (w) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 35;

(x) a variant of the polypeptide selected from the group consisting of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 27, SEQ ID NO: 34 and SEQ ID NO: 35, wherein the variant has RNase activity and comprises one or more amino acid substitutions, and/or one or more amino acid deletions, and/or one or more amino acid insertions or any combination thereof in 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19 or 20 positions;

(y) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal His-tag and/or HQ-tag;

(z) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal extension of between 1 and 10 amino acids;

(aa) a fragment of the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) having RNase activity and having at least 90% of the length of the mature polypeptide;

(bb) a polypeptide comprising one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), YPH (SEQ ID NO: 24), HTGA (SEQ ID NO: 25) or DRV (SEQ ID NO:26); and

(cc) a polypeptide comprising one or more of the motifs YXEYTVXTPXXXXRGXRR (SEQ ID NO: 28), [WY][YRF]E[AYFWC]D[IV] (SEQ ID NO: 29), GXXIGGDXFXN (SEQ ID NO: 30), YPHX[YFA]X[ND]XE (SEQ ID NO: 31 ), PGXDRV (SEQ ID NO: 32) or THTGA[SR]G (SEQ ID NO: 33).

The concentration of the polypeptide having RNase activity in cleaning composition should be at least 0.0002 wt%. In one embodiment of the invention the concentration of the polypeptide having RNase activity is at least 0.002 wt% or at least 0.02 wt% of a polypeptide having RNase activity, wherein the polypeptide is selected from the group consisting of: SEQ ID NO 1 , SEQ ID NO 2, SEQ ID NO 3, SEQ ID NO 4, SEQ ID NO 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ I D NO: 1 1 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17 , SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO 27, SEQ ID NO: 34 and SEQ ID NO: 35 and polypeptides having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity hereto.

The cleaning composition can be used for for cleaning an item by:

(a) preventing, reducing or removing stickiness of the item;

(b) preventing, reducing or removing RNA or RNA components from the item;

(c) preventing, reducing or removing redeposition of soil during cleaning of the item;

(d) preventing, reducing or removing adherence of soil to the item;

(e) maintaining or improving whiteness of the item; or

(f) preventing, reducing or removing malodor from the item;

wherein the item is a textile, a hard surface or a dish ware.

One embodiment relates to the use e.g. any of those indicated above in (a)-(f), wherein measured effect ratio of test panellists preferring fabrics washed with RNase vs test panellists preferring fabrics washed without RNase is at least 60:40, preferably at least 70:30, preferably at least 80:20 or preferably at least 90:10, when measured as described in Example 2.

One embodiment relates to the use according to the invention, wherein the cleaning effect e.g. deep cleaning effect ratio of test panellists preferring fabrics washed with RNase vs test panellists preferring fabrics washed without RNase is at least 60:40, preferably at least 70:30, preferably at least 80:20 or preferably at least 90:10, when measured as described in Example 2.

The cleaning composition according to the invention may have a concentration of the polypeptide having RNase activity in the range of is in the range 0.0002 wt% to 5 wt%, such as in the range of 0.002 wt% to 5 wt%, in the range of 0.002 wt% to 5 wt%, in the range of 0.02 wt% to 2 wt%, in the range of 0.2 wt% to 2 wt% of the total detergent composition.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing stickiness of the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and (c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing RNA or RNA components on the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing redeposition of soil on an item during the wash cycle.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing adherence of soil to the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for maintaining or improving whiteness of the item to be cleaned. In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) optionally one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing malodor from the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) one or more builders;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing stickiness of the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) one or more builders;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing RNA or RNA components on the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) one or more builders;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing redeposition of soil on an item during the wash cycle.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and (c) one or more builders;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing adherence of soil to the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) one or more builders;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for maintaining or improving whiteness of the item to be cleaned.

In one embodiment of the invention the cleaning composition of the invention comprises

(a) one or more anionic surfactants in concentration from 0.5 to about 80 wt %;

(b) a polypeptide having RNase activity; and

(c) one or more builders;

wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25) and can be used for preventing, reducing or removing malodor from the item to be cleaned.

In one aspect the invention pertains to a method of cleaning an item comprising the steps of:

(a) Exposing the item to water;

(b) Optionally remove excess of water;

(c) Exposing the item to a wash liquor comprising the cleaning composition of the invention or at least one polypeptide having RNase activity;

(d) Completing at least one wash cycle; and

(e) Optionally rinsing the item;

wherein the item is a textile, a dish ware or a hard surface.

When the item is exposed to water before being exposed to the wash liquor, the item is already wet, and this allows the active components of the wash liquor, e.g. the polypeptide having RNase activity to be exposed to item at a faster rate.

In one embodiment of the invention the cleaning method is a laundry method and the item is a textile, which textile is a hydrophobically-modified textile. The textile may be selected from textiles comprising cotton, polyester, polyamide, polyacryl, silk and mixtures thereof. In one embodiment of the invention the textile is cotton. In one embodiment of the invention the textile is polyester. In one embodiment of the invention the textile is a cotton/polyester mix.

The hydrophobically-modified textile is a textile having thereon a finishing treatment which provides an increase in the hydrophobicity of the textile surface relative to the untreated textile surface. The hydrophobicity increase can be determined by measuring the water contact angle of the textile surface. How to measure the water contact angle and how to provide textiles that are hydrophobically-modified are described in international patent application published under number WO2016/176280 (The Procter & Gamble company), see page 4, line 6 to page 6, line 24.

In one embodiment of the invention the cleaning method is a method for cleaning dish ware, such as automated dish washing (ADW) or dish washing by hand. In another embodiment of the invention the cleaning method cleans hard surfaces, such as floors, walls, or equipment in domestic or industrial kitchens, hospitals or other institutions.

The pH of the wash liquor should be in the range 5.5 to 1 1 , such as in the range of 7 to 9, in the range of 7 to 8 or in the range of 7 to 8.5. The temperature of the wash liquor should be in the range of 5°C to 95°C, or in the range of 10°C to 80°C, in the range of 10°C to 70°C, in the range of 10°C to 60°C, in the range of 10°C to 50°C, in the range of 15°C to 40°C, in the range of 20°C to 40°C, in the range of 15°C to 30°C or in the range of 20°C to 30°C. In one preferred embodiment the temperature of the wash liquor is from about 20°C to about 40°C, such as from about 15°C to about 30°C. The pH and temperature of the wash liquor ensures that the enzymes have optimal conditions and at the same time will be safe to use and friendly to the environment.

In one embodiment of the invention the concentration of the cleaning composition should be such that the concentration of the polypeptide having RNase activity in the wash liquor 0.0002 mg/L to 5 mg/L, such as in the range of 0.002 mg/L to 5 mg/L, in the range of 0.02 mg/L to 2 mg/L, in the range of 0.2 mg/L to 2 mg/L.

In one embodiment of the invention the item is exposed to water and the excess of water is removed before being exposed to the wash liquor. This has the advantage that wash liquor is not diluted with water, when the item is exposed to the wash liquor. One example is a textile that is exposed to water, the excess of water is removed, e.g. by centrifuging, and the textile is then exposed to the wash liquor. Another example is a dish ware being exposed to water, the excess of water is removed by dripping and the dish ware is then exposed to the wash liquor.

In one embodiment of the invention the item is exposed to water and the excess of water is removed by dripping, wringing and/or centrifuging.

In one embodiment, the invention pertains to a method, wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25). In one embodiment, the invention concerns a method, wherein the polypeptide having RNase activity is, preferably a polypeptide of the clades EYTV, EAD or YPH, selected from the group consisting of:

(a) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 1 ;

(b) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 2;

(c) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 3;

(d) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 4;

(e) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 5;

(f) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 6;

(g) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 7;

(h) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 8;

(i) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 9;

(j) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 10;

(k) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 1 1 ; (L) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 12;

(m)a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 13;

(n) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 14;

(o) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 15;

(p) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 16;

(q) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 17;

(r) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 18;

(s) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 19;

(t) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 20;

(u) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 27;

(v) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 34;

(w) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 35; (x) a variant of the polypeptide selected from the group consisting of SEQ ID NO: 31 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 27, SEQ ID NO: 34 and SEQ ID NO: 35, wherein the variant has RNase activity and comprises one or more amino acid substitutions, and/or one or more amino acid deletions, and/or one or more amino acid insertions or any combination thereof in 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19 or 20 positions;

(y) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal His-tag and/or HQ-tag;

(z) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal extension of between 1 and 10 amino acids;

(aa) a fragment of the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) having RNase activity and having at least 90% of the length of the mature polypeptide;

(bb) a polypeptide comprising one or more of the motif(s) EYTV (SEQ ID NO:

21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), YPH (SEQ ID NO: 24), HTGA (SEQ ID NO: 25) or DRV (SEQ ID NO:26); and

(cc) a polypeptide comprising one or more of the motifs YXEYTVXTPXXXXRGXRR (SEQ ID NO: 28), [WY][YRF]E[AYFWC]D[IV] (SEQ ID NO: 29), GXXIGGDXFXN (SEQ ID NO: 30), YPHX[YFA]X[ND]XE (SEQ ID NO: 31 ), PGXDRV (SEQ ID NO: 32) or THTGA[SR]G (SEQ ID NO: 33).

The cleaning method of the invention has the following advantages, as it comprises cleaning an item by:

(a) preventing, reducing or removing stickiness of the item;

(b) preventing, reducing or removing RNA or RNA components from the item;

(c) preventing, reducing or removing redeposition of soil during cleaning of the item;

(d) preventing, reducing or removing adherence of soil to the item;

(e) maintaining or improving whiteness of the item; or

(f) preventing, reducing or removing malodor from the item;

wherein the item is a textile, a hard surface or a dish ware.

The choice of cleaning components may include, for textile care, the consideration of the type of textile to be cleaned, the type and/or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product. Although components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan.

Surfactants

The cleaning or the detergent composition may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof. In a particular embodiment, the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants. The surfactant(s) is typically present at a level of from about 0.1 % to 60% by weight, such as about 1 % to about 40%, or about 3% to about 20%, or about 3% to about 10%. The surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art.

When included therein the detergent will usually contain from about 1 % to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2, 3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) including methyl ester sulfonate (MES), alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfo-succinic acid or salt of fatty acids (soap), and combinations thereof.

When included therein the detergent will usually contain from about 1 % to about 40% by weigh of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%. Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.

When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%. Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN® and TWEEN®, and combinations thereof.

When included therein the detergent will usually contain from about 0.1 % to about 10% by weight of a semipolar surfactant. Non-limiting examples of semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N-(coco alkyl)-N,N-dimethylamine oxide and N- (tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, , and combinations thereof.

When included therein the detergent will usually contain from about 0.1% to about 10% by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.

Builders and Co-Builders

The cleaning or the detergent composition may contain about 0-65% by weight, such as about 5% to about 50% of a detergent builder or co-builder, or a mixture thereof. In a dish wash detergent, the level of builder is typically 40-65%, particularly 50-65%. The builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in cleaning detergents may be utilized. Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines such as 2- aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1 -ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

The detergent composition may also contain 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder. The detergent composition may include a co-builder alone, or in combination with a builder, for example a zeolite builder. Non-limiting examples of co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA). Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid. Additional specific examples include 2,2’,2”-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N’-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1 ,1 -diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis (methylenephosphonic acid) (DTMPA or DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N- monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)-aspartic acid (SMAS), N-(2-sulfoethyl)-aspartic acid (SEAS), N-(2-sulfomethyl)-glutamic acid (SMGL), N-(2-sulfoethyl)- glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), a-alanine-N,N-diacetic acid (a-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA) , taurine-N,N-diacetic acid (TUDA) and sulfomethyl-N,N-diacetic acid (SMDA), N-(2- hydroxyethyl)ethylenediamine-N,N’,N”-triacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof. Further exemplary builders and/or co-builders are described in, e.g., WO 09/102854, US 5977053

Bleaching Systems

The cleaning or the detergent may contain 0-30% by weight, such as about 1 % to about 20%, of a bleaching system. Any bleaching system comprising components known in the art for use in cleaning detergents may be utilized. Suitable bleaching system components include sources of hydrogen peroxide; sources of peracids; and bleach catalysts or boosters.

Sources of hydrogen peroxide:

Suitable sources of hydrogen peroxide are inorganic persalts, including alkali metal salts such as sodium percarbonate and sodium perborates (usually mono- or tetrahydrate), and hydrogen peroxide— urea (1/1 ).

Sources of peracids:

Peracids may be (a) incorporated directly as preformed peracids or (b) formed in situ in the wash liquor from hydrogen peroxide and a bleach activator (perhydrolysis) or (c) formed in situ in the wash liquor from hydrogen peroxide and a perhydrolase and a suitable substrate for the latter, e.g., an ester.

a) Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids such as peroxybenzoic acid and its ring-substituted derivatives, peroxy-onaphthoic acid, peroxyphthalic acid, peroxylauric acid, peroxystearic acid, e-phthalimidoperoxycaproic acid [phthalimidoperoxyhexanoic acid (PAP)], and o-carboxybenzamidoperoxycaproic acid; aliphatic and aromatic diperoxydicarboxylic acids such as diperoxydodecanedioic acid, diperoxyazelaic acid, diperoxysebacic acid, diperoxybrassylic acid, 2-decyldiperoxybutanedioic acid, and diperoxyphthalic, -isophthalic and -terephthalic acids; perimidic acids; peroxymonosulfuric acid; peroxydisulfuric acid; peroxyphosphoric acid; peroxysilicic acid; and mixtures of said compounds. It is understood that the peracids mentioned may in some cases be best added as suitable salts, such as alkali metal salts (e.g., Oxone®) or alkaline earth-metal salts.

b) Suitable bleach activators include those belonging to the class of esters, amides, imides, nitriles or anhydrides and, where applicable, salts thereof. Suitable examples are tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1 - sulfonate (ISONOBS), sodium 4-(dodecanoyloxy)benzene-1 -sulfonate (LOBS), sodium 4- (decanoyloxy)benzene-l -sulfonate, 4-(decanoyloxy)benzoic acid (DOBA), sodium 4- (nonanoyloxy)benzene-l -sulfonate (NOBS), and/or those disclosed in W098/17767. A particular family of bleach activators of interest was disclosed in EP624154 and particularly preferred in that family is acetyl triethyl citrate (ATC). ATC or a short chain triglyceride like triacetin has the advantage that they are environmentally friendly. Furthermore, acetyl triethyl citrate and triacetin have good hydrolytical stability in the product upon storage and are efficient bleach activators. Finally, ATC is multifunctional, as the citrate released in the perhydrolysis reaction may function as a builder.

Bleach catalysts and boosters

The bleaching system may also include a bleach catalyst or booster.

Some non-limiting examples of bleach catalysts that may be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine catalysts and manganese triazacyclononane (MnTACN) catalysts; particularly preferred are complexes of manganese with 1 ,4,7-trimethyl-1 ,4,7-triazacyclononane (Me3- TACN) or 1 ,2,4,7-tetramethyM ,4,7-triazacyclononane (Me4-TACN), in particular Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(0)3Mn(Me3-TACN)](PF6)2, and [2,2',2"-nitrilotris(ethane-1 ,2-diylazanylylidene-KN-methanylylidene)triphenolato- K30]manganese(lll). The bleach catalysts may also be other metal compounds, such as iron or cobalt complexes.

In some embodiments, where a source of a peracid is included, an organic bleach catalyst or bleach booster may be used having one of the following formulae:

(iii) and mixtures thereof; wherein each R1 is independently a branched alkyl group containing from 9 to 24 carbons or linear alkyl group containing from 1 1 to 24 carbons, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbons or linear alkyl group containing from 1 1 to 18 carbons, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl, 2-hexyldecyl, dodecyl, tetradecyl, hexadecyl, octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl.

Other exemplary bleaching systems are described, e.g. in W02007/087258, W02007/087244, W02007/087259, EP1867708 (Vitamin K) and W02007/087242. Suitable photobleaches may for example be sulfonated zinc or aluminium phthalocyanines.

Metal care agents

Metal care agents may prevent or reduce the tarnishing, corrosion or oxidation of metals, including aluminium, stainless steel and non-ferrous metals, such as silver and copper. Suitable examples include one or more of the following:

(a) benzatriazoles, including benzotriazole or bis-benzotriazole and substituted derivatives thereof. Benzotriazole derivatives are those compounds in which the available substitution sites on the aromatic ring are partially or completely substituted. Suitable substituents include linear or branch-chain Ci-C20- alkyl groups (e.g., C1 -C20- alkyl groups) and hydroxyl, thio, phenyl or halogen such as fluorine, chlorine, bromine and iodine.

(b) metal salts and complexes chosen from the group consisting of zinc, manganese, titanium, zirconium, hafnium, vanadium, cobalt, gallium and cerium salts and/or complexes, the metals being in one of the oxidation states II, III, IV, V or VI. In one aspect, suitable metal salts and/or metal complexes may be chosen from the group consisting of Mn(ll) sulphate, Mn(ll) citrate, Mn(ll) stearate, Mn(ll) acetylacetonate, K A TiF6 (e.g., K2TiF6), K A ZrF6 (e.g., K2ZrF6), CoS04, Co(NOs)2 and Ce(NOs)3, zinc salts, for example zinc sulphate, hydrozincite or zinc acetate.;

(c) silicates, including sodium or potassium silicate, sodium disilicate, sodium metasilicate, crystalline phyllosilicate and mixtures thereof.

Further suitable organic and inorganic redox-active substances that act as silver/copper corrosion inhibitors are disclosed in WO 94/26860 and WO 94/26859. Preferably the composition of the invention comprises from 0.1 to 5% by weight of the composition of a metal care agent, preferably the metal care agent is a zinc salt.

Hydrotropes

The cleaning or the detergent composition may contain 0-10% by weight, for example 0- 5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope. Any hydrotrope known in the art for use in detergents may be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof. Polymers

The cleaning or the detergent composition may contain 0-10% by weight, such as 0.5- 5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide antiredeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties. Some polymers may have more than one of the above-mentioned properties and/or more than one of the below-mentioned motifs. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or polyethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers , hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI). Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S- 403E and Chromabond S-100 from Ashland Aqualon, and Sokalan® HP 165, Sokalan® HP 50 (Dispersing agent), Sokalan® HP 53 (Dispersing agent), Sokalan® HP 59 (Dispersing agent), Sokalan® HP 56 (dye transfer inhibitor), Sokalan® HP 66 K (dye transfer inhibitor) from BASF. Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO- PPO) and diquaternium ethoxy sulfate. Other exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated. Particularly preferred polymer is ethoxylated homopolymer Sokalan® HP 20 from BASF, which helps to prevent redeposition of soil in the wash liquor.

Fabric hueing agents

The cleaning or the detergent compositions of the present invention may also include fabric hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions and thus altering the tint of said fabric through absorption/reflection of visible light. Fluorescent whitening agents emit at least some visible light. In contrast, fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum. Suitable fabric hueing agents include dyes and dye-clay conjugates and may also include pigments. Suitable dyes include small molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.l.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in W02005/03274, W02005/03275, W02005/03276 and EP 1876226 (hereby incorporated by reference). The detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.001 wt% to about 0.04 wt% fabric hueing agent. The composition may comprise from 0.001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch. Suitable hueing agents are also disclosed in, e.g. WO 2007/087257 and W02007/087243.

Enzymes

The detergent additive as well as the cleaning or the detergent composition may comprise one or more additional enzymes such as at least one lipase, cutinase, amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., laccase, and/or peroxidase.

In general, the properties of the selected enzyme(s) should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.

Cellulases

Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 ,178, US 5,776,757 and WO 89/09259.

Especially suitable cellulases are the alkaline or neutral cellulases having colour care benefits. Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/1 1262, WO 96/29397, WO 98/08940. Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471 , WO 98/12307 and W099/001544.

Other cellulases are endo-beta-1 ,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:2 of WO 2002/099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40-559 of SEQ ID NO: 2 of WO 2001/062903.

Commercially available cellulases include Celluzyme™, and Carezyme™ (Novozymes A/S) Carezyme Premium™ (Novozymes A/S), Celluclean ™ (Novozymes A/S), Celluclean Classic™ (Novozymes A/S), Cellusoft™ (Novozymes A/S), Whitezyme™ (Novozymes A/S), Clazinase™, and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation).

Mannanases

Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is Mannaway (Novozymes A/S).

Peroxidases/Oxidases

Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include Guardzyme™ (Novozymes A/S).

Lipases and Cutinases

Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp. strain SD705

(W095/06720 & W096/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (W010/065455), cutinase from Magnaporthe grise a (W010/107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (W01 1/084412), Geobacillus stearothermophilus lipase (W01 1/084417), lipase from Bacillus subtilis (W01 1/084599), and lipase from Streptomyces griseus (W01 1/150157) and S. pristinaespiralis (W012/137147).

Other examples are lipase variants such as those described in EP407225,

WO92/05249, WO94/01541 , W094/25578, W095/14783, WO95/30744, W095/35381 ,

W095/22615, W096/00292, W097/04079, W097/07202, WO00/34450, WO00/60063,

W001/92502, W007/87508 and WO09/109500.

Preferred commercial lipase products include Lipolase™, Lipex™; Lipolex™ and Lipoclean™ (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades).

Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (W010/100028).

Amylases

Suitable amylases include alpha-amylases and/or a glucoamylases and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839.

Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 264, 304, 305, 391 , 408, and 444.

Different suitable amylases include amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.

Other amylases which are suitable are hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof. Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181 , N190, M197, 1201 , A209 and Q264. Most preferred variants of the hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of SEQ ID NO: 4 are those having the substitutions:

M197T;

H156Y+A181T+N190F+A209V+Q264S; or

G48A+T49I+G107A+H156Y+A181T+N190F+I201 F+A209V+Q264S.

Further amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181 , G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.

Additional amylases which can be used are those having SEQ ID NO: 1 , SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7. Preferred variants of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181 , 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181 , 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184. Most preferred amylase variants of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.

Other amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712. Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201 , 207, 21 1 and 264.

Further suitable amylases are amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof. Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131 , T165, K178, R180, S181 , T182, G183, M201 , F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475. More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131 I, T165I, K178L, T182G, M201 L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183. Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:

N128C+K178L+T182G+Y305R+G475K;

N 128C+K178L+T182G+F202Y+Y305R+D319T+G475K;

S125A+N128C+K178L+T182G+Y305R+G475K; or

S125A+N 128C+T131 I+T165I+K178L+T182G+Y305R+G475K wherein the variants are C-terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181.

Further suitable amylases are amylases having SEQ ID NO: 1 of W013184577 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181 , E187, N192, M199, I203, S241 , R458, T459, D460, G476 and G477. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241 QADN, R458N, T459S, D460T, G476K and G477K and/or deletion in position R178 and/or S179 or of T180 and/or G181. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:

E187P+I203Y+G476K

E187P+I203Y+R458N+T459S+D460T+G476K wherein the variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.

Further suitable amylases are amylases having SEQ ID NO: 1 of W010104675 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21 , D97, V128 K177, R179, S180, 1181 , G182, M200, L204, E242, G477 and G478. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21 D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or deletion in position R179 and/or S180 or of 1181 and/or G182. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:

N21 D+D97N+V128I

wherein the variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181.

Other suitable amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R1 18, N 174; R181 , G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471 , N484. Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R1 18K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.

Other examples are amylase variants such as those described in WO201 1/098531 , WO2013/001078 and WO2013/001087.

Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™ (from Novozymes A/S), and Rapidase™, Purastar™/Effectenz™, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S1 10 (from Genencor International Inc./DuPont).

Proteases

Suitable proteases include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as subtilisin. A metalloproteases protease may for example be a thermolysin from e.g. family M4 or other metalloprotease such as those from M5, M7 or M8 families. The term "subtilases" refers to a sub-group of serine protease according to Siezen et al., Protein Engng. 4 (1991 ) 719-737 and Siezen et al. Protein Science 6 (1997) 501 -523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.

Examples of subtilases are those derived from Bacillus such as Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and W009/021867, and Subtilisin lentus, Subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 described in (WO93/18140). Other useful proteases may be those described in W001/016285 and W002/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in W094/25583 and W005/040372, and the chymotrypsin proteases derived from Cellumonas described in W005/052161 and W005/052146.

A further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in W095/23221 , and variants thereof which are described in WO92/21760, W095/23221 , EP1921 147 and EP1921 148.

Examples of metalloproteases are the neutral metalloprotease as described in WO07/044993 (Proctor & Gamble/Genencor Int.) such as those derived from Bacillus amyloliquefaciens.

Examples of useful proteases are the variants described in: WO89/06279 W092/19729, WO96/034946, WO98/201 15, WO98/201 16, WO99/01 1768, WO01/44452, W003/006602, W004/03186, W004/041979, W007/006305, W01 1/036263, W01 1/036264, especially the variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101 , 102, 104, 1 16, 1 18, 121 , 126, 127, 128, 154, 156, 157, 158, 161 , 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200, 203, 206, 21 1 , 212, 216, 218, 226, 229, 230, 239, 246, 255, 256, 268 and 269 wherein the positions correspond to the positions of the Bacillus lentus protease shown in SEQ ID NO 1 of WO 2016/001449. More preferred the protease variants may comprise one or more of the mutations selected from the group consisting of: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G1 16V, G1 16R, H1 18D, H1 18N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A,

R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199I, Y203W,

S206G, L21 1 Q, L21 1 D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K,

N255W, N255D, N255E, L256E, L256D T268A and R269H. The protease variants are preferably variants of the Bacillus lentus protease shown in SEQ ID NO 1 of WO2016/001449, the Bacillus amylolichenifaciens protease (BPN’) shown in SEQ ID NO 2 of WO2016/001449. The protease variants preferably have at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to SEQ ID NO 1 or SEQ ID NO 2 of WO 2016/001449.

A protease variant comprising a substitution at one or more positions corresponding to positions 171 , 173, 175, 179, or 180 of SEQ ID NO: 1 of W02004/067737, wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of W02004/067737.

Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Duralase Tm , Durazyrn Tm , Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Neutrase®, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect Ox®, Purafect OxP®, Puramax®, FN2®, FN3®, FN4®, Excellase®, Excellenz P1000™, Excellenz P1250™, Eraser®, Preferenz P100™, Purafect Prime®, Preferenz P1 10™, Effectenz P1000™, Purafect®™, Effectenz P1050™, Purafect Ox®™, Effectenz P2000™, Purafast®, Properase®, Opticlean® and Optimase® (Danisco/DuPont), Axapem™ (Gist-Brocases N.V.), BLAP (sequence shown in Figure 29 of US5352604) and variants hereof (Henkel AG) and KAP ( Bacillus alkalophilus subtilisin) from Kao.

Peroxidases/Oxidases

A peroxidase according to the invention is a peroxidase enzyme comprised by the enzyme classification EC 1.1 1.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity.

Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (EP 179,486), and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.

A suitable peroxidase includes a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1 .1 1.1 .10) catalyze formation of hypochlorite from chloride ions. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.

Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.

A suitable oxidase includes in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1 ), an o- aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5). Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P. papilionaceus, Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885). Suitable examples from bacteria include a laccase derivable from a strain of Bacillus. A laccase derived from Coprinopsis or Myceliophthora is preferred; in particular, a laccase derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.

DNases

Polypeptide with DNase (deoxyribonuclease) activity also termed DNases catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA. The DNase activity can be determined as described in the Assay I of WO2015/155350. Polypeptides having DNase activity are known to reduce or remove biofilm soil. Biofilm is an extracellular matrix produced by various microorganisms. The extracellular polymeric matrix is composed of polysaccharides, extracellular DNA (exDNA) and proteins. In a preferred embodiment of the invention, the polypeptide having DNase activity is obtained from a microbial source, preferably obtained from Aspergillus such as the DNase described in WO2015/155350, Trichoderma e.g. such as the DNase described in WO2015/155351 , Bacillus such as a DNase described in WO201 1/098579, WO2014/08701 1 or any of the DNases described in WO2017/060475.

Dispersants

The cleaning or the detergent compositions of the present invention can also contain dispersants. In particular, powdered detergents may comprise dispersants. Suitable water- soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker. Dye Transfer Inhibiting Agents

The cleaning or the detergent compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.001 % to about 10%, from about 0.01 % to about 5% or even from about 0.1 % to about 3% by weight of the composition.

Fluorescent whitening agent

The cleaning or the detergent compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01 % to about 0.5%. Any fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6- ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino) stilbene-2.2'- disulfonate, 4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydroxy-ethylamino)-s-tr iazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1 ,2,3-triazol-2-yl)stilbene-2,2'-disulfonate and sodium 5-(2H-naphtho[1 ,2-d][1 ,2,3]triazol-2-yl)-2-[(E)-2-phenylvinyl]benzenesulfonate.

Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba- Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis-(2-morpholino-4- anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate. Tinopal CBS is the disodium salt of 2,2'-bis- (phenyl-styryl)-disulfonate. Also preferred are fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India. Other fluorescers suitable for use in the invention include the 1 -3-diaryl pyrazolines and the 7- alkylaminocoumarins. Suitable fluorescent brightener levels include lower levels of from about 0.01 , from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt%.

Soil release polymers

The cleaning or the detergent compositions of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics. The soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc. Another type of soil release polymers is amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure. The core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (hereby incorporated by reference). Furthermore, random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/1 13314 (hereby incorporated by reference). Suitable polyethylene glycol polymers include random graft co-polymers comprising: (i) hydrophilic backbone comprising polyethylene glycol; and (ii) side chain(s) selected from the group consisting of: C4-C25 alkyl group, polypropylene, polybutylene, vinyl ester of a saturated C1 -C6 mono-carboxylic acid, Cl-C 6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof. Suitable polyethylene glycol polymers have a polyethylene glycol backbone with random grafted polyvinyl acetate side chains. The average molecular weight of the polyethylene glycol backbone can be in the range of from 2,000 Da to 20,000 Da, or from 4,000 Da to 8,000 Da. The molecular weight ratio of the polyethylene glycol backbone to the polyvinyl acetate side chains can be in the range of from 1 : 1 to 1 :5, or from 1 : 1.2 to 1 :2. The average number of graft sites per ethylene oxide units can be less than 1 , or less than 0.8, the average number of graft sites per ethylene oxide units can be in the range of from 0.5 to 0.9, or the average number of graft sites per ethylene oxide units can be in the range of from 0.1 to 0.5, orfrom 0.2 to 0.4. A suitable polyethylene glycol polymer is Sokalan HP22. Other soil release polymers are substituted polysaccharide structures especially substituted cellulosic structures such as modified cellulose deriviatives such as those described in EP 1867808 or WO 2003/040279 (both are hereby incorporated by reference). Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxy methyl cellulose, ethyl cellulose, hydroxyl ethyl cellulose, hydroxyl propyl methyl cellulose, ester carboxy methyl cellulose, and mixtures thereof.

Anti-redeposition agents

The cleaning or the detergent compositions of the present invention may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimines. The cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents. Rheology Modifiers

The cleaning or the detergent compositions of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents. The rheology modifiers are selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition. The rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040.

Other suitable cleaning composition components include, but are not limited to, anti- shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents.

Formulation of detergent products

The cleaning or the detergent composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.

Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact. The pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch. Preferred films are polymeric materials preferably polymers which are formed into a film or sheet. Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC). Preferably the level of polymer in the film for example PVA is at least about 60%. Preferred average molecular weight will typically be about 20,000 to about 150,000. Films can also be of blended compositions comprising hydrolytically degradable and water soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof. The pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water soluble film. The compartment for liquid components can be different in composition than compartments containing solids: US2009/001 1970 A1.

Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.

A liquid or gel detergent, which is not unit dosed, may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids, including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel. An aqueous liquid or gel detergent may contain from 0-30% organic solvent. A liquid or gel detergent may be non-aqueous.

Granular detergent formulations

The composition(s) of the invention may be formulated as a granule for example as a co- granule that combines one or more enzymes. Each enzyme will then be present in more granules securing a more uniform distribution of enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. Methods for producing multi- enzyme co-granulates for the detergent industry are disclosed in the IP.com disclosure IPCOM000200739D.

Another example of formulation of enzymes by the use of co-granulates are disclosed in WO 2013/188331 , which relates to a detergent composition comprising (a) a multi-enzyme co- granule; (b) less than 10 wt zeolite (anhydrous basis); and (c) less than 10 wt phosphate salt (anhydrous basis), wherein said enzyme co-granule comprises from 10 to 98 wt% moisture sink component and the composition additionally comprises from 20 to 80 wt% detergent moisture sink component.

The multi-enzyme co-granule may comprise an RNase of the invention and (a) one or more enzymes selected from DNases, lipases, hemicellulases, proteases, amylases, cellulases, cellobiose dehydrogenases, xylanases, phospho lipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, tannases, pentosanases, lichenases glucanases, arabinosidases, hyaluronidase, chondroitinase, amylases, and mixtures thereof.

The invention is further summarized in the following paragraphs:

1 . A cleaning composition comprising one or more anionic surfactants, and at least one polypeptide having RNase activity.

2. The cleaning composition according to paragraph 1 , wherein the composition further comprises one or more cleaning composition components, preferably selected from surfactants, builders, bleach components, polymers, dispersing agents and additional enzymes.

3. The cleaning composition according to any of paragraphs 1 -2, wherein the composition comprises from 0.5 to about 80 wt % of the anionic surfactant, such as from about 1.0 wt

% to 60 wt %, from about 5 wt % to about 50 wt %, from about 5 wt % to about 40 wt % , from about 5 wt % to about 30 wt % , from about 5 wt % to about 20 wt % , from about 5 wt % to about 10 wt % of the anionic surfactant.

4. The cleaning composition according to paragraph 3, wherein the anionic surfactant is selected from linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2, 3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ethersulfates (AES or AEOS or FES), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid methyl esters (alpha-SFMe or SES) including methyl ester sulfonate (MES), alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfo-succinic acid or salt of fatty acids (soap), and combinations thereof.

5. The cleaning composition according to any of the preceding paragraphs, wherein the composition further comprises a non-ionic surfactant.

6. The cleaning composition according to paragraph 5, wherein the nonionic surfactant is selected from alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA) and combinations thereof.

7. The cleaning composition according to any of paragraphs 6-7, wherein the weight ratio of anionic to non-ionic surfactant is from 10:1 to 1 :5.

8. The cleaning composition according to paragraph 7, wherein the weight ratio of anionic to non-ionic surfactant is from 7:1 to 1 :4, from 6:1 to 1 :3, from 5:1 to 1 :2.5, from 4:1 to 1 :2.2, from 3:1 to 1 :2 or from 2:1 to 1 :1.

9. The cleaning composition according to any of the preceding paragraphs, wherein the composition further comprises from 0.5 to 65% by weight of a builder and/or a co-builder, such as from 5 to 50% by weight or from 40 to 65% by weight or from 50 to 65% by weight.

10. The cleaning composition according to paragraph 9, wherein the builder is selected from the group consisting of zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates, ethanolamines such as 2- aminoethan-1 -ol (MEA), diethanolamine (DEA, also known as 2,2’-iminodiethan-1 -ol), triethanolamine (TEA, also known as 2,2’,2”-nitrilotriethan-1 -ol), and (carboxymethyl)inulin (CMI), and combinations thereof.

1 1 . The cleaning composition according to any of paragraphs 9-10, wherein the co-builder is selected from the group consisting of homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA), citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid, 2,2’,2”-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-/V,/V’-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-/V,/V-diacetic acid (GLDA), 1 - hydroxyethane-1 ,1 -diphosphonic acid (HEDP), ethylenediaminetetra(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis(methylenephosphonic acid) (DTMPA or DTPMPA), N-( 2- hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-/V-monoacetic acid (ASMA), aspartic acid-/V,/V-diacetic acid (ASDA), aspartic acid-/V-monopropionic acid (ASMP), iminodisuccinic acid (IDA), /V-(2-sulfomethyl)-aspartic acid (SMAS), /V-(2-sulfoethyl)- aspartic acid (SEAS), /V-(2-sulfomethyl)-glutamic acid (SMGL), /V-(2-sulfoethyl)-glutamic acid (SEGL), /V-methyliminodiacetic acid (MIDA), a-alanine-/V,/V-diacetic acid (a-ALDA), serine-/V,/V-diacetic acid (SEDA), isoserine-/V,/V-diacetic acid (ISDA), phenylalanine-/V,/V- diacetic acid (PHDA), anthranilic acid-/V,/V-diacetic acid (ANDA), sulfanilic acid -N,N- diacetic acid (SLDA) , taurine-/V,/V-diacetic acid (TUDA) and sulfomethyl-/V,/V-diacetic acid (SMDA), /V-(2-hydroxyethyl)ethylenediamine-/V,/V',/V”-triacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof.

12. The cleaning composition according to any of paragraphs 9-1 1 , wherein the builder is selected from sodium alumino silicate, soluble silicates such as sodium metasilicate, layered silicates, citric acid, methylglycine-N,N-diacetic acid (MGDA), glutamic acid-N,N- diacetic acid (GLDA) and mixtures thereof.

13. The cleaning composition according to any of paragraphs 1-2, wherein the composition comprises at least 80% by weight alkyl benzene sulphonate surfactant, preferably at least 85 % by weight linear alkyl benzene sulphonate (LAS); and from 0.01 to 1 % by weight of sodium alumino silicate.

14. The cleaning composition according to any of the preceding paragraphs, wherein the composition further comprises one or more enzymes selected from the group consisting of DNases, proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthanases, peroxidaes, haloperoxygenases, catalases, galactanase, mannanases, or any mixture thereof. 15. The cleaning composition according to any of the preceding paragraphs, wherein the composition is in the form of a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, a regular liquid, a compact liquid or concentrated liquid.

16. The cleaning composition according to any of the preceding paragraphs, wherein one or more of the enzymes are encapsulated in a microcapsule.

17. The cleaning composition according to any of the preceding paragraphs, wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25).

18. The cleaning composition according to any of the preceding paragraphs, wherein the polypeptide having RNase activity is, preferably a polypeptide of the clades EYTV, EAD or YPH, selected from the group consisting of:

(a) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 1 ;

(b) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 2;

(c) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 3;

(d) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 4;

(e) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 5;

(f) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 6;

(g) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 7; (h) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 8;

(i) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 9;

(j) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 10;

(k) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 1 1 ;

(L) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 12;

(m)a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 13;

(n) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 14;

(o) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 15;

(p) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 16;

(q) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 17;

(r) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 18;

(s) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 19; (t) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 20;

(u) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 27;

(v) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 34;

(w) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 35;

(x) a variant of the polypeptide selected from the group consisting of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 27, SEQ ID NO: 34 and SEQ ID NO: 35, wherein the variant has RNase activity and comprises one or more amino acid substitutions, and/or one or more amino acid deletions, and/or one or more amino acid insertions or any combination thereof in 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19 or 20 positions;

(y) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal His-tag and/or HQ-tag;

(z) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal extension of between 1 and 10 amino acids;

(aa) a fragment of the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s) , (t), (u), (v), (w) or (x)having RNase activity and having at least 90% of the length of the mature polypeptide;

(bb) a polypeptide comprising one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), YPH (SEQ ID NO: 24), HTGA (SEQ ID NO: 25) or DRV (SEQ ID NO:26); and

(cc) a polypeptide comprising one or more of the motifs YXEYTVXTPXXXXRGXRR (SEQ ID NO: 28), [WY][YRF]E[AYFWC]D[IV] (SEQ ID NO: 29), GXXIGGDXFXN (SEQ ID NO: 30), YPHX[YFA]X[ND]XE (SEQ ID NO: 31 ), PGXDRV (SEQ ID NO: 32) or THTGA[SR]G (SEQ ID NO: 33).

19. The cleaning composition according to any of the preceding paragraphs, wherein the composition comprises at least 0.0002 wt%, such as at least 0.002 wt% or at least 0.02 wt%, of a polypeptide having RNase activity, wherein the polypeptide is selected from the group consisting of: SEQ ID NO 1 , SEQ ID NO 2, SEQ ID NO 3, SEQ ID NO 4, SEQ ID NO 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 1 1 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17 , SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 27, SEQ ID NO: 34 and SEQ ID NO: 35 and polypeptides having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity hereto.

20. The cleaning composition according to any of the preceding paragraphs, wherein the concentration of the polypeptide having RNase activity is 0.0002 wt% to 5 wt%.

21 . The cleaning composition according to paragraph 20, wherein the concentration of the polypeptide having RNase activity is in the range of is in the range 0.002 wt% to 5 wt%, such as in the range of 0.002 wt% to 5 wt%, in the range of 0.02 wt% to 2 wt%, in the range of 0.2 wt% to 2 wt% of the total detergent composition.

22. A method of cleaning an item comprising the steps of:

(a) Exposing the item to water;

(b) Optionally remove excess of water;

(c) Exposing the item to a wash liquor comprising the cleaning composition of any of paragraphs 1 -21 or at least one polypeptide having RNase activity;

(d) Completing at least one wash cycle; and

(e) Optionally rinsing the item;

wherein the item is a textile, a dish ware or a hard surface.

23. The method according to paragraph 22, wherein the item is a textile.

24. The method according to paragraph 23, wherein textile is a hydrophobically-modified textile.

25. The method according to any of paragraphs 22-24, wherein the textile comprises ccotton, polyester, polyamide, polyacryl, silk and mixtures thereof.

26. The method according to paragraph 22, wherein the item is a hard surface.

27. The method according to paragraph 22, wherein the item is a dish ware.

28. The method according to any of paragraphs 22-27, wherein the pH of the wash liquor is in the range 5.5 to 1 1 , such as in the range of 7 to 9, in the range of 7 to 8 or in the range of 7 to 8.5.

29. The method according to any of paragraphs 22-28, wherein the temperature of the wash liquor is in the range of 5°C to 95°C, or in the range of 10°C to 80°C, in the range of 10°C to 70°C, in the range of 10°C to 60°C, in the range of 10°C to 50°C, in the range of 15°C to 40°C, in the range of 20°C to 40°C, in the range of 15°C to 30°C or in the range of 20°C to 30°C.

30. The method according to paragraph 29, wherein the temperature of the wash liquor is from about 20°C to about 40°C.

31 . The method according to any of paragraphs 29-30, wherein the temperature of the wash liquor is from about 15°C to about 30°C.

32. The method according to any of paragraphs 22-31 , wherein stickiness of the item is reduced.

33. The method according to any of paragraphs 22-32, wherein redeposition of soil is reduced.

34. The method according to any of paragraphs 22-33, wherein adherence of soil to the item is reduced or removed.

35. The method according to any of paragraphs 22-34, wherein whiteness of the item is maintained or improved.

36. The method according to any of paragraphs 22-35, wherein malodor is reduced or removed from the item.

37. The method according to any of paragraphs 22-36, wherein the concentration of the polypeptide having RNase activity in the wash liquor is in the range 0.0002 mg/L to 5 mg/L, such as in the range 0.002 mg/L to 5 mg/L, in the range of 0.02 mg/L to 2 mg/L, in the range of 0.2 mg/L to 2 mg/L.

38. A method according to any of paragraphs 22-37, wherein the item is exposed to water and the excess of water is removed by dripping, wringing and/or centrifuging.

39. A method according to any of paragraph 22-38, wherein the polypeptide having RNase activity comprises one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), DRV (SEQ ID NO 26), YPH (SEQ ID NO: 24) or HTGA (SEQ ID NO: 25).

40. The method according to any of paragraphs 22-39, wherein the polypeptide having RNase activity, preferably is a polypeptide of the clades EYTV, EAD or YPH, selected from the group consisting of:

(a) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 1 ; (b) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 2;

(c) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 3;

(d) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 4;

(e) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 5;

(f) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 6;

(g) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 7;

(h) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 8;

(i) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 9;

(j) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 10;

(k) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 1 1 ;

(L) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 12;

(m) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 13; (n) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 14;

(o) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 15;

(p) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 16;

(q) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 17;

(r) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 18;

(s) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 19;

(t) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 20;

(u) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 27;

(v) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 34;

(w) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 90%, at least 95%, at least 97%, at least 98 or 100% sequence identity to the polypeptide of SEQ ID NO: 35;

(x) a variant of the polypeptide selected from the group consisting of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11 , SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, SEQ ID NO: 27, SEQ ID NO: 34 and SEQ ID NO: 35, wherein the variant has RNase activity and comprises one or more amino acid substitutions, and/or one or more amino acid deletions, and/or one or more amino acid insertions or any combination thereof in 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10, 1 1 , 12, 13, 14, 15, 16, 17, 18, 19 or 20 positions;

(y) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal His-tag and/or HQ-tag;

(z) a polypeptide comprising the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) and an N-terminal and/or C-terminal extension of between 1 and 10 amino acids;

(aa) a fragment of the polypeptide of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j), (k), (I), (m), (n), (o), (p), (q), (r), (s), (t), (u), (v), (w) or (x) having RNase activity and having at least 90% of the length of the mature polypeptide;

(bb) a polypeptide comprising one or more of the motif(s) EYTV (SEQ ID NO: 21 ), [YRF]E[AYFWC]D (SEQ ID NO: 22), IGGD (SEQ ID NO: 23), YPH (SEQ ID NO: 24), HTGA (SEQ ID NO: 25) or DRV (SEQ ID NO:26); and

(cc) a polypeptide comprising one or more of the motifs YXEYTVXTPXXXXRGXRR (SEQ ID NO: 28), [WY][YRF]E[AYFWC]D[IV] (SEQ ID NO: 29), GXXIGGDXFXN (SEQ ID NO: 30), YPHX[YFA]X[ND]XE (SEQ ID NO: 31 ), PGXDRV (SEQ ID NO: 32) or THTGA[SR]G (SEQ ID NO: 33).

41. Use of a cleaning composition according to any of paragraphs 1-21 for cleaning an item by:

(a) preventing, reducing or removing stickiness of the item;

(b) preventing, reducing or removing RNA or RNA components from the item;

(c) preventing, reducing or removing redeposition of soil during cleaning of the item;

(d) preventing, reducing or removing adherence of soil to the item;

(e) maintaining or improving whiteness of the item; or

(f) preventing, reducing or removing malodor from the item;

wherein the item is a textile, a hard surface or a dish ware.

42. Use according to paragraph 41 , wherein the measured effect ratio of test panellists preferring fabrics washed with RNase vs test panellists preferring fabrics washed without RNase is at least 60:40, preferably at least 70:30, preferably at least 80:20 or preferably at least 90:10, when measured as described in Example 16.

43. Use according to paragraph 41 , wherein the cleaning effect e.g. deep cleaning effect ratio of test panellists preferring fabrics washed with RNase vs test panellists preferring fabrics washed without RNase is at least 60:40, preferably at least 70:30, preferably at least 80:20 or preferably at least 90:10, when measured as described in Example 16.

EXAMPLES

Cleaning compositions

Any of the cleaning compositions described below, may include one or more RNase and any number of additional enzymes. In general, the enzyme(s) should be compatible with the selected detergent, (e.g., with respect to pH-optimum, compatibility with other enzymatic and non- enzymatic ingredients, and the like), and the enzyme(s) should be present in effective amounts.

The products named Tide, Ariel, Gain and Fairy are commercially available products supplied by Procter & Gamble. The products named Persil are commercially available products supplied by Unilever and Henkel. The products named Hey Sport are commercially available products supplied by Hey Sport.

Model detergent A wash liquor (100%) was prepared by dissolving 3.33 g/l of model detergent A containing 12% LAS, 1.1 % AEO Biosoft N25-7 (Nl), 7% AEOS (SLES), 6% MPG, 3% ethanol, 3% TEA (triethanolamine), 2.75% cocoa soap, 2.75% soya soap, 2% glycerol, 2% sodium hydroxide, 2% sodium citrate, 1 % sodium formiate, 0.2% DTMPA and 0.2% PCA (all percentages are w/w (weight volume) in water with hardness 15 dH.

Triple-20 Nonionic Model Detergent (60% surfactant) was prepared by dissolving 3.33 g/l non- ionic detergent containing NaOH 0.87%, MPG (Monopropylenglycol) 6%, Glycerol 2%, Soap- soy 2.75%, Soap-coco 2.75%, PCA (Sokalon CP-5) 0.2%, AEO Biosoft N25-7(NI) 16%, Sodium formiate 1 %, Sodium Citrate 2%, DTMPA 0.2%, Ethanol (96%) 3 %, adjustment of pH with NaOH or Citric acid ass water to 100% (all percentages are w/w (weight volume) in water with hardness 15 dH.

Model Detergent MC: A medical cleaning model detergent (model detergent MC) was prepared containing 5% MPG (propylene glycol), 5% Pluronic PE 4300 (PO/EO block polymer; 70%/30%, approx. 1750 g/mol), 2% Plurafac LF 305 (fatty alcohol alkoxylate; C6-10 + EO/PO), 1 % MGDA (methyl glycine diacetic acid, 1 % TEA (triethanolamine) (all percentages are w/w). The pH was adjusted to 8.7 with phosphoric acid.

Composition of Model detergent T (powder)

Ingredients: 1 1 % LAS, 2% AS/AEOS, 2% soap, 3% AEO, 15.15% sodium carbonate, 3% sodium silicate, 18.75% zeolite, 0.15% chelant, 2% sodium citrate, 1.65% AA MA copolymer, 2.5% CMC and 0.5% SRP (all percentages are w/w).

Composition of Model detergent X (powder)

Ingredients: 16.5% LAS, 15% zeolite, 12% sodium disilicate, 20% sodium carbonate,

1 % sokalan, 35.5% sodium sulfate (all percentages are w/w). Persil 2 in1 with Comfort Passion Flower Powder

Sodium sulfate, Sodium carbonate, Sodium Dodecylbenzenesulfonate, Bentonite, Sodium Carbonate Peroxide, Sodium Silicate, Zeolite, Aqua, Citric acid, TAED, C12-15 Pareth- 7, Stearic Acid, Parfum, Sodium Acrylic Acid/MA Copolymer, Cellulose Gum, Corn Starch Modified, Sodium chloride, Tetrasodium Etidronate, Calcium Sodium EDTMP, Disodium Anilinomorpholinotriazinyl-aminostilbenesulfonate, Sodium bicarbonate, Phenylpropyl Ethyl Methicone, Butylphenyl Methylpropional, Glyceryl Stearates, Calcium carbonate, Sodium Polyacrylate, Alpha-Isomethyl lonone, Disodium Distyrylbiphenyl Disulfonate, Cellulose, Protease, Limonene, PEG-75, Titanium dioxide, , Dextrin, Sucrose, Sodium Polyaryl Sulphonate, Cl 12490, Cl 45100, Cl 42090, Sodium Thiosulfate, Cl 61585.

Persil Biological Tablets

Sodium carbonate, Sodium Carbonate Peroxide, Sodium bicarbonate, Zeolite, Aqua, Sodium Silicate, Sodium Lauryl Sulfate, Cellulose, TAED, Sodium Dodecylbenzenesulfonate, Hemicellulose, Lignin, Lauryl Glucoside, Sodium Acrylic Acid/MA Copolymer, Bentonite, Sodium chloride, Parfum, Tetrasodium Etidronate, Sodium sulfate, Sodium Polyacrylate, Dimethicone, Disodium Anilinomorpholinotriazinylaminostilbenesulfonate, Dodecylbenzene Sulfonic Acid, Trimethylsiloxysilicate, Calcium carbonate, Cellulose, PEG-75, Titanium dioxide, Dextrin, Protease, Corn Starch Modified, Sucrose, Cl 12490, Sodium Polyaryl Sulphonate, Sodium Thiosulfate, Amylase, Kaolin.

Persil Colour Care Biological Powder

Subtilisin, Imidazolidinone, Hexyl Cinnamal, Sucrose, Sorbitol, Aluminum Silicate, Polyoxymethylene Melamine, Cl 61585, Cl 45100, Lipase, Amylase, Xanthan gum, Hydroxypropyl methyl cellulose, Cl 12490, Disodium Distyrylbiphenyl Disulfonate, Sodium Thiosulfate, Cl 42090, Mannanase, Cl 1 1680, Etidronic Acid, Tetrasodium EDTA.

Persil Dual Action Capsules Bio

MEA-Dodecylbenzenesulfonate, MEA-Hydrogenated Cocoate, C12-15 Pareth-7, Dipropylene Glycol, Aqua, Tetrasodium Etidronate, Polyvinyl Alcohol, Glycerin, Aziridine, homopolymer ethoxylated, Propylene glycol, Parfum, Sodium Diethylenetriamine Pentamethylene Phosphonate, Sorbitol, MEA-Sulfate, Ethanolamine, Subtilisin, Glycol, Butylphenyl Methylpropional, Boronic acid, (4-formylphenyl), Hexyl Cinnamal, Limonene, Linalool, Disodium Distyrylbiphenyl Disulfonate, Alpha-Isomethyl lonone, Geraniol, Amylase, Polymeric Blue Colourant, Polymeric Yellow Colourant, Talc, Sodium chloride, Benzisothiazolinone, Mannanase, Denatonium Benzoate.

Persil 2 in1 with Comfort Sunshiny Days Powder

Sodium sulfate, Sodium carbonate, Sodium Dodecylbenzenesulfonate, Bentonite, Sodium Carbonate Peroxide, Sodium Silicate, Zeolite, Aqua, Citric acid, TAED, C12-15 Pareth- 7, Parfum, Stearic Acid, Sodium Acrylic Acid/MA Copolymer, Cellulose Gum, Corn Starch Modified, Sodium chloride, Tetrasodium Etidronate, Calcium Sodium EDTMP, Disodium Anilinomorpholinotriazinyl-aminostilbenesulfonate, Sodium bicarbonate, Phenylpropyl Ethyl Methicone, Butylphenyl Methylpropional, Glyceryl Stearates, Calcium carbonate, Sodium Polyacrylate, Geraniol, Disodium Distyrylbiphenyl Disulfonate, Cellulose, Protease, PEG-75, Titanium dioxide, Dextrin, Sucrose, Sodium Polyaryl Sulphonate, Cl 12490, Cl 45100, Cl 42090, Sodium Thiosulfate, Cl 61585.

Persil Small & Mighty 2in1 with Comfort Sunshiny Days

Aqua, C12-15 Pareth-7, Sodium Dodecylbenzenesulfonate, Propylene glycol, Sodium Hydrogenated Cocoate, Triethanolamine, Glycerin, TEA-Hydrogenated Cocoate, Parfum, Sodium chloride, Polyquaternium-10, PVP, Polymeric Pink Colourant, Sodium sulfate, Disodium Distyrylbiphenyl Disulfonate, Butylphenyl Methylpropional, Styrene/Acrylates Copolymer, Hexyl Cinnamal, Citronellol, Eugenol, Polyvinyl Alcohol, Sodium acetate, Isopropyl alcohol, Polymeric Yellow Colourant, Sodium Lauryl Sulfate.

Persil Small & Mighty Bio

Aqua, MEA-Dodecylbenzenesulfonate, Propylene glycol, Sodium Laureth Sulfate, C12- 15 Pareth-7, TEA-Hydrogenated Cocoate, MEA-Citrate, Aziridine homopolymer ethoxylated, MEA-Etidronate, Triethanolamine, Parfum, Acrylates Copolymer, Sorbitol, MEA-Sulfate, Sodium Sulfite, Disodium Distyrylbiphenyl Disulfonate, Butylphenyl Methylpropional, Styrene/Acrylates Copolymer, Citronellol, Sodium sulfate, Peptides, salts, sugars from fermentation (process), Subtilisin, Glycerin, Boronic acid, (4-formylphenyl), Geraniol, Pectate Lyase, Amylase, Sodium Lauryl Sulfate, Mannanase, Cl 42051 .

Persil Small & Mighty Capsules Biological

MEA-Dodecylbenzenesulfonate, MEA-Hydrogenated Cocoate, C12-15 Pareth-7, Dipropylene Glycol, Aqua, Glycerin, Polyvinyl Alcohol, Parfum, Aziridine homopolymer ethoxylated, Sodium Diethylenetriamine Pentamethylene Phosphonate, Propylene glycol, Sorbitol, MEA-Sulfate, Ethanolamine, Subtilisin, Glycol, Butylphenyl Methylpropional, Hexyl Cinnamal, Starch, Boronic acid, (4-formylphenyl), Limonene, Linalool, Disodium Distyrylbiphenyl Disulfonate, Alpha-Isomethyl lonone, Geraniol, Amylase, Talc, Polymeric Blue Colourant, Sodium chloride, Benzisothiazolinone, Denatonium Benzoate, Polymeric Yellow Colourant, Mannanase.

Persil Small & Mighty Capsules Colour Care

MEA-Dodecylbenzenesulfonate, MEA-Hydrogenated Cocoate, C12-15 Pareth-7, Dipropylene Glycol, Aqua, Glycerin, Polyvinyl Alcohol, Parfum, Aziridine homopolymer ethoxylated, Sodium Diethylenetriamine Pentamethylene Phosphonate, Propylene glycol, MEA- Sulfate, Ethanolamine, PVP, Sorbitol, Butylphenyl Methylpropional, Subtilisin, Hexyl Cinnamal, Starch, Limonene, Linalool, Boronic acid, (4-formylphenyl), Alpha-Isomethyl lonone, Geraniol, Talc, Polymeric Blue Colourant, Denatonium Benzoate, Polymeric Yellow Colourant. Persil Small & Mighty Colour Care

Aqua, MEA-Dodecylbenzenesulfonate, Propylene glycol, Sodium Laureth Sulfate, C12- 15 Pareth-7, TEA-Hydrogenated Cocoate, MEA-Citrate, Aziridine homopolymer ethoxylated, MEA-Etidronate, Triethanolamine, Parfum, Acrylates Copolymer, Sorbitol, MEA-Sulfate, Sodium Sulfite, Glycerin, Butylphenyl Methylpropional, Citronellol, Sodium sulfate, Peptides, salts, sugars from fermentation (process), Styrene/Acrylates Copolymer, Subtilisin, Boronic acid, (4- formylphenyl), Geraniol, Pectate Lyase, Amylase, Sodium Lauryl Sulfate, Mannanase, Cl 61585, Cl 45100.

Composition of Ariel Actilift (powder)

Ingredients: 5-15% Anionic surfactants, Oxygen-based bleaching agents, <5% Non- ionic surfactants, Phosphonates, Polycarboxylates, Zeolites, Optical brightners, Enzymes, Perfumes, Butylphenyl Methylpropional, Coumarin, Hexyl Cinnamal.

Composition of Persil Megaperls (powder)

Ingredients: 15 - 30% of the following: anionic surfactants, oxygen-based bleaching agent and zeolites, less than 5% of the following: non-ionic surfactants, phosphonates, polycarboxylates, soap, Further ingredients: Perfumes, Hexyl cinnamal, Benzyl salicylate, Linalool, optical brighteners, Enzymes and Citronellol.

Liquid Tide, Free and Gentle:

Water, sodium alcoholethoxy sulfate, propylene glycol, borax, ethanol, linear alkylbenzene sulfonate sodium, salt, polyethyleneimine ethoxylate, diethylene glycol, trans sulfated & ethoxylated hexamethylene diamine, alcohol ethoxylate, linear alkylbenzene sulfonate, MEA salt, sodium formate, sodium alkyl sulfate, DTPA, amine oxide, calcium formate, disodium diaminostilbene, disulfonate, amylase, protease, dimethicone, benzisothiazolinone.

Tide Coldwater Liquid, Fresh Scent:

Water, alcoholethoxy sulfate, linear alkylbenzene sulfonate, diethylene glycol, propylene glycol, ethanolamine, citric acid, Borax, alcohol sulfate, sodium hydroxide, polyethyleneimine, ethoxylate, sodium fatty acids, ethanol, protease, Laureth-9, diquaternium ethoxysulfate, lauramine oxide, sodium cumene, sulfonate, fragrance, DTPA, amylase, disodium, diaminostilbene, disulfonate, sodium formate, disodium distyrylbiphenyl disulfonate, calcium formate, polyethylene glycol 4000, mannanase, pectinase, Liquitint™ Blue, dimethicone.

Liquid Tide Plus Bleach Alternative™, Vivid White and Bright, Original and Clean Breeze:

Water, sodium alcoholethoxy sulfate, sodium alkyl sulfate, MEA citrate, linear alkylbenzene sulfonate, MEA salt, propylene glycol, diethylene glycol, polyethyleneimine ethoxylate, ethanol, sodium fatty acids, ethanolamine, lauramine oxide, borax, Laureth-9, DTPA, sodium cumene sulfonate, sodium formate, calcium formate, linear alkylbenzene sulfonate, sodium salt, alcohol sulfate, sodium hydroxide, diquaternium ethoxysulfate, fragrance, amylase, protease, mannanase, pectinase, disodium diaminostilbene disulfonate, benzisothiazolinone, Liquitint™ Blue, dimethicone, dipropylethyl tetraamine.

Tide TOTALCARE HE Liquid, renewing Rain:

Water, alcoholethoxy sulfate, linear alkylbenzene sulfonate, alcohol ethoxylate, citric acid, Ethanolamine, sodium fatty acids, diethylene glycol, propylene glycol, sodium hydroxide, borax, polyethyleneimine ethoxylate, silicone polyether, ethanol, protease, sodium cumene sulfonate, diquaternium ethoxysulfate, Laureth-9, fragrance, amylase, DTPA, disodium diaminostilbene disulfonate, disodium distyrylbiphenyl disulfonate, sodium formate, calcium formate, mannanase, Liquitint™ Orange, dimethicone, polyacrylamide quaternium chloride, cellulase, dipropylethyl tetraamine.

Tide liquid HE Free:

Water, alcoholethoxy sulfate, diethylene glycol, monoethanolamine citrate, sodium formate, propylene glycol, linear alkylbenzene sulfonates, ethanolamine, ethanol, polyethyleneimine ethoxylate, amylase, benzisothiazolin, borax, calcium formate, citric acid, diethylenetriamine pentaacetate sodium, dimethicone, diquaternium ethoxysulfate, disodium diaminostilbene disulfonate, Laureth-9, mannanase, protease, sodium cumene sulfonate, sodium fatty acids.

Tide Coldwater HE Liquid, Fresh Scent:

Water, alcoholethoxy sulfate, MEA Citrate, alcohol sulfate, Alcohol ethoxylate, Linear alkylbenzene sulfonate MEA, sodium fatty acids, polyethyleneimine ethoxylate, diethylene glycol, propylene glycol, diquaternium ethoxysulfate, borax, polyethyleneimine ethoxylate propoxylate, ethanol, sodium cumene sulfonate, fragrance, DTPA, disodium diaminostilbene disulfonate, protease, mannanase, cellulase, amylase, sodium formate, calcium formate, lauramine oxide, Liquitint™ Blue, dimethicone.

Tide for Coldwater HE Free Liquid:

Water, sodium alcoholethoxy sulfate, MEA Citrate, Linear alkylbenzene sulfonate: sodium salt, Alcohol ethoxylate, Linear alkylbenzene sulfonate: MEA salt, sodium fatty acids, polyethyleneimine ethoxylate, diethylene glycol, propylene glycol, diquaternium ethoxysulfate, Borax, protease, polyethyleneimine ethoxylate propoxylate, ethanol, sodium cumene sulfonate, Amylase, citric acid, DTPA, disodium diaminostilbene disulfonate, sodium formate, calcium formate, dimethicone.

Tide Simply Clean & Fresh:

Water, alcohol ethoxylate sulfate, linear alkylbenzene sulfonate Sodium/Mea salts, propylene glycol, diethylene glycol, sodium formate, ethanol, borax, sodium fatty acids, fragrance, lauramine oxide, DTPA, Polyethylene amine ethoxylate, calcium formate, disodium diaminostilbene disulfonate, dimethicone, tetramine, Liquitint™ Blue. Tide Pods, Ocean Mist, Mystic Forest, Spring Meadow:

Linear alkylbenzene sulfonates, C12-16 Pareth-9, propylene glycol, alcoholethoxy sulfate, water, polyethyleneimine ethoxylate, glycerine, fatty acid salts, PEG-136 polyvinyl acetate, ethylene Diamine disuccinic salt, monoethanolamine citrate, sodium bisulfite, diethylenetriamine pentaacetate sodium, disodium distyrylbiphenyl disulfonate, calcium formate, mannanase, exyloglucanase, sodium formate, hydrogenated castor oil, natalase, dyes, termamyl, subtilisin, benzisothiazolin, perfume.

Tide to Go:

Deionized water, Dipropylene Glycol Butyl Ether, Sodium Alkyl Sulfate, Hydrogen Peroxide, Ethanol, Magnesium Sulfate, Alkyl Dimethyl Amine Oxide, Citric Acid, Sodium Hydroxide, Trimethoxy Benzoic Acid, Fragrance.

Tide Stain Release Liquid:

Water, Alkyl Ethoxylate, Linear Alkylbenzenesulfonate, Hydrogen Peroxide, Diquaternium Ethoxysulfate, Ethanolamine, Disodium Distyrylbiphenyl Disulfonate, tetrabutyl Ethylidinebisphenol, F&DC Yellow 3, Fragrance.

Tide Stain Release Powder:

Sodium percarbonate, sodium sulfate, sodium carbonate, sodium aluminosilicate, nonanoyloxy benzene sulfonate, sodium polyacrylate, water, sodium alkylbenzenesulfonate, DTPA, polyethylene glycol, sodium palmitate, amylase, protease, modified starch, FD&C Blue 1 , fragrance.

Tide Stain Release, Pre Treater Spray:

Water, Alkyl Ethoxylate, MEA Borate, Linear Alkylbenzenesulfonate, Propylene Glycol, Diquaternium Ethoxysulfate, Calcium Chlorideenzyme, Protease, Ethanolamine, Benzoisothiazolinone, Amylase, Sodium Citrate, Sodium Hydroxide, Fragrance.

Tide to Go Stain Eraser:

Water, Alkyl Amine Oxide, Dipropylene Glycol Phenyl Ether, Hydrogen Peroxide, Citric Acid, Ethylene Diamine Disuccinic Acid Sodium salt, Sodium Alkyl Sulfate, Fragrance.

Tide boost with Oxi:

Sodium bicarbonate, sodium carbonate, sodium percarbonate, alcohol ethoxylate, sodium chloride, maleic/acrylic copolymer, nonanoyloxy benzene sulfonate, sodium sulfate, colorant, diethylenetriamine pentaacetate sodium salt, hydrated aluminosilicate (zeolite), polyethylene glycol, sodium alkylbenzene sulfonate, sodium palmitate, starch, water, fragrance.

Tide Stain Release boost Duo Pac:

Polyvinyl Alcoholpouch film, wherein there is packed a liquid part and a powder part:

Liquid Ingredients: Dipropylene Glycol, diquaternium Ethoxysulfate, Water, Glycerin, LiquitintTM Orange, Powder Ingredients: sodium percarbonate, nonanoyloxy benzene sulfonate, sodium carbonate, sodium sulfate, sodium aluminosilicate, sodium polyacrylate, sodium alkylbenzenesulfonate, maleic/acrylic copolymer, water, amylase, polyethylene glycol, sodium palmitate, modified starch, protease, glycerine, DTPA, fragrance.

Tide Ultra Stain Release:

Water, sodium alcoholethoxy sulfate, linear alkyl benzene sulfonate, sodium/MEA salts, MEA citrate, propylene glycol, polyethyleneimine ethoxylate, ethanol, diethylene glycol, polyethyleneimine propoxyethoxylate, sodium fatty acids, protease, borax, sodium cumene sulfonate, DTPA, fragrance, amylase, disodium diaminostilbene disulfonate, calcium formate, sodium formate, gluconase, dimethicone, Liquitint™ Blue, mannanase.

Ultra Tide with a Touch of Downy ® Powdered Detergent, April Fresh/Clean Breeze/April Essence:

Sodium Carbonate, Sodium Aluminosilicate, Sodium Sulfate, Linear Alkylbenzene Sulfonate, Bentonite, Water, Sodium Percarbonate, Sodium Polyacrylate, Silicate, Alkyl Sulfate, Nonanoyloxybenzenesulfonate, DTPA, Polyethylene Glycol 4000, Silicone, Ethoxylate, fragrance, Polyethylene Oxide, Palmitic Acid, Disodium Diaminostilbene Disulfonate, Protease, Liquitint™ Red, FD&C Blue 1 , Cellulase.

Ultra Tide with a Touch of Downy Clean Breeze:

Water, sodium alcoholethoxy sulfate, MEA citrate, linear alkyl benzene sulfonate: sodium/MEA salts, propylene glycol, polyethyleneimine ethoxylate, ethanol, diethylene glycol, polyethyleneimine, propoxyethoxylate, diquaternium ethoxysulfate, alcohol sulfate, dimethicone, fragrance, borax, sodium fatty acids, DTPA, protease, sodium bisulfite, disodium diaminostilbene disulfonate, amylase, gluconase, castor oil, calcium formate, MEA, styrene acrylate copolymer, sodium formate, Liquitint™ Blue.

Ultra Tide with Downy Sun Blossom:

Water, sodium alcoholethoxy sulfate, MEA citrate, linear alkyl benzene sulfonate: sodium/MEA salts, propylene glycol, ethanol, diethylene glycol, polyethyleneimine propoxyethoxylate, polyethyleneimine ethoxylate, alcohol sulfate, dimethicone, fragrance, borax, sodium fatty acids, DTPA, protease, sodium bisulfite, disodium diaminostilbene disulfonate, amylase, castor oil, calcium formate, MEA, styrene acrylate copolymer, propanaminium propanamide, gluconase, sodium formate, Liquitint™ Blue.

Ultra Tide with Downy April Fresh/ Sweet Dreams:

Water, sodium alcoholethoxy sulfate, MEA citrate, linear alkyl benzene sulfonate: sodium/MEA salts, propylene glycol, polyethyleneimine ethoxylate, ethanol, diethylene glycol, polyethyleneimin propoxyethoxylate, diquaternium ethoxysulfate, alcohol sulfate, dimethicone, fragrance, borax, sodium fatty acids, DTPA, protease, sodium bisulfite, disodium diaminostilbene disulfonate, amylase, gluconase, castor oil, calcium formate, MEA, styrene acrylate copolymer, propanaminium propanamide, sodium formate, Liquitint™ Blue. Ultra Tide Free Powdered Detergent:

Sodium Carbonate, Sodium Aluminosilicate, Alkyl Sulfate, Sodium Sulfate, Linear Alkylbenzene Sulfonate, Water, Sodium polyacrylate, Silicate, Ethoxylate, Sodium percarbonate, Polyethylene Glycol 4000, Protease, Disodium Diaminostilbene Disulfonate, Silicone, Cellulase.

Ultra Tide Powdered Detergent, Clean Breeze/Spring Lavender/mountain Spring:

Sodium Carbonate, Sodium Aluminosilicate, Sodium Sulfate, Linear

Alkylbenzene Sulfonate, Alkyl Sulfate, Sodium Percarbonate, Water, Sodium Polyacrylate, Silicate, Nonanoyloxybenzenesulfonate, Ethoxylate, Polyethylene Glycol 4000, Fragrance, DTPA, Disodium Diaminostilbene Disulfonate, Palmitic Acid, Protease, Silicone, Cellulase.

Ultra Tide HE (high Efficiency) Pwdered Detergent, Clean Breeze:

Sodium Carbonate, Sodium Aluminosilicate, Sodium Sulfate, Linear

Alkylbenzene Sulfonate, Water, Nonanoyloxybenzenesulfonate, Alkyl Sulfate, Sodium Polyacrylate, Silicate, Sodium Percarbonate, Ethoxylate, Polyethylene Glycol 4000, Fragrance, DTPA, Palmitic Acid, Disodium Diaminostilbene Disulfonate, Protease, Silicone, Cellulase.

Ultra Tide Coldwater Powdered Detergent, Fresh Scent:

Sodium Carbonate, Sodium Aluminosilicate, Sodium Sulfate, Sodium Percarbonate, Alkyl Sulfate, Linear Alkylbenzene Sulfonate, Water, Nonanoyloxybenzenesulfonate, Sodium Polyacrylate, Silicate, Ethoxylate, Polyethylene Glycol 4000, DTPA, Fragrance, Natalase, Palmitic Acid, Protease, Disodium, Diaminostilbene Disulfonate, FD&C Blue 1 , Silicone, Cellulase, Alkyl Ether Sulfate.

Ultra Tide with bleach Powdered Detergent, Clean Breeze:

Sodium Carbonate, Sodium Aluminosilicate, Sodium Sulfate, Linear

Alkylbenzene Sulfonate, Sodium Percarbonate, Nonanoyloxybenzenesulfonate, Alkyl Sulfate, Water, Silicate, Sodium Polyacrylate, Ethoxylate, Polyethylene Glycol 4000, Fragrance, DTPA, Palmitic Acid, Protease, Disodium Diaminostilbene Disulfonate, Silicone, FD&C Blue 1 , Cellulase, Alkyl Ether Sulfate.

Ultra Tide with Febreeze Freshness™ Powdered Detergent, Spring Renewal:

Sodium Carbonate, Sodium Aluminosilicate, Sodium Sulfate, Linear

Alkylbenzene Sulfonate, Sodium Percarbonate , Alkyl Sulfate, Water, Sodium Polyacrylate, Silicate, Nonanoyloxybenzenesulfonate, Ethoxylate, Polyethylene Glycol 4000, DTPA, Fragrance, Cellulase, Protease, Disodium Diaminostilbene Disulfonate, Silicone, FD&C Blue 1.

Liquid Tide Plus with Febreeze Freshness - Sport HE Active Fresh:

Water, Sodium alcoholethoxy sulfate, MEA citrate, linear alkylbenzene sulfonate, sodium salt, linear alkylbenzene sulfonate: MEA salt, alcohol ethoxylate, sodium fatty acids, propylene glycol, diethylene glycol, polyethyleneimine ethoxylate propoxylate, diquaternium ethoxysulfate, Ethanol, sodium cumene sulfonate, borax, fragrance, DTPA, Sodium bisulfate, disodium diaminostilbene disulfonate, Mannanase, cellulase, amylase, sodium formate, calcium formate, Lauramine oxide, Liquitint™ Blue, Dimethicone / polydimethyl silicone.

Tide Plus Febreeze Freshness Spring & Renewal:

Water, sodium alcoholethoxy sulfate, linear alkyl benzene sulfonate: sodium/MEA salts, MEA citrate, propylene glycol, polyethyleneimine ethoxylate, fragrance, ethanol, diethylene glycol, polyethyleneimine propoxyethoxylate, protease, alcohol sulfate, borax, sodium fatty acids, DTPA, disodium diaminostilbene disulfonate, MEA, mannanase, gluconase, sodium formate, dimethicone, Liquitint™ Blue, tetramine.

Liquid Tide Plus with Febreeze Freshness, Sport HE Victory Fresh:

Water, Sodium alcoholethoxy sulfate, MEA citrate, linear alkylbenzene sulfonate, sodium salt, linear alkylbenzene sulfonate: MEA salt, alcohol ethoxylate, sodium fatty acids, propylene glycol, diethylene glycol, polyethyleneimine ethoxylate propoxylate, diquaternium ethoxysulfate, ethanol, sodium cumene sulfonate, borax, fragrance, DTPA, Sodium bisulfate, disodium diaminostilbene disulfonate, Mannanase, cellulase, amylase, sodium formate, calcium formate, Lauramine oxide, Liquitint™ Blue, Dimethicone / polydimethyl silicone.

Tide Vivid White + Bright Powder, Original:

Sodium Carbonate, Sodium Aluminosilicate, Sodium Sulfate, Linear Alkylbenzene Sulfonate, Sodium Percarbonate, Nonanoyloxybenzenesulfonate, Alkyl Sulfate, Water, Silicate, Sodium Polyacrylate Ethoxylate, Polyethylene Glycol 4000, Fragrance, DTPA, Palmitic Acid, Protease, Disodium Diaminostilbene Disulfonate, Silicone, FD&C Blue 1 , Cellulase, Alkyl Ether Sulfate.

Further cleaning composition that can be used in the present invention are the compositions disclosed in WO2013/184577 (Danisco US INC) page 83, line 32 to page 88, line 10.

ADW cleaning compositions

Any of the ADW cleaning compositions described below, may include one or more RNase and any number of additional enzymes. In general, the enzyme(s) should be compatible with the selected detergent, (e.g., with respect to pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, and the like), and the enzyme(s) should be present in effective amounts.

Finish all in 1 tabs (Reckit Benckiser)

Pentasodium triphosphate, sodium carbonate, sodium carbonate peroxide, aqua, 2- propenoic acid homopolymer (sodium salt, sulfonated), sodium bicarbonate, PEG MW>4100, PEG MW<4100, Cellulose, ceteareth-25, dimethicone, taed, citric acid, sodium sulfate, fatty alcohol alkoxylate, tetrasodium etidronate, glycerol, starch, subtilisin, Mangan Oxalate, titanium dioxide, Methyl-1 H-benzotriazole, magnesium stearate, Primary alcohol ethoxylate, limonene, amylase, parfum, colorant. Finish Quantum tabs (Reckit Benckiser)

Pentasodium triphosphate, polyvinylalcohol, sodium carbonate, sodium carbonate peroxide, 2- propenoic acid homopolymer (sodium salt, sulfonated), fatty alcohol alkoxylate, aqua, PEG MW>4100, tetrasodium etidronate, taed, sodium sulfate, PEG MW<4100, sorbitol, trimethylolpropane, sodium chloride, methyl alcohol, cellulose, dimethicone, Methyl-1 H- benzotriazole, subtilisin, titanium dioxide, manganese oxalate (dihydrate), 2-Propenoic acid homopolymer, (sodium salt), C12-13 PARETH-6, citric acid, stereamide, petroleum distillates, Fatty acid; C16-18; Calcium salts, amylase, polyethilenimine, calcium carbonate, Fatty acid; C16- 18; Zinc salts, STEARETH-21 , Diallyldimethylammonium Chloride, Parfum, colorant. ADW Model detergent

Sodium carbonate, sodium citrate, sodium carbonate peroxide, polycarboxylate, taed, non-ionic surfactant, sodium disilicate, peg-75 and vegetable oil.

Assay

Assay I

Mini Launder-O-Meter (MiniLOM) Model Wash System

MiniLOM is a modified mini wash system of the Launder-O-Meter (LOM), which is a medium scale model wash system that can be applied to test up to 20 different wash conditions simultaneously. A LOM is basically a large temperature controlled water bath with 20 closed metal beakers rotating inside it. Each beaker constitutes one small washing machine and during an experiment, each will contain a solution of a specific detergent/enzyme system to be tested along with the soiled and unsoiled fabrics it is tested on. Mechanical stress is achieved by the beakers being rotated in the water bath and by including metal balls in the beaker.

The LOM model wash system is mainly used in medium scale testing of detergents and enzymes at European wash conditions. In a LOM experiment, factors such as the ballast to soil ratio and the fabric to wash liquor ratio can be varied. Therefore, the LOM provides the link between small scale experiments, such as AMSA and mini-wash, and the more time consuming full scale experiments in front loader washing machines. In miniLOM, washes are performed in 50 ml test tubes placed in Stuart rotator.

Delta remission value (ARem): The terms“Delta remission” or“Delta remission value” are defined herein as the result of a reflectance or remission measurement at a certain wavelength which typically is 460 nm. The swatch is measured with one swatch of similar colour as background, preferably a swatch from a repetition wash. A swatch representing each swatch type is measured before the wash. The Delta remission is the remission value of the washed swatch minus the remission value of the unwashed swatch.

Assay II: Testing of RNase activity RNase activity was determined by fluorescence using a fluorescence-quenched oligonucleotide probe. This probe emits a signal after nuclease degradation according to the manual from the supplier (RNase alert kit, Integrated DNA Technology, Coralville, Iowa, USA). Briefly, RNase was diluted in water hardness 15°dH to obtain a concentration of 2ppm, and 5mI of the substrate was added to 95mI of the RNase sample. A kinetic curve was measured for 10min at 22°C using a Clariostar microplate reader (excitation 490nm, emission at 520nm).

Table 1 : Enzyme activity at 2ppm (RFU after 10min).

Example 1

Cotton swatches are cut out of armpits of a white t-shirt. The swatches are placed in 50 ml. test tubes and 10 mL of wash liquor (15°dH water) with 3.33 g/L Ariel Actilift (liquid) and the 5 pg/ml enzyme (polypeptide of SEQ ID NO: 15) are added to each tube. Washes without enzyme are included as controls. The test tubes are placed in a Stuart rotator (as described under MiniLOM) and incubated for 1 hour at 30°C and 20 rpm. The wash liquor is then removed, and the swatches are rinsed twice with 15°dH water and dried on filter paper over night. The swatches are evaluated after wash and show improved whiteness of the swatches.

Ariel Actilift (liquid): 5-15% Anionic surfactants; <5% Non-ionic surfactants, Phosphonates, Soap; Enzymes, Optical brighteners, Benzisothiazolinone, Methylisothiazolinone, Perfumes, Alpha-isomethyl ionone, Citronellol, Geraniol, Linalool. Example 2

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 1 and cleaning composition Tide TOTALCARE™ Liquid, Cool Cotton. The swatches are evaluated after wash and show improved removal RNA and RNA components.

Tide TOTALCARE™ Liquid, Cool Cotton: water, alcoholethoxy sulfate, propylene glycol, sodium fatty acids, laurtrimonium chloride, ethanol, sodium hydroxide, sodium cumene sulfonate, citric acid, ethanolamine, diethylene glycol, silicone polyether, borax, fragrance, polyethyleneimine ethoxylate, protease, Laureth-9, DTPA, polyacrylamide quaternium chloride, disodium diaminostilbene disulfonate, sodium formate, Liquitint™ Orange, dipropylethyl tetraamine, dimethicone, cellulase.

Example 3

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 17 and cleaning composition Persil Small & Mighty (liquid). The swatches are evaluated after wash and show improved whiteness of the swatches.

Persil Small & Mighty (liquid): 15-30% Anionic surfactants, Non-ionic surfactants, 5-15% Soap, < 5% Polycarboxylates, Perfume, Phosphates, Optical Brighteners.

Example 4

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 20 and cleaning composition Gain Liquid, Original. The swatches are evaluated after wash and show reduced amount of malodour adhered the swatches.

Gain Liquid, Original: Water, Alcohol Ethoxysulfate, Diethylene Glycol, Alcohol Ethoxylate, Ethanolamine, Linear Alkyl Benzene Sulfonate, Sodium Fatty Acids, Polyethyleneimine Ethoxylate, Citric Acid, Borax, Sodium Cumene Sulfonate, Propylene Glycol, DTPA, Disodium Diaminostilbene Disulfonate, Dipropylethyl Tetramine, Sodium Hydroxide, Sodium Formate, Calcium Formate, Dimethicone, Amylase, Protease, Liquitint™, Hydrogenated Castor Oil, Fragrance.

Example 5

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 3 and cleaning composition Fairy Non Bio (liquid). The swatches are evaluated after wash and show reduced amount of RNA and RNA components on the swatches.

Fairy Non Bio (liquid): 15-30% Anionic Surfactants, 5-15% Non-Ionic Surfactants, Soap, Benzisothiazolinone, Methylisothiazolinone, Perfumes. Example 6

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO:

26 and cleaning composition Hey sport tex wash. The swatches are evaluated after wash and show reduced adherence of soil to the swatches

Hey sport tex wash: Aqua, dodecylbenzenesulfonsaure, laureth-1 1 , peg-75 lanolin, propylene glycol, alcohol denatured, potassium soyate, potassium hydroxide, disodium cocoamphodiacetate, ethylendiamine triacetate cocosalkyl acetamide, parfum, zinc ricinoleate, sodium chloride, benzisothiazolinone, methylisothiazolinone, ci 16255, benzyl alcohol.

Example 7

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO:

27 and cleaning composition Ariel Sensitive White & Color (liquid). The swatches are evaluated after wash and show improved whiteness of the swatches.

Ariel Sensitive White & Color (liquid): Aqua, Alcohol Ethoxy Sulfate, Alcohol Ethoxylate, Amino Oxide, Citrid Acid, C12-18 topped palm kernel fatty acid, Protease, Glycosidase, Amylase, Ethanol, 1 ,2 Propanediol, Sodium Formate, Calcium Chloride, Sodium hydroxide, Silicone Emulsion, Trans-sulphated EHDQ.

Example 8

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 11 and cleaning composition WFK IEC-A model detergent (powder). The swatches are evaluated after wash and show reduced stickiness of the swatches.

WFK IEC-A model detergent (powder): Linear sodium alkyl benzene sulfonate 8,8 %, Ethoxylated fatty alcohol C12-18 (7 EO) 4,7 %, Sodium soap 3,2 %, Anti foam DC2-4248S 3,9 %, Sodium aluminium silicate zeolite 4A 28,3 %, Sodium carbonate 1 1 ,6 %, Sodium salt of a copolymer from acrylic and maleic acid (Sokalan CP5) 2,4 %, Sodium silicate 3,0 %, Carboxymethylcellulose 1 ,2 %, Dequest 2066 2,8 %, Optical whitener 0,2 %, Sodium sulfate6,5 %, Protease 0,4 %.

Example 9

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 7 and cleaning composition Ariel Actilift Colour&Style (liquid). The swatches are evaluated after wash and show reduced adherence of soil.

Ariel Actilift Colour&Style (liquid): 5-15% Anionic surfactants; <5% Non-ionic surfactants, Phosphonates, Soap; Enzymes, Perfumes, Benzisothiazolinone, Methylisothiazolinone, Alpha- isomethyl ionone, Butylphenyl methylpropional, Citronellol, Geraniol, Linalool. Example 10

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 4 and cleaning composition Ariel Actilift Colour&Style (powder). The swatches are evaluated after wash and show reduced stickiness of the swatches.

Ariel Actilift Colour&Style (powder): 15-30% Anionic surfactants, <5% Non-ionic surfactants, Phosphonates, Polycarboxylates, Zeolites; Enzymes, Perfumes, Hexyl cinnamal.

Example 11

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 33 and cleaning composition Persil Biological Powder. The swatches are evaluated after wash and show improved whiteness of the swatches.

Persil Biological Powder: Sucrose, Sorbitol, Aluminum Silicate, Polyoxymethylene Melamine, Sodium Polyaryl Sulphonate, Cl 61585, Cl 45100, Lipase, Amylase, Xanthan gum, Hydroxypropyl methyl cellulose, Cl 12490, Disodium Distyrylbiphenyl Disulfonate, Sodium Thiosulfate, Cl 42090, Mannanase, Cl 1 1680, Etidronic Acid, Tetrasodium EDTA.

Example 12

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 23 and cleaning composition Persil Colour Care Biological Tablets. The swatches are evaluated after wash and show improved removal of RNA and RNA components from the swatches.

Persil Colour Care Biological Tablets: Sodium bicarbonate, Sodium carbonate, Zeolite, Aqua, Sodium Silicate, Sodium Lauryl Sulfate, Cellulose Gum, Sodium Dodecylbenzenesulfonate, Lauryl Glucoside, Sodium chloride, Sodium Acrylic Acid/MA Copolymer, Parfum, Sodium Thioglycolate, PVP, Sodium sulfate, Tetrasodium Etidronate, Sodium Polyacrylate, Dimethicone, Bentonite, Dodecylbenzene Sulfonic Acid, Trimethylsiloxysilicate, Calcium carbonate, Cellulose, PEG-75, Titanium dioxide, Dextrin, Protease, Corn Starch Modified, Sucrose, Sodium Thiosulfate, Amylase, Cl 74160, Kaolin.

Example 13

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 9 and cleaning composition Tide Liquid, Original. The swatches are evaluated after wash and show reduced reduced adherence of soil to the swatches.

Tide Liquid, Original: Linear alkylbenzene sulfonate, propylene glycol, citric acid, sodium hydroxide, borax, ethanolamine, ethanol , alcohol sulfate, polyethyleneimine ethoxylate, sodium fatty acids, diquaternium ethoxysulfate, protease, diethylene glycol, laureth-9, alkyldimethylamine oxide, fragrance, amylase, disodium diaminostilbene disulfonate, DTPA, sodium formate, calcium formate, polyethylene glycol 4000, mannanase, Liquitint™ Blue, dimethicone. Example 14

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 14 and cleaning composition Liquid Tide HE, Original Scent. The swatches are evaluated after wash and show improved whiteness of the swatches.

Liquid Tide HE, Original Scent: Water, Sodium alcoholethoxy sulfate, MEA citrate, Sodium Alkyl Sulfate, alcohol ethoxylate, linear alkylbenzene sulfonate, MEA salt, sodium fatty acids, polyethyleneimine ethoxylate, diethylene glycol, propylene glycol, diquaternium ethoxysulfate, borax, polyethyleneimine, ethoxylate propoxylate, ethanol, sodium cumene sulfonate, fragrance, DTPA, disodium diaminostilbene disulfonate, Mannanase, cellulase, amylase, sodium formate, calcium formate, Lauramine oxide, Liquitint™ Blue, Dimethicone / polydimethyl silicone.

Example 15

The washing experiment of example 1 is repeated with the polypeptide of SEQ ID NO: 32 and cleaning composition Biotex black (liquid). The swatches are evaluated after wash and show reduced malodor of the swatches.

Biotex black (liquid): 5-15% Anionic surfactants, <5% Nonionic surfactants, perfume, enzymes, DMDM and hydantoin.

Example 16

A wash and wear trial to evaluate the benefit of RNase enzyme (SEQ ID NO 34) on real laundry items was carried out with voluntary participants. In total, 13 males and 7 females, took part in this trial. All participants were given two identical T-shirts (ID Active Game T-shirts, white, product number 0570 (male model) or 0571 (female model). The participants were asked to use the items for similar heavy exercise (running, fitness, biking, etc.) before handing the T-shirts back for washing. After the T-shirts had been washed they were handed back to participants for another round of exercise. This process was carried out for up to 15 cycles. Two of the males had two sets of T-shirts, giving a total of 22 sets of T-shirts in this trial.

Washing was carried out in Miele W 1935 WTL EU front-loader washing machines. For each participant, one T-shirt was continuously throughout all wash cycles washed with addition of 1 ppm RNase enzyme, the other T-shirt was continuously washed without addition of RNase as a control. The detergent used in this trial was a European commercial liquid detergent, Domol Colorwaschmittel supplied directly by the manufacturer (Nopa Nordic). Washing was carried out with the following conditions: 30°C, cotton program, short cycle (total program time 1 h49min), tap water. Detergent was added to a wash concentration of approx. 3 g/L. 5 g soil from the grounds around Bagsvaerd, Denmark was added to each washing machine to promote visualization of body soil and dinginess in the T-shirts. T-shirts were line-dried after wash. Following the last wash cycle, all T-shirts were washed once more as described above, however without RNase addition and instead of soil addition, 26 g wfk 09 V pigment soil (wfk Testgewebe GmbH) was added to further enhance visualization of body soil.

Following the final wash, T-shirts were evaluated by a panel of 5 panelists. For each set of T-shirts (washed with RNase or without RNase), the panelists were asked to decide on which T-shirt they preferred. Results are listed in Table 2. The table indicates which T-shirt in each set the panel overall preferred.

Table 2. Preference data for T-shirts in wash and wear trial with RNase enzyme.

As seen from the results, for 14 of the T-shirt sets, the panelists generally preferred the T-shirt washed with RNase added to the wash. For 6 of the T-shirt sets, the panelists generally preferred the T-shirt washed without RNase added to the wash. And for 2 of the T-shirt sets, there was no clear preference towards any of the two T-shirts. Taken together, out of 22 T-shirt sets, a benefit was observed on 14 T-shirt sets, while for only 6 sets, the benefit was observed on the T-shirt washed without RNase enzyme. This is a significant result that will not likely occur by pure chance which demonstrates that RNase enzyme reduces the level of dinginess in real items over multiple wash cycles.