The present invention is directed towards a process for making a powder or granule containing

(A) at least one chelating agent selected from alkali metal salts of methyl glycine diacetic ac id (MGDA) and of glutamic acid diacetate (GLDA) and of iminodisuccinic acid (IDS),

(B) at least one enzyme

in a weight ratio of (A):(B) of from 5 : 1 up to 1 ,000:1 ,

wherein said powder or granule contains at least 75% by weight of chelating agent (A), said process comprising the steps of

(a) mixing the at least one chelating agent (A) and the at least one enzyme (B) in the pres ence of water, thereby forming a solution or slurry,

(b) removing most of said water by spray-drying or spray granulation using a gas with an in let temperature of at least 125°C.

In addition, the present invention is directed towards powders and granules containing a chelat ing agent (A) and an enzyme (B), and to methods of use of such powders and granules.

Chelating agents of the aminopolycarboxylate type such as methyl glycine diacetic acid (MGDA) and glutamic acid diacetic acid (GLDA) and their respective alkali metal salts are useful seques- trants for alkaline earth metal ions such as Ca ²⁺ and Mg ²⁺ . A lot of aminopolycarboxylates show good biodegradability and are thus environmentally friendly. For that reason, they are recom mended and used for various purposes such as laundry detergents and for automatic dishwash ing (ADW) formulations, in particular for so-called phosphate-free laundry detergents and phos phate-free ADW formulations.

Depending on the type of product - liquid home care and fabric care products versus solid home care and fabric care products - and the manufacturing process of solid home care and fabric care products care product manufacturers may either prefer to handle solutions of ami- nocarboxylates or solid arminocarboxylates, for example joint spray drying or solid mixing. Powders and granules of aminocarboxylates may be shipped economically due to their high active ingredient content that goes along with low water content. Therefore, convenient pro cesses for providing granules are still of great commercial interest.

In WO 2009/103822, a process is disclosed in which slurries are granulated that have a certain solids content, with a gas inlet temperature of 120°C or less. In WO 2012/168739, a process is disclosed wherein slurries of complexing agents are spray-dried under non-agglomerating con ditions.

The removal of organic materials such as milk, blood, and especially of egg residues from both dishware and fibers is best facilitated by the addition of an enzyme or a combination of enzymes to the respective detergent formulation. However, degradation of enzymes is attributed to a loss of activity of detergent compositions after some time of storage or even during manufacture.

Without wishing to be bound to any theory it is believed that strong complexing agents may ex tract the central Ca ²⁺ metal ion(s) of the active site(s) of detergent proteases and amylases, thus, reduce the activity of said enzymes.

It was therefore an objective of the present invention to provide a component of detergent com positions that facilitates both removal of organic materials from fibers and dishware and allows only reduced spotting.

Accordingly, the process and granules and powders defined at the outset have been found, hereinafter also referred to as inventive process and inventive granules, respectively.

The inventive process comprises several steps that may be referred to as step (a) or step (b) etc. and that will be explained in more detail below.

The inventive process is a process for making a powder or granule, said powders and granules also being referred to as inventive powders and inventive granules, respectively. In the context of the present invention, the term“powder” refers to particulate materials that are solids at am bient temperature and that preferably have an average particle diameter in the range of from 30 pm to less than 0.1 mm, preferably 30 pm up to 75 pm. The average particle diameter of in ventive powders can be determined, e.g., by LASER diffraction methods, for example with Mal vern apparatus, and refers to the volume average.

The term“granule” in the context of the present invention refers to particulate materials that are solids at ambient temperature and that preferably have an average particle diameter (D50) in the range of from 0.1 mm to 2 mm, preferably 0.4 mm to 1.25 mm, even more preferably 400 pm to 1 mm. The average particle diameter of inventive granules can be determined, e.g., by optical or preferably by sieving methods. Sieves employed may have a mesh in the range of from 60 to 3,000 pm. In one embodiment of the present invention, inventive powders or inventive granules have a broad particle diameter distribution. In another embodiment of the present invention, inventive powders or inventive granules have a narrow particle diameter distribution. The particle diame ter distribution can be adjusted, if desired, by multiple sieving steps.

Granules and powders made by the inventive process may contain residual moisture, moisture referring to water including water of crystallization and adsorbed water. The amount of water may be in the range of from 0.1 to 20% by weight, preferably 1 to 15% by weight, referring to the total solids content of the respective powder or granule, and may be determined by Karl- Fischer-titration or by drying at 160°C to constant weight with infrared light.

Particles of powders and granules made by the inventive process may have regular or irregular shape. Preferred shapes of particles of powders and of granules made by the inventive process are spheroidal shapes.

Particles of powders or granules made by the inventive process contain at least one chelating agent, hereinafter also referred to as chelating agent (A). Chelating agent (A) is selected from alkali metal salts of methyl glycine diacetic acid (MGDA) and glutamic acid diacetate (GLDA) and iminodisuccinic acid (IDS).

Alkali metals of MGDA are selected from compounds according to general formula (I a)

[CH ₃ -CH(COO)-N(CH ₂ -COO) ₂ ]M _3-X H (l a) wherein

M is selected from alkali metal cations, same or different, for example cations of lithium, sodium, potassium, rubidium, cesium, and combinations of at least two of the foregoing. Preferred ex amples of alkali metal cations are sodium and potassium and combinations of sodium and po tassium.

The variable x in formula (la) may be in the range of from zero to 1 .0, preferred are 0.01 to 0.5 and even more preferred from 0.01 to 0.25. In particularly preferred embodiments, x is from 0.02 to 0.2 or from 0.1 to 0.3.

The variable z in formula (I a) may be in the range of from zero to 1 .0, preferred are 0.01 to 0.5. zero < x + y < 1 .0. However, the sum of x+z in formula (I a) is preferably greater than zero, for example 0.05 to 0.6.

Examples of M _3-X H _X are Na _3-X H _X , [Na ₀ 7(NH ₄ )o3]3- _x H _x , [(NH ₄ )o7Na ₀ 3]3- _x H _x , (Ko ₇ Nao3)3- _x H _x ,

(Nao Kos _x H _x , (Ko ₂₂ Na ₀₇₈ ) _3-x H _x , (Na ₀₂₂ K ₀₇₈ ) _3-x H _x , and K _3-X H _X . Preferred examples of M _3-X H _X are selected from Na ₃ , Na _3.x H _x, Na K, K ₂ Na, Na2e5K ₀₃ 5, K2e5Nao ₃ 5, K ₃ , (KossNaois _x H _x , and

(Nao ₈₅ Ko ₁₅ ) _3-x H _x .

Alkali metals of GLDA are selected from compounds according to general formula (I b)

[OOC-CH ₂ CH ₂ C-CH(COO)-N(CH ₂ -COO) ₂ ]M _4-X H (l b) wherein

M is selected from alkali metal cations, same or different, as defined above, x in formula (I b) is in the range of from zero to 2.0, preferred are zero to 0.5. In a particularly preferred embodiment, x is zero.

The variable x in formula (I b) may be in the range of from zero to 2.0, preferred are 0.02 to 0.5. In particularly preferred embodiments, x is from 0.1 to 0.3.

The variable z in formula (I b) may be in the range of from zero to 1.0, preferred are 0.01 to 0.5. Furthermore, zero < x + y < 1.0.

Preferably, the sum of x+z in formula (I b) is greater than zero, for example 0.05 to 0.6.

Examples of M _4-X H _X are Na _.x H _x , Na, 7Na ₀ 3] _4-x H _x , (Ko7Na ₀ 3) ₄ -xHx, (Na ₀ 7Ko3) ₄ -xHx, (K ₀₂₂ N Preferred examples of M _4-X H _X are selected from ₀ 6 ₅ Na ₃₃ 5, K ₄ ,

(Ko ₈₅ Na _0i5 ) _4-x H _x , and (Nao ₈₅ Koi ₅ ) _4-x H _x .

Compounds according to general formulae (I a) and (I b) with x bigger than zero, e.g., 0.02 < x < 0.5, may be obtained, e.g., by saponification of the respective nitrile precursors with a shortcut of alkali metal hydroxide or by subsequent addition of an acid, for example a mineral acid such as sulfuric acid, or an organic acid such as, but not limited to citric acid, tartaric acid, formic ac id, acetic acid, with formic acid and citric acid being preferred. Alkali metals of IDS are selected from compounds according to general formula (I c)

[H-N-(CH(COO)-CH ₂ COO) ₂ ]M4- _X H _X (I c) wherein

M is selected from alkali metal cations, same or different, as defined above, x in formula (I c) is in the range of from zero to 2.0, preferred are zero to 0.5, preferred are 0.02 to 0.5. In particularly preferred embodiments, x is from 0.1 to 0.3.

In one embodiment of the present invention, alkali metal salts of MGDA are selected from lithi um salts, potassium salts and preferably sodium salts of MGDA. MGDA can be partially or pref erably fully neutralized with the respective alkali. In a preferred embodiment, an average of from 2.7 to three COOH groups of MGDA is neutralized with alkali metal, preferably with sodium. In a particularly preferred embodiment, chelating agent (A) is the trisodium salt of MGDA.

MGDA and its respective alkali metal salts are selected from the racemic mixtures, the D- isomers and the L-isomers, and from mixtures of the D- and L-isomers other than the racemic mixtures. Preferably, MGDA and its respective alkali metal salts are selected from the racemic mixture and from mixtures containing in the range of from 55 to 85 mole-% of the L-isomer, the balance being D-isomer. Particularly preferred are mixtures containing in the range of from 60 to 80 mole-% of the L-isomer, the balance being D-isomer. Other particularly preferred embodi ments are racemic mixtures.

GLDA and its respective alkali metal salts are selected from the racemic mixtures, the D- isomers and the L-isomers, and from mixtures of the D- and L-isomers other than the racemic mixtures. Preferably, GLDA and its respective alkali metal salts are selected from the racemic mixture and from mixtures containing in the range of from 55 to 99 mole-% of the L-isomer, the balance being D-isomer. Particularly preferred are mixtures containing in the range of from 60 to 98.5 mole-% of the L-isomer, the balance being D-isomer. Other particularly preferred embodi ments are racemic mixtures.

IDS and its respective alkali metal salts are selected from various mixtures of isomers, for ex ample D,D-IDS, L,L-IDS and D,L-IDS and combinations therefrom. Preferred are optically inac tive mixtures since they are cheaper to be manufactured. In any way, minor amounts of chelating agent (A) may bear a cation other than alkali metal. It is thus possible that minor amounts, such as 0.01 to 5 mol-% of total MGDA, GLDA or IDS, re spectively, bear alkali earth metal cations such as Mg ²⁺ or Ca ²⁺ , or an Fe ²⁺ or Fe ³⁺ cation.

In one embodiment of the present invention, alkali metal salt of chelating agent (A) may contain one or more impurities that may result from the synthesis of the respective chelating agent (A). In the cases of MGDA and GLDA and their alkali metal salts, such impurities may be selected from propionic acid, lactic acid, alanine, nitrilotriacetic acid (NTA) or the like and their respective alkali metal salts. In the case of IDS, such impurities may be selected from maleic acid, mono amides of maleic/fumaric acid, and racemic asparagine. Such impurities are usually present in minor amounts.“Minor amounts” in this context refer to a total of 0.1 to 5% by weight, referring to alkali metal salt of chelating agent (A), preferably up to 2.5% by weight. In the context of the present invention, such minor amounts are neglected when determining the composition of granule made according to the inventive process.

In a special embodiment of the present invention, a combination alkali metal salts of at least two different chelating agents is used, for example sodium salts of MGDA and GLDA in a weight ratio of from 1 :1 to 5:1 . In other embodiments, alkali metal salts of only one chelating agent is used, in particular sodium metal salts of MGDA.

Particles of powders or granules made by the inventive process further contain

(B) at least one enzyme, hereinafter also referred to as enzyme (B), for example hydrolase (B). Enzyme (B) may be selected from cellulases, licheninases, pektinases, and man- nanases. Preferred enzymes (B) are selected from proteases, amylases, and lipases, hereinafter also referred to as proteases (B), amylases (B), or lipases (B), respectively.

Amounts of enzyme (B) refer to active mass, that is without, e.g. stabilizers or inactive impuri ties.

It has been found that enzymes (B) in inventive granules and powders exhibit a particularly good life-time. Enzymes (B) that are particularly beneficial in inventive granules and powders are sele3cted from hydrolases (EC 3). Preferred enzymes (B) are selected from the group of enzymes acting on ester bond (E.C. 3.1 ), glycosylases (E.C. 3.2), and peptidases (E.C. 3.4). Enzymes acting on ester bond (E.C. 3.1 ), hereinafter also refer to lipases (B), respectively. Gly cosylases (E.C. 3.2) hereinafter also refer to either amylases (B) and cellulases (B). Peptidases hereinafter also refer to peptidases (B). Lichenases and mannanases hereinafter also may be referred to as lichenases (B) and mannanases (B); respectively. Hydrolases (B) in the context of the present invention are identified by polypeptide sequences, also called amino acid sequences herein. The polypeptide sequence specifies the three- dimensional structure including the“active site” of an enzyme which in turn determines the cata lytic activity of the same. Polypeptide sequences may be identified by a SEQ ID NO. According to the World Intellectual Property Office (WIPO) Standard ST.25 (1998) the amino acids herein are represented using three-letter code with the first letter as a capital or the corresponding one letter.

Enzymes (B) in the context of the present invention may relate to parent enzymes and/or variant enzymes, both having enzymatic activity. Enzymes having enzymatic activity are enzymatically active or exert enzymatic conversion, meaning that enzymes act on substrates and convert these into products. The term“enzyme” herein excludes inactive variants of an enzyme.

A“parent” sequence of a parent protein or enzyme, also called“parent enzyme” is the starting sequence for introduction of changes, e.g., by introducing one or more amino acid substitutions, insertions, deletions, or a combination thereof to the sequence, resulting in“variants” of the par ent sequences. The term parent enzyme (or parent sequence) includes wild-type enzymes (se quences) and synthetically generated sequences (enzymes) which are used as starting se quences for introduction of (further) changes.

The term“enzyme variant” or“sequence variant” or“variant enzyme” refers to an enzyme that differs from its parent enzyme in its amino acid sequence to a certain extent. If not indicated otherwise, variant enzyme“having enzymatic activity” means that this variant enzyme has the same type of enzymatic activity as the respective parent enzyme.

In describing the variants of the present invention, the nomenclature described as follows is used:

Amino acid substitutions are described by providing the original amino acid of the parent en zyme followed by the number of the position within the amino acid sequence, followed by the substituted amino acid.

Amino acid deletions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by ^* .

Amino acid insertions are described by providing the original amino acid of the parent enzyme followed by the number of the position within the amino acid sequence, followed by the original amino acid and the additional amino acid. For example, an insertion at position 180 of lysine next to glycine is designated as“Gly180Glyl_ys” or“G180GK”. In cases where a substitution and an insertion occur at the same position, this may be indicated as S99SD+S99A or in short S99AD. In cases where an amino acid residue identical to the exist ing amino acid residue is inserted, it is clear that degeneracy in the nomenclature arises. If for example a glycine is inserted after the glycine in the above example this would be indicated by G180GG.

Where different alterations can be introduced at a position, the different alterations are separat ed by a comma, e.g.“Arg170Tyr, Glu” represents a substitution of arginine at position 170 with tyrosine or glutamic acid. Alternatively different alterations or optional substitutions may be indi cated in brackets e.g. Arg170[Tyr, Gly] or Arg170{Tyr, Gly}; or in short R170 [Y,G] or R170 {Y, G}; or in long R170Y, R170G.

Enzyme variants may be defined by their sequence identity when compared to a parent en zyme. Sequence identity usually is provided as“% sequence identity” or“% identity”. For calcu lation of sequence identities, in a first step a sequence alignment has to be produced. According to this invention, a pairwise global alignment has to be produced, meaning that two sequences have to be aligned over their complete length, which is usually produced by using a mathemati cal approach, called alignment algorithm.

In the context of the present invention, the alignment is generated by using the algorithm of Needleman and Wunsch (J. Mol. Biol. 1979 48 p. 443-453). Preferably, the program“NEEDLE” (The European Molecular Biology Open Software Suite (EMBOSS)) is used for the purposes of the current invention, with using the programs default parameter (gap open=10.0, gap ex- tend=0.5 and matrix=EBLOSUM62). According to this invention, the following calculation of %- identity applies: %-identity = (identical residues / length of the alignment region which is show ing the respective sequence of this invention over its complete length)· 100.

In the context of the present invention, enzyme variants may be described as an amino acid sequence which is at least n% identical to the amino acid sequence of the respective parent enzyme with“n” being an integer between 10 and 100. In one embodiment, variant enzymes are at least 70%, at least 75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical when compared to the full length amino acid sequence of the parent enzyme, wherein the enzyme variant has enzymatic activity. Enzyme variants may be defined by their sequence similarity when compared to a parent en zyme. Sequence similarity usually is provided as“% sequence similarity” or“%-similarity”. % sequence similarity takes into account that defined sets of amino acids share similar properties, e.g by their size, by their hydrophobicity, by their charge, or by other characteristics. Herein, the exchange of one amino acid with a similar amino acid may be called“conservative mutation”.

For determination of %-similarity according to this invention the following applies: amino acid A is similar to amino acids S; amino acid D is similar to amino acids E and N; amino acid E is simi lar to amino acids D and K and Q; amino acid F is similar to amino acids W and Y; amino acid H is similar to amino acids N and Y; amino acid I is similar to amino acids L and M and V; amino acid K is similar to amino acids E and Q and R; amino acid L is similar to amino acids I and M and V; amino acid M is similar to amino acids I and L and V; amino acid N is similar to amino acids D and H and S; amino acid Q is similar to amino acids E and K and R; amino acid R is similar to amino acids K and Q; amino acid S is similar to amino acids A and N and T ; amino acid T is similar to amino acids S; amino acid V is similar to amino acids I and L and M; amino acid W is similar to amino acids F and Y; amino acid Y is similar to amino acids F and H and W. Conservative amino acid substitutions may occur over the full length of the sequence of a poly peptide sequence of a functional protein such as an enzyme. In one embodiment, such muta tions are not pertaining the functional domains of an enzyme. In one embodiment, conservative mutations are not pertaining the catalytic centers of an enzyme.

To take conservative mutations into account, a value for sequence similarity of two amino acid sequences may be calculated from the same alignment, which is used to calculate %-identity. According to this invention, the following calculation of %-similarity applies: %-similarity = [(iden tical residues + similar residues) / length of the alignment region which is showing the respec tive sequence(s) of this invention over its complete length]· 100.

In the context of the present invention, enzyme variants may be described as an amino acid sequence which is at least m% similar to the respective parent sequences with“m” being an integer between 10 and 100. In one embodiment, variant enzymes are at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when com pared to the full length polypeptide sequence of the parent enzyme, wherein the variant enzyme has enzymatic activity.

“Enzymatic activity” means the catalytic effect exerted by an enzyme, which usually is ex pressed as units per milligram of enzyme (specific activity) which relates to molecules of sub strate transformed per minute per molecule of enzyme (molecular activity). Variant enzymes may have enzymatic activity according to the present invention when said en zyme variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the enzymatic activity of the respective parent enzyme.

In one embodiment, inventive powders and inventive granules comprise at least one protease (B). Enzymes (B) having proteolytic activity are called“proteases” or peptidases in the context of the present invention. Such enzymes are members of class EC 3.4.

Proteases (B) are further classified as aminopeptidases (EC 3.4.1 1 ), dipeptidases (EC 3.4.13), dipeptidyl-peptidases and tripeptidyl-peptidases (EC 3.4.14), peptidyl-dipeptidases (EC 3.4.15), serine-type carboxypeptidases (EC 3.4.16), metallocarboxypeptidases (EC 3.4.17), cysteine- type carboxypeptidases (EC 3.4.18), omega peptidases (EC 3.4.19), serine endopeptidases (EC 3.4.21 ), cysteine endopeptidases (EC 3.4.22), aspartic endopeptidases (EC 3.4.23), metal- lo-endopeptidases (EC 3.4.24), threonine endopeptidases (EC 3.4.25), or endopeptidases of unknown catalytic mechanism (EC 3.4.99).

Protease (B) may be an endopeptidase of any kind or a mixture of endopeptidases of any kind. In one embodiment, protease according to the invention is selected from serine protease (EC 3.4.21 ).

Serine proteases or serine peptidases are characterized by having a serine in the catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction. A ser ine protease in the context of the present invention is selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1 ), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71 ), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21.79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.1 18, or EC 3.4.21.1 19,) plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5), and subtilisin. Subtilisin is also known as subtilopepti- dase, e.g., EC 3.4.21.62, the latter hereinafter also being referred to as“subtilisin”.

Crystallographic structures of proteases (B) show that the active site is commonly located in a groove on the surface of the molecule between adjacent structural domains, and the substrate specificity is governed by the properties of binding sites arranged along the groove on one or both sides of the catalytic site that is responsible for hydrolysis of the scissile bond. Accordingly, the specificity of protease (B) can be described by use of a conceptual model in which each specificity subsite is able to accommodate the sidechain of a single amino acid residue. The sites are numbered from the catalytic site, S1 , S2...Sn towards the N-terminus of the substrate, and ST, S2'...Sn' towards the C-terminus. The residues they accommodate are numbered P1 , P2...Pn, and PT, P2'...Pn', respectively:

In this representation the catalytic site of the enzyme is marked“ ^* ” and the peptide bond cleaved (the scissile bond) is indicated by the symbol“+”.

In general, the three main types of protease activity (proteolytic activity) are: trypsin-like, where there is cleavage of amide substrates following Arg (N) or Lys (K) at P1 , chymotrypsin-like where cleavage occurs following one of the hydrophobic amino acids at P1 , and elastase-like with cleavage following an Ala (A) at P1 .

A sub-group of the serine proteases tentatively designated as subtilases has been proposed by Siezen et al. (1991 ), Protein Eng. 4:719-737 and Siezen et al. (1997), Protein Science 6:501 - 523. They are defined by homology analysis of more than 170 amino acid sequences of serine proteases previously referred to as subtilisin-like proteases. A subtilisin was previously often defined as a serine protease produced by Gram-positive bacteria or fungi, and according to Siezen et al. now is a subgroup of the subtilases. A wide variety of subtilases have been identi fied, and the amino acid sequence of a number of subtilases has been determined. For a more detailed description of such subtilases and their amino acid sequences reference is made to Siezen et al. (1997), Protein Science 6:501 -523. 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.

A subgroup of the subtilases are the subtilisins which are serine proteases from the family S8 as defined by the MEROPS database (http://merops.sanger.ac.uk). Peptidase family S8 con tains the serine endopeptidase subtilisin and its homologues. In subfamily S8A, the active site residues frequently occur in the motifs Asp-Thr/Ser-Gly similarly to the sequence motif in fami lies of aspartic endopeptidases in clan AA, His-Gly-Thr-His and Gly-Thr-Ser-Met-Ala-Xaa-Pro. Prominent members of family S8, subfamily A are:

The subtilisin related class of serine proteases shares a common amino acid sequence defining a catalytic triad which distinguishes them from the chymotrypsin related class of serine proteas es. Subtilisins and chymotrypsin related serine proteases both have a catalytic triad comprising aspartate, histidine and serine.

In subtilisin related proteases (B) the relative order of these amino acids, reading from the ami no to carboxy-terminus is aspartate-histidine-serine. In the chymotrypsin related proteases the relative order, however is histidine-aspartate-serine. Thus, subtilisin herein refers to a serine protease having the catalytic triad of subtilisin related proteases. Examples include the subtil isins as described in WO 89/06276 and EP 0283075, WO 89/06279, WO 89/09830, WO

89/09819, WO 91/06637 and WO 91/02792.

Parent proteases of the subtilisin type (EC 3.4.21.62) and variants may be bacterial proteases. Said bacterial protease may be a Gram-positive bacterial polypeptide such as a Bacillus, Clos tridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococ cus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, llyobacter, Neis seria, Pseudomonas, Salmonella, or Ureaplasma protease. They act as unspecific endopepti- dases, i.e. they hydrolyze any peptide bonds.

Commercially available protease enzymes include those sold under the trade names Alcalase®, Blaze®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Pri- mase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Co- ronase® Ultra, Neutrase®, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect® Prime, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Eraser®, Ultimase®, Opticlean®, Effectenz®, Preferenz® and Optimase® (Danisco/DuPont), Axapem™ (Gist-Brocases N.V.), Bacillus lentus Alkaline Protease (BLAP; sequence shown in Figure 29 of US 5,352,604) and variants thereof and KAP ( Bacillus alkalophilus subtilisin) from Kao.

In one aspect of the invention, the parent enzymes and variants may be a Bacillus alcalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagu- lans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacil lus subtilis, or Bacillus thuringiensis protease.

In one embodiment of the present invention, the subtilase is selected from the following:

• subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J.

Bacteriol. Volume 159, p. 81 1 -819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 1 1 , p. 791 1 -7925),

• subtilisin from Bacillus licheniformis (subtilisin Carlsberg; disclosed in EL Smith et al.

(1968) in J. Biol Chem, Volume 243, pp. 2184-2191 , and Jacobs et al. (1985) in Nucl. Acids Res, Vol 13, p. 8913-8926),

• subtilisin PB92 (original sequence of the alkaline protease PB92 is described in EP

283075 A2),

• subtilisin 147 and/or 309 (Esperase®, Savinase®) as disclosed in GB 1243784,

• subtilisin from Bacillus lentus as disclosed in WO 91/02792, such as from Bacillus lentus

DSM 5483 or the variants of Bacillus lentus DSM 5483 as described in WO 95/23221 ,

• subtilisin from Bacillus alcalophilus (DSM 1 1233) disclosed in DE 10064983,

• subtilisin from Bacillus gibsonii (DSM 14391 ) as disclosed in WO 2003/054184,

• subtilisin from Bacillus sp. (DSM 14390) disclosed in WO 2003/056017,

• subtilisin from Bacillus sp. (DSM 14392) disclosed in WO 2003/055974,

• subtilisin from Bacillus gibsonii (DSM 14393) disclosed in WO 2003/054184,

• subtilisin having SEQ ID NO: 4 as described in WO 2005/063974 or a subtilisin which is at least 40% identical thereto and having proteolytic activity,

• subtilisin having SEQ ID NO: 4 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity,

• subtilisin having SEQ ID NO: 7 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity, and

• subtilisin having SEQ ID NO: 2 as described in application DE 102005028295.4 or subtil isin which is this at least 66% identical thereto and having proteolytic activity. Examples of useful proteases (B) in accordance with the present invention comprise the vari ants described in: WO 92/19729, WO 95/23221 , WO 96/34946, WO 98/201 15, WO 98/201 16, WO 99/1 1768, WO 01/44452, WO 02/088340, WO 03/006602, WO 2004/03186, WO

2004/041979, WO 2007/006305, WO 201 1 /036263, WO 201 1 /036264, and WO 201 1/072099. Suitable examples comprise especially protease variants of subtilisin protease derived from SEQ ID NO:22 as described in EP 1921 147 (which is the sequence of mature alkaline protease from Bacillus lentus DSM 5483) with amino acid substitutions in one or more of the following positions: 3, 4, 9, 15, 24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101 , 102, 103,

104, 106, 1 18, 120, 123, 128, 129, 130, 131 , 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and 274 (according to the BPN' numbering), which have proteolytic activity. In one embodiment, such a subtilisin protease is not mutated at posi tions Asp32, His64 and Ser221 (according to BPN’ numbering).

In one embodiment, subtilisin has SEQ ID NO:22 as described in EP 1921 147, or a subtilisin which is at least 80% identical thereto and has proteolytic activity. In one embodiment, a subtil isin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by having amino acid glutamic acid (E), or aspartic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity. In one embodiment, subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by having amino acid glutamic acid (E), or aspartic acid (D), at position 101 (according to BPN’ numbering) and has proteolytic activity. Such a subtilisin variant may comprise an amino acid substitution at position 101 , such as R101 E or R101 D, alone or in combination with one or more substitutions at positions 3, 4, 9, 15, 24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101 , 102, 103, 104, 106, 1 18, 120, 123, 128, 129, 130, 131 , 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and/or 274 (according to BPN’ numbering) and has proteolytic activity.

In another embodiment, a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising at least the following amino acids (according to BPN’ numbering) and has proteolytic activity:

(a) threonine at position 3 (3T)

(b) isoleucine at position 4 (4I)

(c) alanine, threonine or arginine at position 63 (63A, 63T, or 63R)

(d) aspartic acid or glutamic acid at position 156 (156D or 156E)

(e) proline at position 194 (194P)

(f) methionine at position 199 (199M) (g) isoleucine at position 205 (205I)

(h) aspartic acid, glutamic acid or glycine at position 217 (217D, 217E or 217G),

(i) combinations of two or more amino acids according to (a) to (h).

In another embodiment, a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising one amino acid (according to (a)-(h)) or combi nations according to (i) together with the amino acid 101 E, 101 D, 101 N, 101 Q, 101 A, 101 G, or 101 S (according to BPN’ numbering) and has proteolytic activity.

In one embodiment, a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising the mutation (according to BPN’ numbering)

R101 E, or S3T + V4I + V205I, or S3T + V4I + V199M + V205I + L217D and has proteolytic ac tivity.

In another embodiment, the subtilisin comprises an amino acid sequence having at least 80% identity to SEQ ID NO:22 as described in EP 1921 147 and being further characterized by com prising R101 E and S3T, V4I, and V205I (according to the BPN’ numbering) and has proteolytic activity.

In another embodiment, a subtilisin comprises an amino acid sequence having at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and being further characterized by comprising R101 E, and one or more substitutions selected from the group consisting of S156D, L262E, Q137H, S3T, R45E,D,Q, P55N, T58W,Y,L, Q59D,M,N,T, G61 D,R, S87E, G97S, A98D,E,R, S106A,W, N1 17E, H120V,D,K,N, S125M, P129D, E136Q, S144W, S161 T,

S163A,G, Y171 L, A172S, N185Q, V199M, Y209W, M222Q, N238H, V244T, N261 T,D and L262N,Q,D (as described in WO 2016/09671 1 and according to the BPN’ numbering), and has proteolytic activity.

Percentage-identity for subtilisin variants is calculated as disclosed above. Subtilisin variant enzymes as disclosed above which are at least n% identical to the respective parent sequences include variants with n being at least 40 to 100. Depending on the %-identity values applicable as provided above, subtilisin variants in one embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme.

In another embodiment, the invention relates to subtilisin variants comprising conservative mu tations not pertaining the functional domain of the respective subtilisin protease. Depending on the %-identity values applicable as provided above, subtilisin variants of this embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.

Proteases (B), including serine proteases, according to the invention have“proteolytic activity” or“protease activity”. This property is related to hydrolytic activity of a protease (proteolysis, which means hydrolysis of peptide bonds linking amino acids together in a polypeptide chain) on protein containing substrates, e.g. casein, hemoglobin and BSA. Quantitatively, proteolytic activity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a defined course of time. The methods for analyzing proteolytic activity are well-known in the liter ature (see e.g. Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60: 381 -395). Proteolytic activity as such can be determined by using Succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF; see e.g. DelMar et al. (1979), Analytical Biochem 99, 316-320) as substrate. pNA is cleaved from the substrate molecule by proteolytic cleavage, resulting in release of yellow color of free pNA which can be quantified by measuring OD405.

Protease variants may have proteolytic activity when said protease variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the proteolytic activity of the respective parent protease.

Preferably, the pi value (isoelectric point) of subtilisin protease used in the present invention is in the range of from pH 7.0 to pH 10.0, preferably from pH 8.0 to pH 9.5.

Lipases and cutinases

In one embodiment, inventive powders and inventive granules comprise at least one lipase (B). “Lipases”,“lipolytic enzyme”,“lipid esterase”, all refer to an enzyme of EC class 3.1.1 (“carbox ylic ester hydrolase”). Such an enzyme (B) may have lipase activity (or lipolytic activity; triacyl- glycerol lipase, EC 3.1 .1 .3), cutinase activity (EC 3.1 .1 .74; enzymes having cutinase activity may be called cutinase herein), sterol esterase activity (EC 3.1 .1 .13) and/or wax-ester hydro lase activity (EC 3.1 .1 .50). Lipases include those of bacterial or fungal origin. Commercially available lipase (B) include but are not limited to those sold under the trade names Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (Gist-Brocades/ now DSM).

In one aspect of the invention, a suitable lipase is selected from the following:

• lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa (T. lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. insolens as described in WO 96/13580,

• lipases derived from Phizomucor miehei as described in WO 92/05249.

• lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. from P. alcaligenes or P. pseudoalcaligenes (EP 218272, WO 94/25578, WO 95/30744, WO 95/35381 , WO 96/00292), P. cepacia (EP 331376), P. stutzeri (GB 1372034), P. fiuorescens, Pseudomonas sp. strain SD705 (WO 95/06720 and WO 96/27002), P. wis- consinensis (WO 96/12012), Pseudomonas mendocina (WO 95/14783), P. glumae (WO 95/35381 , WO 96/00292)

• lipase from Streptomyces griseus (WO 201 1/150157) and S. pristinaespiralis (WO

2012/137147), GDSL-type Streptomyces lipases (WO 2010/065455),

• lipase from Thermobifida fusca as disclosed in WO 201 1/084412,

• lipase from Geobacillus stearothermophilus as disclosed in WO 201 1 084417,

• Bacillus lipases, e.g. as disclosed in WO 00/60063, lipases from B. subtilis as disclosed in

Dartois et al. (1992), Biochemica et Biophysica Acta, 1 131 , 253-360 or WO

201 1/084599, B. stearothermophilus (JP S64-074992) or B. pumilus (WO 91/16422).

• Lipase from Candida antarctica as disclosed in WO 94/01541 .

• cutinase from Pseudomonas mendocina (US 5389536, WO 88/09367)

• cutinase from Magnaporthe grisea (WO 2010/107560),

• cutinase from Fusarum solani pisi as disclosed in WO 90/09446, WO 00/34450 and WO

01/92502

• cutinase from Humicola lanuginosa as disclosed in WO 00/34450 and WO 01/92502

Suitable lipases (B) also include those referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO 2010/1 1 1 143), acyltrans- ferase from Mycobacterium smegmatis (WO 2005/056782), perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant (WO 2010/100028).

Suitable lipases include also those which are variants of the above described lipases and/or cutinases which have lipolytic activity. Such suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105. Suitable lipases/cutinases (B) include also those that are variants of the above described lipas- es/cutinases which have lipolytic activity. Suitable lipase/cutinase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the par ent enzyme as disclosed above. In one embodiment lipase/cutinase variants having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least

92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent en zyme as disclosed above.

In another embodiment, inventive powders and inventive granules comprise at least one li pase/cutinase variant comprising conservative mutations not pertaining the functional domain of the respective lipase/cutinase. Lipase/cutinase variants of such embodiments having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least

92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.

Lipases (B) have“lipolytic activity”. The methods for determining lipolytic activity are well-known in the literature (see e.g. Gupta et al. (2003), Biotechnol. Appl. Biochem. 37, p. 63-71 ). E.g. the lipase activity may be measured by ester bond hydrolysis in the substrate para-nitrophenyl pal- mitate (pNP-Palmitate, C:16) and releases pNP which is yellow and can be detected at 405 nm.

Lipase variants may have lipolytic activity according to the present invention when said lipase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the lipolytic activity of the re spective parent lipase.

In one embodiment of the present invention, a combination of at least two of the foregoing li pases (B) may be used.

Lipase (B) may be used in its non-purified form or in a purified form, e.g. purified with the aid of well-known adsorption methods, such as phenyl sepharose adsorption techniques.

In one embodiment of the present invention, lipases (B) are included in inventive powders and inventive granule in such an amount that a finished inventive powders and inventive granule has a lipolytic enzyme activity in the range of from 100 to 0.005 LU/mg, preferably 25 to 0.05 LU/mg of the composition. A Lipase Unit (LU) is that amount of lipase which produces 1 pmol of titrata- ble fatty acid per minute in a pH stat. under the following conditions: temperature 30° C.;

pH=9.0; substrate is an emulsion of 3.3 wt. % of olive oil and 3.3% gum arabic, in the presence of 13 mmol/l Ca ²⁺ and 20 mmol/l NaCI in 5 mmol/l Tris-buffer.

In one embodiment of the present invention, proteases (B) are included in inventive powders and inventive granule in such an amount that an inventive powder or inventive granule, respec tively, has a proteolytic enzyme activity in the range of from 0.1 to 50 GU.

It is preferred to use a combination of lipase (B) and protease (B) in inventive powder or in ventive granule, respectively, for example 1 to 2% by weight of protease (B) and 0.1 to 0.5% by weight of lipase (B).

In the context of the present invention, an enzyme (B) is called stable when its enzymatic activi ty“available in application” equals 100% when compared to the initial enzymatic activity before storage. An enzyme may be called stable within this invention if its enzymatic activity available in application is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% when compared to the initial enzymatic activity before storage.

In one embodiment, lipolytic activity available after storage at 37°C for 30 days is at least 60% when compared to the initial lipolytic activity before storage.

Subtracting a% from 100% gives the“loss of enzymatic activity during storage” when compared to the initial enzymatic activity before storage. In one embodiment, an enzyme is stable accord ing to the invention when essentially no loss of enzymatic activity occurs during storage, i.e. loss in enzymatic activity equals 0% when compared to the initial enzymatic activity before stor age. Essentially no loss of enzymatic activity within this invention may mean that the loss of enzymatic activity is less than 30%, less than 25%, less than 20%, less than 15%, less than 10%, less than 9%, less than 8%, less than 7%, less than 6%, less than 5%, less than 4%, less than 3%, less than 2%, or less than 1 % when compared to the initial enzymatic activity before storage.

In one embodiment, the loss of lipolytic activity after storage at 37°C for 30 days is less than 40% when compared to the initial lipolytic activity before storage. Reduced loss of enzymatic activity within this invention may mean that the loss of enzymatic activity is reduced by at least 5%, by at least 10%, by at least 15%, by at least 20%, by at least 25%, by at least 30%, by at least 40%, by at least 50%, by least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% when compared to the initial enzymatic activity before storage.

In one embodiment of the present invention enzyme (B) is used in combination with serine pro tease inhibitors known per se. Examples of serine protease inhibitors are boric acid, a borate, or another boronic acid derivative or a peptide aldehyde. The inhibitor may have an inhibition con stant to a serine protease Ki (M, mol/L) of 1 E-12-1 E-03; more preferred 1 E-1 1 -1 E-04; even more preferred: 1 E-10-1 E-05; even more preferred 1 E-10-1 E-06; most preferred 1 E-09-1 E-07.

It is preferred, though, to use enzyme (B) in inventive formulations without boron based inhibi tors.

Mixing of chelating agent (A) and enzyme (B) is usually performed in the presence of water.

Said mixing can be conducted in a way that an aqueous solution or slurry of enzyme (B) and an aqueous solution of chelating agent (A) are being combined in a vessel, preferably under stir ring. It is also possible to combine an aqueous solution of enzyme (B) and solid chelating agent (A), or to combine an aqueous solution of chelating agent (A) with solid enzyme (B), or to com bine aqueous slurries of chelating agent (A) and enzyme (B) and then dilute it with water. In an alternative embodiment, water is provided and subsequently, enzyme (B) and then chelating agent (A) are added. In a preferred embodiment, a solution of chelating agent (A) is provided that has a temperature of 4 to 50°C, for example 4 to 10°C or 35 to 50°C, and enzyme (B) is added, either in bulk or as solution.

The resultant aqueous formulation is preferably in the form of a slurry or solution, solutions be ing preferred.

In preferred embodiments, step (a) is being performed at 10 to 30°C. Step (a) may be per formed at ambient temperature. Temperatures of 65°C or more instep (a) may lead to a degra dation of enzyme (B).

The water used in step (a) may be present in an amount that both chelating agent (A) and en zyme (B) are dissolved. However, it is also possible to use less amounts of water and mix che lating agent (A) and enzyme (B) in a way that a slurry is being formed, with the continuous phase having the appearance of a solution. Solutions are preferred. In one embodiment of the present invention, the total solids content of such solution or slurry formed as result of step (a) is in the range of from 20 to 75%, preferably 35 to 50%.

In one embodiment of the present invention, such solution or slurry has a pH value in the range of from 2.5 to 13, preferably from 7 to 13 and even more preferably at least 8.

Mixing may be performed with mechanical support, for example shaking or stirring.

In step (b), a spray-drying or spray granulation is performed, using a gas with an inlet tempera ture of at least 125°C. Said gas, hereinafter also being referred to as“hot gas”, may be nitrogen, a rare gas or preferably air. In the course of step (b), most of the water used in step (a) will be removed, for example at least 55%, preferably at least 65% of the water. In one embodiment of the present invention, 99% of the water at most will be removed.

Spray-drying and spray granulation will be described in more detail below.

The aqueous slurry or aqueous solution according to step (a) may have a temperature in the range of from 4 to 95°C, preferably 4 to 10 or 20 to 90°C and even more preferably 50 to 90°C.

In step (b), said aqueous slurry or aqueous solution is introduced into a spray tower or spray granulator. A spray granulator usually contains a fluidized bed, in the context of the present in vention it is a fluidized bed of chelating agent (A) or of inventive granule. Such fluidized bed of chelating agent is preferably in the form of chelating agent in crystalline form, for example in at least 66% crystalline form, determined by X-Ray diffraction. In one embodiment of the present invention, the fluidized bed may have a temperature in the range of from 80 to 150°C, preferably 85 to 1 10°C. Spray towers usually do not contain any fluidized bed. The gas used for fluidization is the gas inlet stream, It may have a temperature in the range of from 125 to 250°C, preferably 160 to 220°C.

Spraying is being performed through one or more nozzles per spray tower or spray granulator. Suitable nozzles are, for example, high-pressure atomizers, rotary atomizers, three-fluid noz zles, single-fluid nozzles and two-fluid nozzles, single-fluid nozzles and two-fluid nozzles being preferred. The first fluid is the aqueous slurry or aqueous solution, respectively, the second fluid is compressed gas, for example with a pressure of 1.1 to 7 bar. Said compressed gas may have a temperature in the range of from ambient temperature to 100°C.

In step (b), the aqueous slurry or aqueous solution of complexing agent (A) is introduced in the form of droplets. In one embodiment of the present invention, the droplets formed during the spray-granulating or spray-drying have an average diameter in the range of from 10 to 500 pm, preferably from 20 to 180 pm, even more preferably from 30 to 100 pm.

In one embodiment of the present invention, the off-gas departing the spray tower or spray granulator, respectively, may have a temperature in the range of from 40 to 140°C, preferably 80 to 1 10°C but in any way colder than the hot gas stream. Preferably, the temperature of the off-gas departing the drying vessel and the temperature of the solid product present in the dry ing vessel are identical.

In one embodiment of the present invention, the pressure in the spray tower or spray granulator in step (b) is normal pressure ± 100 mbar, preferably normal pressure ± 20 mbar, for example one mbar less than normal pressure.

In one embodiment of the present invention, especially in a process for making an inventive granule, the average residence time of chelating agent (A) in step (b) is in the range of from 2 minutes to 4 hours, preferably from 30 minutes to 2 hours.

In another embodiment of the present invention, spray-granulation is being performed by per forming two or more consecutive spray-drying processes, for example in a cascade of at least two spray dryers, for example in a cascade of at least two consecutive spray towers or a combi nation of a spray tower and a spray chamber, said spray chamber containing a fluidized bed. In the first dryer, a spray-drying process is being performed in the way as follows.

Spray-drying may be preferred in a spray dryer, for example a spray chamber or a spray tower. An aqueous slurry or solution with a temperature preferably higher than ambient temperature, for example in the range of from 4 to 95°C, preferably from 4 to 10 or 20 to 90°C is introduced into the spray dryer through one or more spray nozzles into a hot gas inlet stream, for example nitrogen or air, the solution or slurry being converted into droplets and the water being vapor ized. The hot gas inlet stream may have a temperature in the range of from 125 to 350°C. The second spray dryer is charged with a fluidized bed with solid from the first spray dryer and solu tion or slurry obtained according to the above step is sprayed onto or into the fluidized bed, to gether with a hot gas inlet stream. The hot gas inlet stream may have a temperature in the range of from 125 to 350°C, preferably 160 to 220°C.

In embodiments wherein an aged slurry is used, such aging may take in the range of from 2 hours to 24 hours at the temperature preferably higher than ambient temperature. In the course of step (b), most of the water is removed. Most of the water shall mean that a re sidual moisture content of 0.1 to 20% by weight, referring to the powder or granule, remains. in embodiments that start of from a solution, about 51 to 75% by weight of the water present in the aqueous solution is removed in step (b).

A powder or granule is obtained.

In one embodiment of the inventive process, the inventive process may contain further steps, for example separating off fines or lumps, milling down lumps, and/or returning fines and milled down lumps into the inventive process, for example by directly returning them into a spray gran ulator - or dissolving them in water and then spray-drying.

Such optional additional steps are hereinafter also referred to step (c) and they are briefly dis cussed hereinafter.

At the end of step (b), powder or granule, respectively, is removed from the spray tower or spray granulator. Said powder or granule has been at least partially formed in the course of step (b) of the inventive process. Said removal may be performed through one or more openings in the spray tower or spray granulator. Preferably, such one or more openings are at the bottom of the respective spray tower or spray granulator. Powder or granules, respectively, are removed including fines and lumps.

In embodiments in which a powder is made preferably 70 to 95% by weight of the solid formed are withdrawn from the spray tower per hour. In embodiments in which a granule is made, 20 to 60 % of the fluidized bed are withdrawn per hour, for example with an extruder screw. Additional solids, especially fines, may be collected in the off-gas purification.

In one embodiment of the inventive process, in the course of step (c) fines may be separated off from said powder or granules, wherein said fines have a maximum particle diameter of 350 pm. Preferably, fines in processes wherein granules are desired may have a particles diameter in the range of from 1 to 150 pm. The act of separating off the fines may be performed by sieving or by air classification, preferably by sieving.

In embodiments wherein spray-drying is performed, fines have a particles diameter of 30 pm or less, for example 1 to 30 pm.

In one embodiment of the present invention, in step (b) 40 to 100% of the fines present in the respective material withdrawn at the end of step (b) are separated off. In a preferred embodi- merit, in step (c) 80 to 99% by weight of the fines are separated off, and the residual 1 to 20% are left in the respective powder or granule. It is tedious to try to remove the fines quantitatively.

In step (c) of the inventive process, so-called lumps or“overs” may be separated off from said powder or granules.

In embodiments wherein granules are desired, said lumps to be separated off are particles that have a minimum particle diameter of 1 ,000 pm, for example, 1 ,500 pm to 2 mm or even more.

In a preferred embodiment, lumps are particles that have a minimum particle diameter of 1 ,250 pm or more, even more preferably 900 pm to 2 mm.

In embodiments wherein powders are desired, said lumps or overs have a minimum particle diameter of 250 pm or more, for example 250 to 1 ,000 pm.

Overs or lumps may be removed, e.g., with the help of a discharge screw or a rotary valve, usually together with desired product, and then classified.

It is observed that in connection with the recycling, the smaller the maximum size of the lumps to be separated off in step (c) the better the hygroscopicity behavior of the later chelating agent, and the better the peroxide stability.

Separating off lumps and fines may be performed in any order, consecutively or simultaneously.

In one embodiment of the present invention, the amount of powder or granule, respectively, other than fines and overs is in the range of from 55 to 70% by weight, referring to total amount of material removed at the end of step (b).

The lumps separated of in step (c) may be milled down to a smaller size, for example to maxi mum particle diameter of 500 pm, preferably to a maximum particle diameter of 400 pm. The milling may be performed in any type of mills. Examples of particularly useful mills are jet mills, pin mills and bolting machines (German: StiftmGhlen). Further examples are roller mills and ball mills.

In one embodiment, said fines from step (c) and milled lumps from step (c) are reintroduced into a spray-dryer or spray-granulator. Such reintroducing may be performed by pneumatically transporting said fines milled lumps from step (c) into the spray tower or spray granulator, re spectively, preferably through an extra opening rather than together with solution or slurry from step (a). The share of fines withdrawn in step (c) may be in the range of from 0.5 to 20 % by weight of the total chelating agent (A) withdrawn in step (b), preferably 4 to 18 % by weight. The share of lumps is in the range of from 5 to 60% by weight of the total chelating agent (A) withdrawn in step (b), preferably 20 to 40% by weight and even more preferably 25 to 35 % by weight. With a higher share of lumps, the inventive process becomes economically unfavorable because it is too much recycling. With a lower share of lumps the hygroscopicity may become too high.

By performing the inventive process, powders and granules may be obtained. Such powders and granules have a particularly high bulk (German: Schuttdichte), density, for example 650 to 900g/l, preferred are 700 to 870 g/l, as determined according to DIN ISO 697.

In one embodiment of the present invention, the inventive process furnishes a granule, and the inventive process comprises a subsequent step (d) comprising coating the resultant granule with an organic polymer.

Suitable organic polymers are selected from water-soluble polymers, for example polyethylene glycol, homo- and copolymers of acrylic acid, as free acids or partially or fully neutralized with alkali, for example with Na ⁺ .

Suitable polyethylene glycols are preferably solid at ambient temperature. Suitable polyethylene glycols may have an average molecular weight M _n in the range of from 2,000 to 10,000 g/mol, preferred are 2,500 to 7,000 g/mole.

Suitable homo- and copolymers of (meth)acrylic acid have an average molecular weight M _w in the range of from 1 ,200 to 30,000 g/mol, preferably from 2,500 to 15,000 g/mol and even more preferably from 3,000 to 10,000 g/mol, determined by gel permeation chromatography (GPC) and referring to the respective free acid.

Useful copolymers of (meth)acrylic acid are, for example, random copolymers of acrylic acid and methacrylic acid, random copolymers of acrylic acid and maleic anhydride, ternary random copolymers of acrylic acid, methacrylic acid and maleic anhydride, random or block copolymers of acrylic acid and styrene, random copolymers of acrylic acid and methyl acrylate. More pre ferred are homopolymers of methacrylic acid. Even more preferred are homopolymers of acrylic acid.

Said coating step may be performed in a mixer or in a fluidized bed, a fluidized bed being pre ferred. Preferred vessels are equipped with Wurster tubes. In one embodiment of step (d), a coating liquor, for example a solution or slurry of water soluble polymer is sprayed on a fluidized bed of granule or powder made in accordance with steps (a) and (b) and, optionally, step (c) according to the inventive process. For such spraying, one-fluid nozzles or two-fluid nozzles may be used, with two-fluid nozzles being preferred. The spraying may be performed from top or from bottom, so-called bottom-spray being preferred. As spray gas, inert gasses such as nitrogen or noble gasses may be applied or - preferably - air.

In one embodiment of the present invention, step (d) is performed with a one-fluid-nozzle or preferably a two-fluid nozzle with a pressure in the range of from 1 .1 to 10 bar, even more pre ferred from 1.5 to 4 bar.

In one embodiment of the present invention, the temperature of the spray gas in step (d) is in the range of from 20 to 150°C, preferably 25 to 60°C.

As solvent for the water-soluble polymer, water is preferred but organic solvents and mixtures of organic solvents and water are feasible as well. A suitable organic solvent is ethanol.

The amount of water-soluble polymer used in step (d) may be in the range of from 0.1 to 50% by weight, preferably 0.5 to 30% by weight and even more preferably from 1 to 15% by weight, referring to the amount of (A).

Said coating liquor may be free from inorganic materials. In other embodiments, coating liquor used in step (d) may contain one or more inorganic material, for example a pigment. Preferred pigments are selected from colorless (“white”) pigments, e.g., titanium dioxide (C.l. Pigment White 6), zinc white, pigment grade zinc oxide; zinc sulfide, lithopone; lead white, furthermore white fillers such as barium sulfate and CaC0 ₃ which are also referred to as inorganic white pigments in the context of the present invention, especially titanium dioxide, Ti0 ₂ . Such pigment may have an average particle diameter (D50) in the range of from 20 nm to 50 pm, preferably in the range from 50 nm to 20 pm, more preferably to a maximum of 5 pm and even more prefera bly from 0.1 to 1 pm, measured, e.g., by Coulter counter or with a Hegman gauge.

A further aspect of the present invention is related to granules and powders, hereinafter also referred to as inventive granules and inventive powders, respectively. Inventive powders and inventive granules contain (A) at least one chelating agent selected from methyl glycine diacetic acid (MGDA) and glutam ic acid diacetate (GLDA) and iminodisuccinic acid (IDS) and their respective alkali metal salts,

(B) at least one enzyme

in a weight ratio of (A):(B) of from 5 : 1 up to 1 ,000:1 , wherein chelating agent (A) and enzyme (B) are uniformly distributed in said powder or granule, and wherein said powder or granule contains at least 75% by weight of chelating agent (A), the per centage referring to the solids content of said powder or granule.

In the context of the present invention, the term“uniformly distributed” implies that all or a vast majority, for example at least 80% of the particles of inventive powder and of inventive granules contain chelating agent (A) and enzymes (B). The term“uniformly distributed” implies as well that chelating agent (A) and enzymes (B) are distributed over the diameter of the particle in an almost homogeneous way.

In a preferred embodiment of the present invention, the weight ratio of (A)/(B) is in the range of from 10:1 to 100:1. In this weight ratio, impurities of chelating agent (A) that stem from the syn thesis, see above, are neglected.

In one embodiment of the present invention, inventive powders are selected from powders hav ing an average particle diameter in the range of from 1 pm to less than 0.1 mm.

In one embodiment of the present invention, inventive granules are selected from granules with an average particle diameter in the range of from 0.1 mm to 2 mm, preferably 0.75 mm to 1.25 mm.

In one embodiment of the present invention, inventive powder or inventive granule contains in the range of from 80 to 99 % by weight chelating agent (A) and 1 to 2 % by weight enzyme(s) (B), percentages referring to the solids content of said powder or granule.

Inventive powders and inventive granules exhibit overall advantageous properties including but not limited to an excellent yellowing behavior, especially in the presence of bleaching agents. They are therefore excellently suitable for the manufacture of cleaning agents that contain at least one bleaching agent, such cleaning agent hereinafter also being referred to as bleach. In particular, inventive powders and inventive granules are suitable for the manufacture of cleaning agent for fibers or hard surfaces.

Inventive granules and especially inventive powders may easily be converted into compactates and into agglomerates.

Another aspect of the present invention is therefore the use of an inventive powder or an in ventive granule according for the manufacture of a cleaning agent that contains at least one bleaching agent, and in particular for the manufacture of cleaning agent for fibers or hard sur faces, wherein said cleaning agent contains at least one peroxy compound. Another aspect of the present invention is a process for making at a cleaning agent by combining at least one in ventive powder or at least one inventive granule with at least one bleaching agent, preferably at least one peroxy compound. Another aspect of the present invention is a cleaning agent, here inafter also being referred to as inventive cleaning agent.

Inventive cleaning agents may contain at least one bleaching agent and at least one inventive powder or at least one inventive granule. Inventive cleaning agents show a reduced tendency for yellowing and therefore have an extended shelve-life.

Examples of suitable peroxy compounds are sodium perborate, anhydrous or for example as monohydrate or as tetrahydrate or so-called dihydrate, sodium percarbonate, anhydrous or, for example, as monohydrate, hydrogen peroxide, persulfates, organic peracids such as peroxylau- ric acid, peroxystearic acid, peroxy-a-naphthoic acid, 1 ,12-diperoxydodecanedioic acid, per- benzoic acid, peroxylauric acid, 1 ,9-diperoxyazelaic acid, diperoxyisophthalic acid, in each case as free acid or as alkali metal salt, in particular as sodium salt, also sulfonylperoxy acids and cationic peroxy acids.

In a preferred embodiment, peroxy compound is selected from inorganic percarbonates, persul fates and perborates. Examples of sodium percarbonates are 2 Na ₂ C0 ₃ -3 H ₂ 0 ₂ . Examples of sodium perborate are (Na ₂ [B(0H) ₂ (0 ₂ )] ₂ ), sometimes written as NaB0 ₂ O ₂ -3H ₂ 0 instead. Most preferred peroxy compound is sodium percarbonate.

The term“cleaning agents” includes compositions for dishwashing, especially hand dishwash and automatic dishwashing and ware-washing, and compositions for hard surface cleaning such as, but not limited to compositions for bathroom cleaning, kitchen cleaning, floor cleaning, de scaling of pipes, window cleaning, car cleaning including truck cleaning, furthermore, open plant cleaning, cleaning-in-place, metal cleaning, disinfectant cleaning, farm cleaning, high pressure cleaning, and in addition, laundry detergent compositions. Such cleaning agents may be liquids, gels or preferably solids at ambient temperature, solids cleaning agents being preferred. They may be in the form of a powder or in the form of a unit dose, for example as a tablet.

In one embodiment of the present invention, inventive cleaning agents may contain

in the range of from 2 to 50 % by weight of inventive powder or inventive granule,

in the range of from 0.5 to 15 % by weight of bleach.

Percentages are based on the solids content of the respective inventive cleaning agent.

Inventive cleaning agents may contain further ingredients such as one or more surfactants that may be selected from non-ionic, zwitterionic, cationic, and anionic surfactants. Other ingredients that may be contained in inventive cleaning agents may be selected from bleach activators, bleach catalysts, corrosion inhibitors, sequestering agents, fragrances, dyestuffs, antifoams, and builders.

Particularly advantageous inventive cleaning agents may contain one or more complexing agents other than MGDA or GLDA. Advantageous detergent compositions for cleaners and ad vantageous laundry detergent compositions may contain one or more sequestrant (chelating agent) other than a mixture according to the present invention. Examples for sequestrants other than a mixture according to the present invention are IDS (iminodisuccinate), citrate, phosphon- ic acid derivatives, for example the disodium salt of hydroxyethane-1 ,1 -diphosphonic acid (“HEDP”), and polymers with complexing groups like, for example, polyethylenimine in which 20 to 90 mole-% of the N-atoms bear at least one CH COO group, and their respective alkali metal salts, especially their sodium salts, for example IDS-Na ₄ , and trisodium citrate, and phosphates such as STPP (sodium tripolyphosphate). Due to the fact that phosphates raise environmental concerns, it is preferred that advantageous inventive cleaning agents are free from phosphate. "Free from phosphate" should be understood in the context of the present invention, as meaning that the content of phosphate and polyphosphate is in sum in the range from 10 ppm to 0.2% by weight, determined by gravimetric methods and referring to the respective inventive cleaning agent.

Inventive cleaning agents may contain one or more surfactant, preferably one or more non-ionic surfactant.

Preferred non-ionic surfactants are alkoxylated alcohols, di- and multiblock copolymers of eth ylene oxide and propylene oxide and reaction products of sorbitan with ethylene oxide or pro pylene oxide, alkyl polyglycosides (APG), hydroxyalkyl mixed ethers and amine oxides. Preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds of the general formula (II)

in which the variables are defined as follows:

R ¹ is identical or different and selected from hydrogen and linear Ci-Cio-alkyl, preferably in each case identical and ethyl and particularly preferably hydrogen or methyl,

R ² is selected from C ₈ -C22-alkyl, branched or linear, for example n-C ₈ Hi ₇ , n-Ci ₀ H _2i , n-Ci ₂ H ₂₅ , n-Ci ₄ H ₂₉ , n-Ci ₆ H ₃₃ or n-Ci ₈ H ₃₇ ,

R ³ is selected from Ci-Cio-alkyl, methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, isopentyl, sec-pentyl, neopentyl, 1 ,2-dimethylpropyl, isoamyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl or isodecyl, m and n are in the range from zero to 300, where the sum of n and m is at least one, preferably in the range of from 3 to 50. Preferably, m is in the range from 1 to 100 and n is in the range from 0 to 30.

In one embodiment, compounds of the general formula (II) may be block copolymers or random copolymers, preference being given to block copolymers.

Other preferred examples of alkoxylated alcohols are, for example, compounds of the general formula (III)

in which the variables are defined as follows:

R ¹ is identical or different and selected from hydrogen and linear CrCo-alkyl, preferably iden tical in each case and ethyl and particularly preferably hydrogen or methyl,

R ⁴ is selected from C ₆ -C2o-alkyl, branched or linear, in particular n-C ₈ Hi ₇ , n-Ci ₀ H _2i , n-Ci ₂ H ₂₅ , n-Ci 4H ₂₉ , n-Ci 6H ₃ 3, n-Ci ₈ H37, a is a number in the range from zero to 10, preferably from 1 to 6,

b is a number in the range from 1 to 80, preferably from 4 to 20, d is a number in the range from zero to 50, preferably 4 to 25.

The sum a + b + d is preferably in the range of from 5 to 100, even more preferably in the range of from 9 to 50.

Preferred examples for hydroxyalkyl mixed ethers are compounds of the general formula (IV)

in which the variables are defined as follows:

R ¹ is identical or different and selected from hydrogen and linear Ci-Cio-alkyl, preferably in each case identical and ethyl and particularly preferably hydrogen or methyl,

R ² is selected from C ₈ -C22-alkyl, branched or linear, for example iso-CnH ₂ 3, iso-Ci ₃ H ₂₇ , n-

0 ₈ Hΐ7, n-CioH _2i , n-Ci ₂ H ₂₅ , n-Ci4H _2g , n-Ci ₆ H ₃₃ or n-Ci ₈ H ₃₇ ,

R ³ is selected from CrCi ₈ -alkyl, methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, isopentyl, sec-pentyl, neopentyl, 1 ,2-dimethylpropyl, isoamyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl, isodecyl, n-dodecyl, n-tetradecyl, n-hexadecyl, and n-octadecyl. The variables m and n are in the range from zero to 300, where the sum of n and m is at least one, preferably in the range of from 5 to 50. Preferably, m is in the range from 1 to 100 and n is in the range from 0 to 30.

Compounds of the general formula (II) and (III) may be block copolymers or random copoly mers, preference being given to block copolymers.

Further suitable nonionic surfactants are selected from di- and multiblock copolymers, com posed of ethylene oxide and propylene oxide. Further suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Amine oxides or alkyl polyglycosides, espe cially linear C4-Ci ₆ -alkyl polyglucosides and branched C ₈ -Ci4-alkyl polyglycosides such as com pounds of general average formula (V) are likewise suitable.

wherein the variables are defined as follows:

R ⁵ is CrC4-alkyl, in particular ethyl, n-propyl or isopropyl,

R ⁶ is -(CH ₂ ) ₂ -R ⁵ ,

G ¹ is selected from monosaccharides with 4 to 6 carbon atoms, especially from glucose and xylose, x in the range of from 1.1 to 4, x being an average number.

An overview of suitable further nonionic surfactants can be found in EP-A 0 851 023 and in DE- A 198 19 187.

Mixtures of two or more different nonionic surfactants may also be present.

Other surfactants that may be present are selected from amphoteric (zwitterionic) surfactants and anionic surfactants and mixtures thereof.

Examples of amphoteric surfactants are those that bear a positive and a negative charge in the same molecule under use conditions. Preferred examples of amphoteric surfactants are so- called betaine-surfactants. Many examples of betaine-surfactants bear one quaternized nitrogen atom and one carboxylic acid group per molecule. A particularly preferred example of amphoter ic surfactants is cocamidopropyl betaine (lauramidopropyl betaine).

Examples of amine oxide surfactants are compounds of the general formula (V)

R ⁷ R ⁸ R ⁹ N— >0 (V) wherein R ⁷ , R ⁸ and R ⁹ are selected independently from each other from aliphatic, cycloaliphatic or C ₂ -C4-alkylene Ci ₀ -C2o-alkylamido moieties. Preferably, R ⁷ is selected from C ₈ -C2o-alkyl or C ₂ - C4-alkylene Ci ₀ -C2o-alkylamido and R ⁸ and R ⁹ are both methyl.

A particularly preferred example is lauryl dimethyl aminoxide, sometimes also called lauramine oxide. A further particularly preferred example is cocamidylpropyl dimethylaminoxide, some times also called cocamidopropylamine oxide.

Examples of suitable anionic surfactants are alkali metal and ammonium salts of C ₈ -Ci8-alkyl sulfates, of C ₈ -Ci ₈ -fatty alcohol polyether sulfates, of sulfuric acid half-esters of ethoxylated C4- Ci2-alkylphenols (ethoxylation: 1 to 50 mol of ethylene oxide/mol), Ci ₂ -Ci ₈ sulfo fatty acid alkyl esters, for example of Ci ₂ -Ci ₈ sulfo fatty acid methyl esters, furthermore of Ci ₂ -Ci ₈ -alkylsulfonic acids and of Cio-Cis-alkylarylsulfonic acids. Preference is given to the alkali metal salts of the aforementioned compounds, particularly preferably the sodium salts.

Further examples for suitable anionic surfactants are soaps, for example the sodium or potassi um salts of stearic acid, oleic acid, palmitic acid, ether carboxylates, and alkylether phosphates.

Preferably, laundry detergent compositions contain at least one anionic surfactant.

In one embodiment of the present invention, inventive cleaning agents that are determined to be used as laundry detergent compositions may contain 0.1 to 60 % by weight of at least one sur factant, selected from anionic surfactants, amphoteric surfactants and amine oxide surfactants.

In one embodiment of the present invention, inventive cleaning agents that are determined to be used for hard surface cleaning may contain 0.1 to 60 % by weight of at least one surfactant, selected from anionic surfactants, amphoteric surfactants and amine oxide surfactants.

In a preferred embodiment, inventive cleaning agents do not contain any anionic detergent. Inventive cleaning agents may comprise one or more bleach catalysts. Bleach catalysts can be selected from bleach-boosting transition metal salts or transition metal complexes such as, for example, manganese-, iron-, cobalt-, ruthenium- or molybdenum-salen complexes or carbonyl complexes. Manganese, iron, cobalt, ruthenium, molybdenum, titanium, vanadium and copper complexes with nitrogen-containing tripod ligands and also cobalt-, iron-, copper- and rutheni um-amine complexes can also be used as bleach catalysts.

Inventive cleaning agents may comprise one or more bleach activators, for example N- methylmorpholinium-acetonitrile salts (“MMA salts”), trimethylammonium acetonitrile salts, N- acylimides such as, for example, N-nonanoylsuccinimide, 1 ,5-diacetyl-2,2-dioxohexahydro- 1 ,3,5-triazine (“DADHT”) or nitrile quats (trimethylammonium acetonitrile salts).

Further examples of suitable bleach activators are tetraacetylethylenediamine (TAED) and tetraacetylhexylenediamine.

Inventive cleaning agents may comprise one or more corrosion inhibitors. In the present case, this is to be understood as including those compounds which inhibit the corrosion of metal. Ex amples of suitable corrosion inhibitors are triazoles, in particular benzotriazoles, bisbenzotria- zoles, aminotriazoles, alkylaminotriazoles, also phenol derivatives such as, for example, hydro- quinone, pyrocatechol, hydroxyhydroquinone, gallic acid, phloroglucinol or pyrogallol.

In one embodiment of the present invention, inventive cleaning agents comprise in total in the range from 0.1 to 1.5% by weight of corrosion inhibitor.

Inventive cleaning agents may comprise one or more builders, selected from organic and inor ganic builders. Examples of suitable inorganic builders are sodium sulfate or sodium carbonate or silicates, in particular sodium disilicate and sodium metasilicate, zeolites, sheet silicates, in particular those of the formula a-Na ₂ Si ₂ 05, 3-Na ₂ Si ₂ 0 ₅ , and 6-Na ₂ Si ₂ 0 ₅ , also fatty acid sul fonates, a-hydroxypropionic acid, alkali metal malonates, fatty acid sulfonates, alkyl and alkenyl disuccinates, tartaric acid diacetate, tartaric acid monoacetate, oxidized starch, and polymeric builders, for example polycarboxylates and polyaspartic acid.

Examples of organic builders are especially polymers and copolymers other than copolymer (B), or one additional copolymer (B). In one embodiment of the present invention, organic builders are selected from polycarboxylates, for example alkali metal salts of (meth)acrylic acid homo polymers or (meth)acrylic acid copolymers, partially or completely neutralized with alkali.

Suitable comonomers for (meth)are monoethylenically unsaturated dicarboxylic acids such as maleic acid, fumaric acid, maleic anhydride, itaconic acid and citraconic acid. A suitable polymer is in particular polyacrylic acid, which preferably has an average molecular weight M _w in the range from 2000 to 40 000 g/mol, preferably 3,000 to 10,000 g/mol.

It is also possible to use copolymers of at least one monomer from the group consisting of mo- noethylenically unsaturated C ₃ -Cio-mono- or C4-Cio-dicarboxylic acids or anhydrides thereof, such as maleic acid, maleic anhydride, acrylic acid, methacrylic acid, fumaric acid, itaconic acid and citraconic acid, with at least one hydrophilic or hydrophobic monomer as listed below.

Suitable hydrophobic monomers are, for example, isobutene, diisobutene, butene, pentene, hexene and styrene, olefins with 10 or more carbon atoms or mixtures thereof, such as, for ex ample, 1 -decene, 1 -dodecene, 1 -tetradecene, 1 -hexadecene, 1 -octadecene, 1 -eicosene, 1 - docosene, 1 -tetracosene and 1 -hexacosene, C ₂ 2-a-olefin, a mixture of C ₂ o-C24-a-olefins and polyisobutene having on average 12 to 100 carbon atoms per molecule.

Suitable hydrophilic monomers are monomers with sulfonate or phosphonate groups, and also nonionic monomers with hydroxyl function or alkylene oxide groups. By way of example, men tion may be made of: allyl alcohol, isoprenol, methoxypolyethylene glycol (meth)acrylate, meth- oxypolypropylene glycol (meth)acrylate, methoxypolybutylene glycol (meth)acrylate, methoxy- poly(propylene oxide-co-ethylene oxide) (meth)acrylate, ethoxypolyethylene glycol

(meth)acrylate, ethoxypolypropylene glycol (meth)acrylate, ethoxypolybutylene glycol

(meth)acrylate and ethoxypoly(propylene oxide-co-ethylene oxide) (meth)acrylate. Polyalkylene glycols here may comprise 3 to 50, in particular 5 to 40 and especially 10 to 30 alkylene oxide units per molecule.

Particularly preferred sulfonic-acid-group-containing monomers here are 1 -acrylamido-

1 -propanesulfonic acid, 2-acrylamido-2-propanesulfonic acid, 2-acrylamido-

2-methylpropanesulfonic acid, 2-methacrylamido-2-methylpropanesulfonic acid,

3-methacrylamido-2-hydroxypropanesulfonic acid, allylsulfonic acid, methallylsulfonic acid, al- lyloxybenzenesulfonic acid, methallyloxybenzenesulfonic acid, 2-hydroxy- 3-(2-propenyloxy)propanesulfonic acid, 2-methyl-2-propene-1 -sulfonic acid, styrenesulfonic ac id, vinylsulfonic acid, 3-sulfopropyl acrylate, 2-sulfoethyl methacrylate, 3-sulfopropyl methacry late, sulfomethacrylamide, sulfomethylmethacrylamide, and salts of said acids, such as sodium, potassium or ammonium salts thereof.

Particularly preferred phosphonate-group-containing monomers are vinylphosphonic acid and its salts.

Moreover, amphoteric polymers can also be used as builders. Inventive cleaning agents may comprise, for example, in the range from in total 10 to 50% by weight, preferably up to 20% by weight, of builder.

In one embodiment of the present invention, inventive cleaning agents according to the inven tion may comprise one or more cobuilders.

Inventive cleaning agents may comprise one or more antifoams, selected for example from sili cone oils and paraffin oils.

In one embodiment of the present invention, inventive cleaning agents comprise in total in the range from 0.05 to 0.5% by weight of antifoam.

Inventive cleaning agents may comprise one or more enzymes beyond enzyme (B) contained in inventive granule or inventive powder. Examples of enzymes are lipases, hydrolases, amylases, proteases, cellulases, esterases, pectinases, oxidoreductases and peroxidases.

In one embodiment of the present invention, inventive cleaning agents may comprise, for ex ample, up to 5% by weight of enzyme, preference being given to 0.1 to 3% by weight. Said en zyme may be stabilized, for example with the sodium salt of at least one Ci-C ₃ -carboxylic acid or C4-Cio-dicarboxylic acid. Preferred are formates, acetates, adipates, and succinates.

In one embodiment of the present invention, inventive cleaning agents may comprise at least one zinc salt. Zinc salts can be selected from water-soluble and water-insoluble zinc salts. In this connection, within the context of the present invention, water-insoluble is used to refer to those zinc salts which, in distilled water at 25°C, have a solubility of 0.1 g/l or less. Zinc salts which have a higher solubility in water are accordingly referred to within the context of the pre sent invention as water-soluble zinc salts.

In one embodiment of the present invention, zinc salt is selected from zinc benzoate, zinc glu conate, zinc lactate, zinc formate, ZnCI ₂ , ZnSC , zinc acetate, zinc citrate, Zn(N0 ₃ ) ₂ ,

Zn(CH ₃ S0 ₃ ) ₂ and zinc gallate, preferably ZnCI ₂ , ZnSC , zinc acetate, zinc citrate, Zn(N0 ₃ ) ₂ , Zn(CH ₃ S0 ₃ ) ₂ and zinc gallate.

In another embodiment of the present invention, zinc salt is selected from ZnO, ZnO-aq, Zn(OH) ₂ and ZnC0 ₃ . Preference is given to ZnO-aq. In one embodiment of the present invention, zinc salt is selected from zinc oxides with an aver age particle diameter (weight-average) in the range from 10 nm to 100 pm.

The cation in zinc salt can be present in complexed form, for example complexed with ammonia ligands or water ligands, and in particular be present in hydrated form. To simplify the notation, within the context of the present invention, ligands are generally omitted if they are water lig ands.

Depending on how the pH of mixture according to the invention is adjusted, zinc salt can change. Thus, it is for example possible to use zinc acetate or ZnCI ₂ for preparing formulation according to the invention, but this converts at a pH of 8 or 9 in an aqueous environment to ZnO, Zn(OH) ₂ or ZnO-aq, which can be present in non-complexed or in complexed form.

Zinc salt may be present in those inventive cleaning agents that are solid at room temperature. In such inventive cleaning agents zinc salts are preferably present in the form of particles which have for example an average diameter (number-average) in the range from 10 nm to 100 pm, preferably 100 nm to 5 pm, determined for example by X-ray scattering.

Zinc salt may be present in those inventive cleaning agents that are liquid at room temperature. In such inventive cleaning agents zinc salts are preferably present in dissolved or in solid or in colloidal form.

In one embodiment of the present invention, inventive cleaning agents comprise in total in the range from 0.05 to 0.4% by weight of zinc salt, based in each case on the solids content of the cleaning agent in question.

Here, the fraction of zinc salt is given as zinc or zinc ions. From this, it is possible to calculate the counterion fraction.

In one embodiment of the present invention, inventive cleaning agents are free from heavy met als apart from zinc compounds. Within the context of the present, this may be understood as meaning that inventive cleaning agents are free from those heavy metal compounds which do not act as bleach catalysts, in particular of compounds of iron and of bismuth. Within the context of the present invention, "free from" in connection with heavy metal compounds is to be under stood as meaning that the content of heavy metal compounds which do not act as bleach cata lysts is in sum in the range from 0 to 100 ppm, determined by the leach method and based on the solids content. Preferably, inventive cleaning agents has, apart from zinc, a heavy metal content below 0.05 ppm, based on the solids content of the formulation in question. The fraction of zinc is thus not included. Within the context of the present invention, "heavy metals" are deemed to be all metals with a specific density of at least 6 g/cm ³ with the exception of zinc. In particular, the heavy metals are metals such as bismuth, iron, copper, lead, tin, nickel, cadmium and chromium.

Preferably, inventive cleaning agents comprise no measurable fractions of bismuth compounds, i.e. for example less than 1 ppm.

Inventive cleaning agents are excellent for cleaning hard surfaces and fibres.

The present invention is further illustrated by working examples.

General remarks: Nl: Norm liter, liters under normal conditions; Nm ³ : norm cubic meter, cubic meter under normal conditions

Amounts of protease (B) refer to active content, determined by an enzyme assay based on suc- cinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF) as substrate, wherein para- nitroaniline (“pNA”) is cleaved off from the substrate molecule by proteolytic cleavage at pH 8.6, resulting in the release of yellow color of free pNA which was quantified by measuring OD405. If not indicated otherwise, the enzymatic activity was measured at 30°C.

Amounts of complexing agent (A) are based on iron binding capacity, determined by titration with Fe(lll) chloride and potentiometric detection.

Starting materials:

(A.1 ): 45 % by weight aqueous solution of trisodium salt of methylglycine diacetic acid (MGDA- Na _3-X ) with x = 0.05

(B.1 ): protease“PA2” which is an alkaline subtilisin from bacillus licheniformis, as concentrate, active enzyme content 17%

A coating slurry CS.1 was made as follows: 50 g titanium dioxide, (D50) 0.25 pm, and 50 g pol yethylene glycol, M _n 6,000 g/mol, were stirred into 235 ml of water at 25°C until a uniform slurry was formed.

Manufacture of spray liquors

1.1 Manufacture of spray liquor SL.1

A vessel was charged with 19 kg of an aqueous solution of (A.1 ). An amount of 9 kg concen trate of (B.1 ) was added. The slurry SL.1 so obtained was stirred at ambient temperature and then subjected to spray granulation. 1.2 Manufacture of spray liquor SL.2

A vessel was charged with 19 kg of an aqueous solution of (A.1 ). An amount of 3 kg concentrate of (B.1 ) was added. The slurry SL.2 so obtained was stirred at ambient temperature and then subjected to spray granulation.

II. Spray granulation

11.1 Spray granulation of Spray Liquor SL.1 , step (b.1 )

A cylindrical vessel with a perforated plate at the bottom, diameter of the cylinder: 148 mm, top lateral area 0.017 m ² , height: 40 cm, with zig-zag air classifier, commercially available as Glatt Lab System with Vario 3 Insert, was charged with 0.9 kg of solid MGDA-Na ₃ spherical particles, diameter 350 to 1 ,250 pm, and 600 g of milled MGDA-Na ₃ particles. An amount of 200 Nm ³ /h of air with a temperature of 170°C was blown from the bottom. A fluidized bed of MGDA-Na ₃ particles was obtained. The above liquor SL.1 was introduced by spraying 6.7 kg of SL.1 (20°C) per hour into the fluidized bed from the bottom through a two-fluid nozzle, absolute pressure in the nozzle: 5 bar. A granule was formed, and the bed temperature, which corresponds to the surface temperature of the solids in the fluidized bed, was 98 to 201 °C.

After every 30 minutes, portions of solids were removed with an in-line discharge screw attached to the cylindrical vessel directly above the perforated plate. After such removal, an amount of 1 kg of granule remained in the fluidized bed. The solids removed were subjected to two sieving steps. Three fractions were obtained: coarse particles (diameter > 1 .25 mm), fines (diameter < 0.355 mm), middle fraction (0.355 mm < diameter < 1 .25 mm). The coarse particles were milled using a hammer mill (Kinetatica Polymix PX-MFL 90D) at 4000 rpm (rounds per minute), 2 mm mesh. The powder so obtained was mixed with the fines and then altogether returned into the fluidized bed.

After 90 minutes of spray granulating a steady state was reached. The middle fraction was collected as inventive granule Gr.1 . The residual moisture of Gr.1 was determined to be 10.5 to 1 1 .0 %, referring to the total solids content of the granule.

In the above example, hot air of 170°C can be replaced by hot N having a temperature of 170°C. 11.2 Spray granulation of Spray Liquor SL.2, step (b.2)

The spray granulation of SL.2 was performed as above but instead of SL.1 , SL. was used.

After 90 minutes of spray granulating a steady state was reached. The middle fraction was collected as inventive granule Gr.2. The residual moisture of Gr.2 was determined to be 10.5 to 1 1 .0 %, referring to the total solids content of the granule.

11.3 Additional coating step, (d.1 ) and (d.2)

If applicable, the coating step was performed as follows:

A commercially available Glatt Lab System with Vario 3 Insert, was charged with 1 kg of Gr.1 and fluidized with air (60°C). Over a period of 45 minutes, CS.1 was sprayed into the fluidized bed by means of a two-fluid-nozzle, pressure: 3 bar. After completion of the spraying, fluidization was continued for another 5 minutes at 60°C. A coated granule was obtained, Gr.1 -coat.

The activity of the granules was tested as follows:

1 g of a sample was dissolved in 99ml TRIS buffer, pH value of 8.6, and the activity was determined after 15 min dissolution with the above assay at 30°C. The rate of cleavage was determined by the increase of the yellow color of free para-nitroaniline by measuring OD405, the optical density at 405 nm.

The following residual activities were found