SUBTILASE VARIANTS AND COMPOSITIONS COMPRISING THEM

Abstract

Subtilase variants having improved stability are provided, detergent compositions comprising the variants, the use of the variants and detergent compositions in a cleaning method, such as washing clothes or cleaning hard surfaces, such as washing dishes, and methods for producing the variants.

Description

SUBTILASE VARIANTS AND COMPOSITIONS COMPRISING THEM FIELD OF INVENTION The present invention relates to subtilase variants, compositions comprising the variants, polynucleotides encoding the variants, methods for producing the variants, and methods for using the variants and compositions. BACKGROUND OF THE INVENTION Subtilisins are serine proteases of the S8 family, specifically the S8A subfamily, as defined by the MEROPS database (https: / / www.ebi.ac.uk / merops / index.shtml). In the S8A subfamily, the key active site residues Asp, His, and Ser are generally found in motifs that differ from those of the S8B subfamily. In the detergent industry, enzymes have been used in washing formulations for many decades. These formulations include proteases, lipases, amylases, cellulases, and mannosidases, as well as other enzymes and mixtures thereof. Commercially, proteases are the most important enzymes. A growing number of proteases used commercially in, for example, laundry detergents and dishwashing liquids are genetically modified variants of natural proteases. Furthermore, other proteases have been described in the art. Ref. 317870 Subtilase variants with alterations relative to a precursor subtilase that result in improvements such as increased washing performance, thermal stability, storage stability, or catalytic activity. However, several factors make further protease enhancement advantageous. For example, washing conditions, such as temperature and pH, tend to change over time and also differ between countries and regions, and many stains remain difficult to remove completely under conventional washing conditions. Another challenge in detergent compositions is enzyme stability, since the chemical components of these compositions, as well as pH, temperature, and humidity conditions, often tend to inactivate enzymes. Furthermore, washing conditions can also lead to enzyme inactivation (due, for example, to pH, temperature, or chelation instability), resulting in a loss of washing performance during the wash cycle.Therefore, despite the intense research in protease development, there remains a need for new and improved proteases that have improved stability, for example, improved storage stability, for example, in a detergent composition, and at the same time have similar or improved washing performance compared to the precursor subtilase. The present invention addresses these challenges by providing novel subtilase variants that have advantageous properties in terms of stability and washing performance. BRIEF DESCRIPTION OF THE INVENTION The present invention relates to novel subtilase variants suitable for use in, for example, detergent compositions, wherein the variants comprise substitutions in at least positions 9, 19 and 62 relative to SEC. ID NO.: 1, in particular the S9R+R19L+N62D substitutions, for example, the S3T+S9R+R19L+N62D+A194P substitutions. The present invention also relates to compositions comprising the variants, in particular detergent compositions, polynucleotides encoding the variants; nucleic acid constructs, vectors and host cells comprising the polynucleotides; and methods for producing the variants. Sequence synthesis SEC. ID NO.: 1 is the amino acid sequence of the protease subtilisin 309, also known as Savinase®. SEC. ID NO.: 2 is the amino acid sequence of subtilisin BPN'. BRIEF DESCRIPTION OF THE FIGURES Figure 1 is an alignment of the 1 / UUOO» I amino acid sequences of subtilisin 309 (SEC. ID NO.: 1) and subtilisin BPN' (SEC. ID NO.: 2). DEFINITIONS Subtilase / protease: The terms subtilase and protease may be used interchangeably herein and refer to an enzyme that hydrolyzes peptide bonds in proteins. This includes any enzyme belonging to the EC 3.4 enzyme group (including each of its thirteen subclasses), and in particular endopeptidases (EC 3.4.21). The EC number refers to the NC-IUBMB Enzyme Nomenclature 1992, Academic Press, San Diego, California, including Supplements 1–5 published in Eur. J. Biochem. 1994, 223, 1–5; Eur. J. Biochem. 1995, 232, 1–6; Eur. J. Biochem. 1996, 237, 1–5; Eur. J. Biochem. 1997, 250, 1–6; and Eur. J. Biochem. 1999, 264, 610-650; respectively. Protease activity: The term protease activity means proteolytic activity (EC 3.4), in particular endopeptidase activity (EC 3.4.21). There are several types of protease activity; the three main types are: trypsin-like, when cleavage of amide substrates occurs after Arg or Lys at Pl; chymotrypsin-like, when cleavage occurs after one of the hydrophobic amino acids at Pl; and elastase-like, with cleavage after Ala at Pl. Protease activity can be determined according to the method described in WO. 2016 / 087619. The subtilisin variants of the present invention preferably have at least 80%, at least 90%, at least 95% or at least 100% of the protease activity of the SEC polypeptide. ID NO.: 1. Allelic variant: The term allelic variant refers to any of two or more alternative forms of a gene that occupy the same chromosomal locus. Allelic variation occurs naturally due to mutation and can generate polymorphism in populations. Gene mutations can be silent (with no change in the encoded polypeptide) or they can encode polypeptides with altered amino acid sequences. An allelic variant of a polypeptide is a polypeptide encoded by an allelic variant of a gene. cDNA: The term cDNA refers to a DNA molecule that can be prepared by reverse transcription from a mature mRNA molecule, which has already undergone splicing, obtained from a eukaryotic or prokaryotic cell. cDNA lacks the intronic sequences that may be present in the corresponding genomic DNA. The initial primary RNA transcript is an mRNA precursor that is processed through a series of steps, including splicing, before appearing as mature mRNA that has already undergone splicing. Coding Sequence: The term coding sequence refers to a polynucleotide that directly specifies the amino acid sequence of a variant. The boundaries of the coding sequence are generally determined by an open reading frame that begins with a start codon such as ATG, GTG, or TTG and ends with a stop codon such as TAA, TAG, or TGA. The coding sequence can be genomic DNA, cDNA, synthetic DNA, or a combination thereof. Control sequences: The term "control sequences" refers to nucleic acid sequences required for the expression of a polynucleotide encoding a variant of the present invention. Each control sequence may be native (i.e., derived from the same gene) or exogenous (i.e., derived from a different gene) with respect to the polynucleotide encoding the variant, or it may be native or exogenous relative to each other. Control sequences include, but are not limited to, a leader sequence, a polyadenylation sequence, a polypeptide sequence, a promoter sequence, a signal peptide sequence, and a transcription termination sequence. At a minimum, control sequences include a promoter sequence and transcription and translation termination signals.Control sequences can be provided with connectors in order to introduce specific restriction sites that facilitate the binding of control sequences to the coding region of the polynucleotide that encodes a variant. Expression: The term expression includes any stage involved in the production of a variant, including, but not limited to, transcription, post-transcription modification, translation, post-translation modification, and secretion. Expression vector: The expression expression vector refers to a linear or circular DNA molecule comprising a polynucleotide that encodes a variant and that operatively binds to control sequences that generate its expression. Fragment: The term fragment means a polypeptide having one or more amino acids missing from the amino and / or carboxyl terminus of a mature polypeptide; wherein the fragment has subtilase activity. Such a segment preferably contains at least 85%, at least 90%, or at least 95% of the number of amino acids of SEC. ID NO.: 1. Host cell: The term host cell means any cell type susceptible to transformation, transduction, or the like, with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention. The term host cell encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that may occur during replication. i / uuooa i Improved Property: The term "improved property" refers to a characteristic associated with a variant that is improved compared to the precursor protease, the protease with SEC. ID NO.: 1, or a selected reference protease such as a variant of SEC. ID NO.: 1. Such improved properties may include, but are not limited to, catalytic efficiency, catalytic flow rate, chemical stability, oxidation stability, pH activity, pH stability, specific activity, stability under storage conditions, substrate binding, substrate cleavage, substrate specificity, substrate stability, surface properties, thermal activity, and thermostability. In one aspect of the present invention, the improved property is improved stability, for example, improved thermostability or improved storage stability in a detergent formulation or a pH stress buffer.In another aspect of the invention, the improved property is an improved washing performance. Isolated: The term isolated refers to a substance in a form or environment that does not occur in nature. Non-limiting examples of isolated substances include (1) any substance that does not have a natural origin, (2) any substance that includes, but is not limited to, any enzyme, variant, nucleic acid, protein, peptide, or cofactor, that has been separated, at least in part, from one or more or all of the naturally occurring constituents with which it is associated in nature; (3) any substance modified by human intervention with respect to the substance found in nature; or (4) any substance modified by increasing the amount of the substance with respect to other components with which it is naturally associated (e.g., multiple copies of a gene encoding the substance; the use of a more potent promoter than the promoter naturally associated with the gene encoding the substance).An isolated substance may be present in a sample of fermentation broth. Mature polypeptide: The term mature polypeptide refers to a polypeptide in its mature form after processing at the amino terminus (e.g., signal peptide deletion). Sequence that encodes a mature polypeptide: The expression sequence that encodes a mature polypeptide refers to a polynucleotide that encodes a mature polypeptide that has subtilase activity. Mutant: The term mutant means a polynucleotide that codes for a variant. Nucleic acid construct: The term nucleic acid construct means a nucleic acid molecule, either single- or double-stranded, that is isolated from a naturally occurring gene or modified to contain nucleic acid segments in a manner that would not otherwise exist in nature or that is synthetic, comprising one or more control sequences. Operationally linked: The term operationally linked refers to a configuration in which a control sequence is placed in a suitable position relative to the coding sequence of a polynucleotide so that the control sequence directs the expression of the coding sequence. Precursor or precursor subtilase / protease: The term precursor or the expression precursor subtilase or precursor protease refers to any polypeptide with subtilase activity in which an alteration is made to produce the enzymatic variants of the present invention. The precursor may be a naturally occurring (natural) polypeptide or a variant thereof of a natural polypeptide. In one particular embodiment, the precursor is a protease with at least 75% identity, such as 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% identity with SEC. ID NO.: 1. Alternatively, the precursor may have 100% identity with SEC. ID NO.: 1. Sequence identity: The relationship between two amino acid sequences or between two nucleotide sequences is described by the sequence identity parameter. For the purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later. The parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 substitution matrix (EMBOSS version of BLOSUM62). The Needle output labeled as longest identity (obtained using the -nobrief option) is used as the percent identity and is calculated as follows: (Identical remains x 100) / (Length of alignment - Total number of gaps in alignment) For the purposes of the present invention, the sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, mentioned above) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, mentioned above), preferably version 5.0.0 or later. The parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL substitution matrix (NCBI NUC4.4 EMBOSS version). The Needle result marked as the longest identity (obtained using the -not short option) is used as the percent identity and is calculated as follows: (Identical deoxyribonucleotides x 100) / (Length of alignment - Total number of gaps in the alignment). Variant: The term variant means a polypeptide having subtilase activity comprising an alteration, i.e., a substitution, insertion, and / or deletion, at one or more positions. A substitution means the replacement of the amino acid occupying a position with a different amino acid; a deletion means the removal of the amino acid occupying a position; and an insertion means the addition of an amino acid adjacent to or immediately following the amino acid occupying a position. Natural subtilase: The term natural subtilase refers to a subtilase expressed by a naturally occurring microorganism, such as a bacterium, yeast, or filamentous fungus found in nature. Conventions for the design of variants For the purposes of the present invention, the polypeptide of SEC. ID NO.: 2 is used to determine the corresponding amino acid residue in a subtilase variant of the invention. This is explained in more detail below under the heading Numbering of the positions / amino acid residues. i / uuooa i The identification of the corresponding amino acid residue in another subtilase can be determined by aligning multiple polypeptide sequences using various computer programs, including, but not limited to, MUSCLE (log-expected multiple sequence comparison; version 3.5 or later; Edgar, 2004, Nucleic Acids Research 32: 1792-1797), MAFFT (version 6.857 or later; Katoh and Kuma, 2002, Nucleic Acids Research 30: 3059-3066; Katoh et al., 2005, Nucleic Acids Research 33: 511-518; Katoh and Toh, 2007, Bioinformatics 23: 372-374; Katoh et al., 2009, Methods in Molecular Biology 537: 39-64; Katoh and Toh, 2010, Bioinformatics 26: 1899-1900), and EMBOSS EMMA using ClustalW (1.83 or later; Thompson et al., 1994, Nucleic Acids Research 22: 4673-4680), using their respective default parameters. When describing variants of the present invention, the nomenclature described below is adapted for ease of reference. The three-letter or single-letter abbreviations for amino acids accepted by the IUPAC are used. The terms alteration or mutation may be used interchangeably in the present invention to refer to substitutions, insertions, and deletions. Substitutions. For the substitution of an amino acid, the following nomenclature is used: precursor amino acid, position, substituted amino acid. For example, the substitution of a threonine at position 220 with alanine is designated as Thr220Ala or T220A. Multiple substitutions may be separated by plus signs (+), for example, Thr220Ala + Gly229Val or T220A + G229V, representing substitutions at positions 220 and 229 of threonine (T) with alanine (A) and glycine (G) with valine (V), respectively. Alternatively, multiple substitutions may be listed with individual mutations separated by a space or a comma. Alternative substitutions at a particular position may be indicated with a slash ( / ). For example, the substitution of threonine at position 220 with alanine, valine, or leucine can be designated T220A / V / L. Substitutions may also be indicated with an X before a position number, meaning that any precursor amino acid in a precursor subtilase other than the subtilase of SEC. ID NO.: 1 may be substituted at the corresponding indicated position in the precursor subtilase. For example, X19L means that any amino acid residue at position 19 of a precursor subtilase other than L is substituted with L. Deletions. For the deletion of an amino acid, the following nomenclature is used: precursor amino acid, position, *. Therefore, the deletion of threonine at position 220 is designated as Thr220* or T220*. Multiple deletions can be separated by plus signs (+), for example, i / uuooa i Thr220* + Gly229* or T220* + G229*, or alternatively, they can be separated by a space or a comma. The use of an X before a position number is as described above for substitutions, for example, X131* means that the amino acid residue at position 131 is removed. Insertions. For the insertion of an amino acid, the following nomenclature is used: precursor amino acid, position, precursor amino acid, inserted amino acid. Therefore, the insertion of thymine after threonine at position 220 is designated as Thr220ThrLys or T220TK. A multi-amino acid insertion is designated [precursor amino acid, position, precursor amino acid, inserted amino acid #1, inserted amino acid #2; etc.]. For example, the insertion of thymine and alanine after threonine at position 220 is indicated as Thr220ThrLysAla or T220TKA. In such cases, the inserted amino acid residue(s) are numbered by adding lowercase letters to the position number of the amino acid residue preceding the inserted amino acid residue(s). Thus, in the previous example, the sequence would be: i / uuooa i Precursor: Variant: 220 220 220a 220b TT - K - A Multiple alterations. Variants comprising multiple alterations are separated by plus signs (+), for example, Argl70Tyr+Glyl95Glu or R170Y+G195E, representing a substitution of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively. Alternatively, multiple alterations may be listed with individual mutations separated by a space or a comma. Different alterations. When different alterations can be introduced at a position, the different alterations can be separated by a comma, e.g., Argl7OTyr,Glu represents a substitution of arginine at position 170 with either tyrosine or glutamic acid. Therefore, Tyrl67Gly,Ala + Argl70Gly,Ala designates the following variants: Tyrl67Gly+Argl70Gly , Tyrl67Gly+Argl7 OAla , Tyr167Ala+Argl7OGly, and Tyrl67Ala+Argl70Ala. Different accidentals in a position can also be indicated with a forward slash ( / ), for example T220A / V / L as explained above. Alternatively, different accidentals can be indicated with square brackets, for example Argl70[Tyr, Gly] or with a one-letter code R170[Y,G]. Numbering of amino acid positions / residues. The amino acid position numbers as used in this document are based on the numbering of the BPN' polypeptide of SEC. ID NO.: 2. Thus, the amino acid positions of a precursor protease polypeptide having, for example, SEC. ID NO.: 1 are those of the corresponding positions of SEC. ID NO.: 2. This numbering system is conventional in the art, where the position numbers used for subtilisin proteases in the patent literature are frequently based on the corresponding position numbers of BPN'. Specifically, the numbering is based on the alignment in Table 1 of WO 89 / 06279, which shows an alignment of five proteases, including the mature polypeptide sequence of BPN' subtilase (BASBPN) (sequence c in the table) and the mature polypeptide of Bacillus lentus subtilisin 309, also known as Savinase® (BLSAVI) (sequence a in the table). Figure 1 attached is provided for reference purposes and shows an alignment between SEC. ID NO.: 1 and SEC. ID NO.: 2, based on Table 1 of WO 89 / 06279, from which the position numbers corresponding to the positions of SEC. ID NO.: 2 can be easily determined. For a precursor protease in addition to SEC. ID NO.: 1, the amino acid sequence of another protease can be similarly aligned with SEC. ID NO.: 2 to determine the amino acid position numbers corresponding to the numbering of SEC. ID NO.: 2. DETAILED DESCRIPTION OF THE INVENTION Variants In one aspect, the present invention relates to the subtilase variant comprising the substitutions X9R+X19L+X62D, where (a) the position numbers correspond to the positions of the polypeptide of SEC. ID NO.: 2; (b) the variant has protease activity; and (c) the variant has at least 80%, for example, 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% or at least 98% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1; and on the condition that the variant does not comprise a histidine residue at position 14. In one particular aspect, the present invention relates to the subtilase variant comprising the substitutions X3T+ X9R+ X19L+X62D+X194P, where (a) the position numbers correspond to the positions of the polypeptide of SEC. ID NO.: 2; (b) the variant has protease activity; and (c) the variant has at least 80% but less than one 100% sequence identity with the SEC polypeptide. ID In one version of this aspect, the substitutions X3T+X9R+X19L+X62D+X194P are S3T+S9R+R19L+N62D+A194P. Therefore, in one embodiment, the subtilase variant has at least 80%, for example, 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%, but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+ S9R+ R19L+ N62D+ A194P. In a preferred embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+A194P. In some forms, the subtilase variant further comprises at least one selected alteration from the group consisting of N43R, N76D, P131*, Q245R, S259D, and R275Q, where the position numbers correspond to the positions of the polypeptide in SEC. ID NO.: 2. Non-limiting examples of such variants are provided below. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N62D+A194P+Q245R+S259D. In a preferred embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+A194P+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+A194P+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+A194P+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N62D+P131*+A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+P131*+A194P. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N62D+P131*+A194P+Q245R+S259D. i / uuooa i In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+P131*+A194P+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+P131*+A194P+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+P131*+A194P+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+N76D+A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+N76D+A194P. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity i / uuooa i with the polypeptide of SEQ. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+N76D+P131*+A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+N76D+P131*+A194P. As stated above, in one aspect of the invention the subtilase variants do not comprise a histidine residue at position 14. In one embodiment of the broad aspect of the invention described above relating to a subtilase variant comprising the substitutions X9R+X19L+X62D, and wherein the variant does not comprise a histidine residue at position 14, the substitutions X9R+X19L+X62D are S9R+R19L+N62D. In some embodiments of this aspect, the subtilase variant further comprises at least one alteration selected from the group consisting of S3T, S3A, N43R, V68A, N76D, P131*, A194P, V205I, Q245R, S259D, N261D and R275Q, preferably two, three or more of the alterations, where the position numbers correspond to the positions of the polypeptide of SEC. ID NO.: 2. Non-limiting examples of such variants are provided below. In one modality, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least i / uuooa i 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N62D+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N62D+P131*. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+P131* . In one modality, the subtilase variant has at least i / uuooa i 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N62D+P131*+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+P131*+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+P131*+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+P131*+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+N76D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+N76D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+N76D+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+N76D+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3T+S9R+R19L+N43R+N62D+N76D+P131*. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N43R+N62D+N76D+P131*. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% or at least 96% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+A15T+G61E+N62D+V68A+A194P+V205I+Q245R+N26ID. i / uuooa i In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+A15T+G61E+N62D+V68A+A194P+V205I+Q245R+N261D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95% or at least 96% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+A15T+G61E+V68A+A194P+V205I+Q245R+S259D+N26ID. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+A15T+G61E+V68A+A194P+V205I+Q245R+S259D+N261D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+ R19L+ N43R+ N62D+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N62D+P131*. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N62D+P131*. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N62D+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N62D+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+ S9R+ R19L+ N62D+ A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with i / uuooa i the substitutions S3A+S9R+R19L+N62D+A194P. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+Q245R+S259D+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+Q245R+S259D+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N62D+P131*+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N62D+P131*+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+A194P+R275Q. In one particular embodiment, the subtilase i / uuooa i variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+A194P+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N62D+P131*+A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N62D+P131*+A194P. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+ R19L+ N43R+ N62D+N76D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+N76D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the i / uuooa i substitutions S3A+S9R+R19L+N43R+N62D+Q245R+S259D+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+Q245R+S259D+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N62D+P131*+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N62D+P131*+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N62D+A194P+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N62D+A194P+Q245R+S259D. In one modality, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 1 / UUOO» I 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N43R+N62D+P131*+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+P131*+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N43R+N62D+A194P+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+A194P+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N62D+P131*+A194P In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N62D+P131*+A194P. In one form, the subtilase variant has at least 1 / UUOO» I 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N43R+N62D+N76D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+N76D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+P131*+Q245R+S259D+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+P131*+Q245R+S259D+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+A194P+Q245R+S259D+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with i / uuooa i the substitutions S9R+R19L+N43R+N62D+A194P+Q245R+S259D+ R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N62D+P131*+A194P+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N62D+P131*+A194P+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+N76D+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+N76D+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+P131*+A194P+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+P131*+A194P+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+N76D+P131*. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+N76D+P131*. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+N76D+A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+N76D+A194P. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity i / uuooa i with the polypeptide of SEQ. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N62D+P131*+A194P+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N62D+P131*+A194P+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N43R+N62D+N76D+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+N76D+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N43R+N62D+P131*+A194P+R275Q. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+P131*+A194P+R275Q. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N43R+N62D+N76D+P131*. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+N76D+P131*. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S3A+S9R+R19L+N43R+N62D+N76D+A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S3A+S9R+R19L+N43R+N62D+N76D+A194P. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+N76D+P131*+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+N76D+P131*+Q245R+S259D. i / uuooa i In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+N76D+A194P+Q245R+S259D. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+N76D+A194P+Q245R+S259D. In one embodiment, the subtilase variant has at least 80%, for example, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97% but less than 100% sequence identity with the polypeptide of SEC. ID NO.: 1 and comprises the substitutions S9R+R19L+N43R+N62D+N76D+P131*+A194P. In one particular embodiment, the subtilase variant comprises or consists of the polypeptide of SEC. ID NO.: 1 with the substitutions S9R+R19L+N43R+N62D+N76D+P131*+A194P. In one aspect, the subtilase variant may comprise 2 to 6, such as 3, 4, or 5, histidine residues added to the amin or carboxyl terminus. An example of such a variant is one comprising SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+A194P+R275RHHHH, where R275RHHHH indicates four additional histidine residues after the Arg residue at the carboxyl terminus. i / uuooa i In addition to the amino acid alterations specifically described in this invention, a protease variant of the invention may comprise further alterations at one or more other positions. These further alterations may be minor, i.e., conservative amino acid insertions or substitutions that do not significantly affect the folding and / or activity of the protein; small deletions, typically of 1 to 30 amino acids; small amino acid extensions at the amino or carboxyl terminus, such as a methionine residue at the amino terminus; a small linker peptide of up to 20 to 25 residues; or a small extension that facilitates purification by changing the net charge or other function, such as a polyhistidine tract, an antigenic epitope, or a binding domain. Examples of conservative substitutions are found within the groups of basic amino acids (arginine, lysine, and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine, and valine), aromatic amino acids (phenylalanine, tryptophan, and tyrosine), and small amino acids (glycine, alanine, serine, threonine, and methionine). Amino acid substitutions that generally do not alter specific activity are known in the field and are described, for example, by H. Neurath and R.L. Hill, 1979, in *The Proteins*, Academic Press, New York. Common conservative substitution groups include, but are not limited to: G=A=S; I=V=L=M; D=E; Y=F; and N=Q (where, for example, G=A=S means that these three amino acids can be substituted for each other). Alternatively, changes in amino acids can alter the physicochemical properties of polypeptides. For example, changes in amino acids can improve the polypeptide's thermal stability, alter its substrate specificity, change its optimum pH, and produce similar effects. The essential amino acids of a polypeptide can be identified using methods known in the art, such as site-directed mutagenesis or alanine scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are introduced into each residue of the molecule, and the resulting mutated molecules are evaluated for protease activity to identify the amino acid residues that are crucial for the molecule's activity. See also Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. The active site of an enzyme or other biological interaction can also be determined by physical analysis of the structure, as determined by techniques such as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity titration, along with mutation of potential amino acids at the contact site. See, for example, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity of essential amino acids can also be deduced from alignment with a related polypeptide. In one aspect of the invention, the protease variant has at least one improved property compared to a reference protease, where the reference protease may, for example, be the protease of SEC. ID NO.: 1 or a variant thereof. In one embodiment, the protease variant of the invention has improved stability, for example, improved thermostability, improved storage stability in a detergent formulation in a defined pH stress buffer. Improved stability can, for example, be determined as described in the examples of the present invention with one or both of the following tests: • Stability test with a low pH stress buffer (pH 4.0) • Stability test with a high pH stress buffer (pH 10.5) and LAS. Stability can also be measured as the stability of a detergent composition, for example, a powdered detergent composition, such as a model powdered laundry detergent composition containing the ingredients listed in Table 3 herein. For instance, a protease variant in the model powdered laundry detergent composition of Table 3 can be tested in an accelerated storage stability test, where the detergent composition is stored for, for example, 2 or 4 weeks at 37°C and 70% relative humidity. In this case, the protease can be added to the powdered detergent composition in the form of granules, for example, comprising a coating such as an inorganic salt coating; for further information, see below under the heading Granular Detergent Formulations.Proteolytic activity is determined before and after storage, and residual activity after storage is calculated based on the initial activity. Proteolytic activity can be determined using the Suc-AAPF-pNA activity assay; see the examples section below for a description of this assay. Improved stability can, for example, be expressed as a half-life improvement factor of a protease variant relative to the half-life of a reference protease. In one embodiment, the stability of a protease variant of the invention is determined as a half-life improvement factor (TU IF) relative to the half-life of a variant of SEC. ID NO.: 1 having the substitutions S9R, P14H, R19L, and N62D. In this embodiment, the protease variant of the invention has a half-life improvement factor of at least approximately 1.2, more preferably at least approximately 1.5, such as at least approximately 2.0, at least approximately 3, at least approximately 4, at least approximately 5, at least approximately 6, at least approximately 7, at least approximately 8, at least approximately 9, or at least approximately 10, in at least one stability test. In one embodiment, the protease variant of the invention has a half-life enhancement factor (TA IF), relative to the half-life of a variant of SEC. ID NO.: 1 having the substitutions S9R, P14H, R19L and N62D, of at least approximately 2, such as at least approximately 3, at least approximately 4, at least approximately 5, at least approximately 6, at least approximately 7, at least approximately 8, at least approximately 9 or at least approximately 10, in the low pH stability test described in Example 2 of this invention. In one embodiment, the protease variant of the invention has a half-life improvement factor (1.5 IF), relative to the half-life of a variant of SEC. ID NO.: 1 having the substitutions S9R, P14H, R19L, and N62D, of at least approximately 1.2, preferably at least approximately 1.3, more preferably at least approximately 1.4, such as at least approximately 1.5, at least approximately 2, at least approximately 3 or at least approximately 4, in the high pH + LAS stability test described in Example 2 below. In a preferred embodiment, the protease variant of the invention has improved stability in both the low pH stability test and the high pH + LAS stability test described in Example 2 of this invention. For example, the protease variant may have a half-life improvement factor (1.5 IF), relative to the half-life of a variant of SEC. ID NO.: 1 having the substitutions S9R, P14H, R19L, and N62D, of at least approximately 2, such as at least approximately 3, at least approximately 4, at least approximately 5, at least approximately 6, at least approximately 7, at least approximately 8, at least approximately 9, or at least approximately 10, in the low pH stability test described in Example 2 of this invention; and a half-life improvement factor (1.5 IF), relative to the half-life of a variant of SEC. ID NO.: 1 having the substitutions S9R, P14H, R19L and N62D, of at least approximately 1.2, preferably at least approximately 1.3, more preferably at least approximately 1.4, such as at least approximately 1.5, at least approximately 2, at least approximately 3 or at least approximately 4, in the i / uuooa i high pH stability test + LAS described in Example 2 below. In another embodiment, the protease variant of the invention preferably has a half-life enhancement factor, relative to the half-life of a variant of SEC. ID NO.: 1 having the substitutions S9R, P14H, R19L, and N62D, of at least approximately 1.2, more preferably at least approximately 1.5, such as at least approximately 2, at least approximately 3, at least approximately 4, or at least approximately 5, in an accelerated storage stability test in a powdered detergent composition. The accelerated storage stability test may, for example, comprise storage for, for example, 2 weeks or 4 weeks at 37°C and 70% relative humidity, wherein the enzyme is added to the powdered detergent composition in the form of a granule, for example, comprising a coating such as an inorganic salt coating; for further information, see below under the heading Granular Detergent Formulations. In another aspect of the invention, the protease variant has an improved washing performance compared to a reference protease, where the reference protease may, for example, be the protease of SEC. ID NO.: 1. An improved washing performance in this context may be defined as an improved relative washing performance of the EMPA117EH stain, i / uuooa i, for example, as determined by the ANSA assay as described in Example 3 of this invention with a protease concentration of 10 nM or 20 nM and compared to a reference protease with SEC. ID NO.: 1, of at least approximately 1.1, preferably at least approximately 1.2, more preferably at least approximately 1.3, such as at least approximately 1.4, at least approximately 1.5, or at least approximately 1.6. In one embodiment, the protease variant has a relative washing performance on the PC-03 stain, for example as determined by the AMSA assay as described in Example 3 of this invention with a protease concentration of 10 nM or 20 nM and compared to a reference protease with SEC. ID NO.: 1, of at least approximately 1.0, such as at least approximately 1.1, preferably at least approximately 1.2, more preferably at least approximately 1.3, such as at least approximately 1.4. In another embodiment, improved washing performance may be defined in relation to the performance on any of the stains PC-03, PC-05, EMPA116 and / or EMPA117EH, as determined by the TOM test as described in Example 4 of this invention, compared to a reference protease with SEC. ID NO.: 1, of at least approximately 1.2, preferably at least approximately 1.3, more preferably at least approximately 1.4, such as at least approximately 1.5, at least approximately 1.6, at least approximately 1.7, at least approximately 1.8, at least approximately 1.9, or at least approximately 2.0. The improved washing performance in TOM in relation to SEC. ID NO.: 1 may, for example, relate to the washing performance of at least approximately 1.5, at least approximately 1.8, at least approximately 2.0 or at least approximately 2.2 on the EMPA117EH stain and / or on the PC-03 stain. precursor subtilases The precursor subtilase of a variant of the invention will normally be a protease having at least 75% identity with the subtilase of SEC. ID NO.: 1. In preferred embodiments, the precursor subtilase may have at least 80% identity with SEC. ID NO.: 1, such as 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% identity with SEC. ID NO.: 1. Alternatively, the precursor subtilase may have a sequence comprising SEC. ID NO.: 1. The precursor may, for example, have the sequence of the subtilase of SEC. ID NO.: 1, or alternatively it may be a variant of SEC. ID NO.: 1. The precursor may also be a related subtilase, for example, from the S8A family that has at least 75% sequence identity with SEC. ID NO.: 1 as stated above. In one modality, the amino acid sequence of the precursor may, for example, differ by up to 20 amino acids, such as up to 10 amino acids, for example, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 amino acids, of the polypeptide of SEC. ID NO.: 1. The precursor subtilase may also be a fragment of the polypeptide of SEC. ID NO.: 1 that has protease activity, or an allelic variant of the polypeptide of SEC. ID NO.: 1. The precursor subtilase can be obtained from a microorganism of any suitable genus, particularly a suitable bacterial genus. The precursor subtilase is therefore generally a bacterial subtilase. For example, the precursor may be a polypeptide from a Gram-positive bacterium, such as a subtilase from Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces, or a polypeptide from a Gram-negative bacterium, such as a subtilase from Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, or Ureaplasma. In one modality, the precursor is obtained from a species of Bacillus. The precursor can be, for example, a subtilase from Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, or Bacillus clausii. Badilas coagalans, Bacíllus firmas, Badilas lautas, Badilaslentes, Badilas licheniformis, Badilas megateríum, Badilas pamilas, Badilas stearothermophilas, Badilas sabtilis or Badilas tharingiensis. In one modality, the precursor is a protease derived from slow Badilas or a variant thereof, for example, the protease of SEC. ID NO.: 1. Strains of these species are readily accessible to the public in various culture collections, such as the American Type Culture Collection (ATCC), Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (DSMZ), Centraalbureau Voor Schimmelcultures (CBS) and Agricultural Research Service Patent Culture Collection, Northern Regional Research Center (NRRL). The precursor can be identified and obtained from other sources, including microorganisms isolated from nature (e.g., soil, compost, water, etc.) or DNA samples obtained directly from natural materials (e.g., soil, compost, water, etc.) using the probes mentioned above. Techniques for isolating microorganisms and DNA directly from natural habitats are well known in the art. A polynucleotide encoding a precursor can then be obtained by similarly screening a genomic DNA or cDNA library from another microorganism or mixed DNA sample. Once a polynucleotide encoding a precursor has been detected by probe(s), the polynucleotide can be isolated or cloned using techniques known to those skilled in the art (see, for example, Sambrook et al., Molecular Cloning; 3rd ed., 2001, Cold Spring Harbor Laboratory Press). Preparation of the variants The present invention also relates to methods for obtaining a variant of subtilase as described herein. A modality refers to a method for obtaining a subtilase variant; the method comprises: (a) providing a host cell comprising a polynucleotide encoding a precursor protease variant comprising mutations X9R+X19L+X62D compared to SEC. ID NO.: 1, wherein the position numbers correspond to positions in the polypeptide of SEC. ID NO.: 2, wherein the variant has protease activity and sequence identity with SEC. ID NO.: 1 of at least 80% but less than 100%, and provided that the variant does not comprise a histidine residue at position 14; (b) cultivate the host cell under certain conditions suitable for the expression of the variant; and (c) recover the variant. In one particular embodiment, the method for obtaining a subtilase variant comprises: l / UUOO» I (a) providing a host cell comprising a polynucleotide encoding a variant of a precursor protease comprising mutations X3T+ X9R+ XI9L+X62D+X194P compared to SEQ. ID NO.: 1, wherein the position numbers correspond to positions in the polypeptide of SEQ. ID NO.: 2, and wherein the variant has protease activity and sequence identity with SEQ. ID NO.: 1 of at least 80% but less than 100%; (b) cultivate the host cell under certain conditions suitable for the expression of the variant; and (c) recover the variant. The variants can be prepared using any mutagenesis method known to the art, such as site-directed mutagenesis, semisynthetic gene construction, randomized mutagenesis, DNA transposition, etc. For information on the use of these mutagenesis techniques, see, for example, WO 2017 / 207762. The method for obtaining a subtilase variant is understood to encompass the expression and recovery of variants that have any combination of mutations described above under the heading "Variants". Polynucleotides The present invention also relates to polynucleotides encoding a variant of the present invention. i / uuooa i Nucleic acid constructs The present invention also relates to nucleic acid constructs comprising a polynucleotide encoding a variant of the present invention operatively linked to one or more control sequences that direct the expression of the encoding sequence in a suitable host cell under conditions compatible with the control sequences. Polynucleotides can be manipulated in a variety of ways to provide and optimize the expression of a variant. Techniques for modifying polynucleotides using recombinant DNA methods are commonly used in this field. These include, for example, the use of control sequences as promoters, transcription terminators, mRNA stabilizing regions downstream of a promoter and upstream of the coding sequence, signal peptide coding regions, propeptide coding sequences, and regulatory sequences. For further information, see, for example, WO 2017 / 207762. Vectors of expression The present invention also relates to recombinant expression vectors comprising a polynucleotide encoding a variant of the present invention, a promoter, and transcription and translation termination signals. The various nucleotide and control sequences can be joined to produce a recombinant expression vector that may include one or more restriction sites to permit the insertion or substitution of the polynucleotide encoding the variant at such sites. Alternatively, the polynucleotide can be expressed by inserting the polynucleotide or a nucleic acid construct comprising the polynucleotide into a vector suitable for expression. When creating the expression vector, the coding sequence is positioned within the vector so that it is operatively linked to the control sequences appropriate for expression. The recombinant expression vector can be any vector (e.g., a plasmid or virus) that can be conveniently subjected to recombinant DNA methods and that can promote the expression of the polynucleotide. The choice of vector will normally depend on the vector's compatibility with the host cell into which it will be introduced. The vector can be a linear or closed circular plasmid. For information on expression vectors, see, for example, document WO 2017 / 207762. Host cells The present invention also relates to recombinant host cells comprising a polynucleotide encoding a variant of the present invention linked to one or more control sequences that direct the production of a variant of the present invention. A construct or vector comprising a polynucleotide is introduced into a host cell, such that the construct or vector is maintained as a chromosomal component or as a self-replicating extrachromosomal vector, as described above. The term "host cell" encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that may occur during replication. The choice of a host cell will depend largely on the gene encoding the variant and its source. The host cell can be any cell useful in the recombinant production of a variant, for example, a prokaryote or a eukaryote. The prokaryotic host cell will normally be a gram-positive or gram-negative bacteria, such as a gram-positive bacteria selected from Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus and Streptomyces, or a gram-negative bacteria selected from Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neissería, Pseudomonas, Salmonella and Ureaplasma. The bacterial host cell can be, for example, a Bacillus cell selected from Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus brevis, iviA / a / ¿u¿ i / uuooa i Bacillus circulans, Bacillus clausíi, Bacillus coagulans, Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus pumilus, Bacillus stearothermophilus, Bacillus subtilis and Bacillus thuringiensis. For information on suitable host cells, see, for example, document WO 2017 / 207762. Production methods The present invention also relates to methods of producing a variant, comprising: (a) cultivating a host cell of the present invention under conditions suitable for the expression of the variant; and (b) recovering the variant. Host cells are cultured in a nutrient medium suitable for the production of the variant using methods known in the art. For example, the cell may be cultured by shake-flask culture or small- or large-scale fermentation (including continuous, batch, fed-batch, or solid-state fermentations) in laboratory or industrial fermenters, carried out in a suitable medium and under conditions that allow the variant to be expressed and / or isolated. Culture takes place in a suitable nutrient medium comprising carbon and nitrogen sources and inorganic salts, using methods known in the art. Suitable media may be purchased from commercial suppliers or may be prepared according to published compositions (e.g., in the American Type Culture Collection catalogs).If the variant is secreted into the nutrient medium, it can be recovered directly from the medium. If the variant is not secreted, it can be recovered from cellular waste. The variant can be detected using known methods in the art that are specific to variants with protease activity, and can be recovered and purified using known methods in the art. See, for example, WO 2017 / 207762 for further information. Compositions The invention also relates to a composition comprising a subtilase variant of the invention, for example, a detergent or cleaning composition. The invention also relates to a composition comprising a subtilase variant of the invention and further comprising: one or more detergent components; and / or one or more additional enzymes. In a preferred embodiment, the composition is a detergent composition comprising one or more detergent components, in particular one or more non-natural detergent components. The present invention also relates to a composition comprising a subtilase variant of the present invention and further comprising one or more subtilase variants of the present invention and further comprising one or more additional enzymes selected from the group consisting of amylases, catalases, cellulases (e.g., endoglucanases), cutinases, haloperoxygenases, lipases, mannanases, pectinases, pectin lyases, peroxidases, proteases, xantanases, lichenases, and xyloglucanases, or any mixture thereof. A detergent composition can, for example, be in the form of a bar, a homogeneous tablet, a tablet that has two or more layers, a bag that has one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid. In a preferred embodiment, the detergent composition is a powder composition. The invention also relates to the use of a composition of the present invention in a cleaning process, such as washing clothes or cleaning hard surfaces, such as washing dishes. The selection of additional components for a detergent composition is within the expertise of the technician and includes conventional ingredients, including the non-limiting components listed below. For fabric care, the selection of components may include considering the type of fabric to be cleaned, the type and / or degree of soiling, the cleaning temperature, and the formulation of the detergent product. In a particular embodiment, a detergent composition comprises a subtilase variant of the invention and one or more non-natural detergent components, such as surfactants, hydrotropes, enhancers, conditioners, chelators or chelating agents, bleaching system or bleaching components, polymers, fabric tinting agents, fabric conditioners, foam boosters, foam suppressants, dispersants, dye transfer inhibitors, fluorescent bleaching agents, perfume, optical brighteners, bactericides, fungicides, soil suspending agents, soil-releasing polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, and solubilizers. In one embodiment, the subtilase variant of the invention can be added to a detergent composition in an amount corresponding to 0.01 to 200 mg of enzyme protein per liter of washing liquid, preferably 0.05 to 50 mg of enzyme protein per liter of washing liquid, in particular 0.1 to 10 mg of enzyme protein per liter of washing liquid. An automatic dishwasher composition (ADW) may, for example, include 0.001% to 30%, such as 0.01% to 20%, such as 0.1% to 15%, such as 0.5% to 10% of enzymatic protein in i / uuooa i weight of the composition. A granulated composition for laundry may, for example, include 0.001% to 20%, such as 0.01% to 10%, such as 0.05% to 5% of enzymatic protein by weight of the composition. A liquid composition for washing clothes may, for example, include 0.0001% to 10%, such as 0.001% to 7%, such as 0.1% to 5% of the enzymatic protein by weight of the composition. Enzymes such as the subtilase variant of the invention can be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid or a boric acid derivative, e.g., an aromatic borate ester or a phenylboronic acid derivative such as 4-formylphenolboronic acid, and the composition can be formulated as described, for example, in WO 92 / 19709 and WO 92 / 19708, or variants according to the invention can be stabilized using peptide aldehydes or ketones as described in WO 2005 / 105826 and WO 2009 / 118375. The subtilase variants of the invention can be formulated in liquid laundry compositions such as liquid laundry compositions comprising: a) at least 0.01 mg of active subtilase variant per liter of detergent, i / uuooa i b) 2% to 60% by weight of at least one surfactant c) 5 to 50% by weight of at least one detergency improver The detergent composition can be formulated as a granular laundry detergent. Such a detergent may comprise: a) at least 0.01 mg of active protease variant per gram of composition b) anionic surfactant, preferably 5% to 50% by weight c) non-ionic surfactant, preferably 1% to 8% by weight d) surfactant, preferably 5% to 40% by weight, such as carbonates, zeolites, phosphate enhancer, calcium sequestering enhancers or complexing agents. Although the components mentioned below are categorized by a general heading according to a particular functionality, this should not be considered a limitation, as a component may include additional functionalities as will be appreciated by a person skilled in the art. Surfactants The detergent composition may comprise one or more surfactants, which may be anionic, cationic, nonionic, semipolar, and / or zwitterionic, or a mixture thereof. In one particular embodiment, the detergent composition includes a mixture of one or more nonionic surfactants and one or more anionic surfactants. The surfactant(s) are typically present at a level of between approximately 0.1% and 60% by weight, such as between approximately 1% and approximately 40%, or between approximately 3% and approximately 20%, or between approximately 3% and approximately 10%. The surfactant(s) are selected based on the desired cleaning application and include any conventional surfactant(s) known in the art. Any surfactant known in the art for use in detergents may be used.Surfactants reduce surface tension in the detergent, allowing the stain to be lifted and dispersed and then removed by washing. When included in this description, the detergent will typically contain from approximately 1% to approximately 40% by weight, such as approximately 5% to approximately 30%, including approximately 5% to approximately 15% or approximately 20% to approximately 25% of an anionic surfactant. Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS), isomers of LAS, branched alkylbenzenesulfonates (BABS), i / uuooa i phenylalkanesulfonates, alpha-olefinsulfonates (AOS), olefinsulfonates, alkenesulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (as) such as sodium dodecyl sulfate (SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates (FAS), alcohol ether sulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, glycerol and fatty acid sulfonated esters, alpha-sulfonated fatty acid methyl esters (alpha-SFMe or SES) including the sulfonate of a methyl ester (MES), alkyl or alkenylsuccinic acid, dodecenyl / tetradecenylsuccinic acid (DTSA), fatty acid-type derivatives of amino acids, diesters and monoesters of sulfosuccinic acid or soap and combinations thereof. When included in detergent, it will normally contain between approximately 0% and approximately 10% by weight of a cationic surfactant. Non-limiting examples of cationic surfactants include quaternary alkyldimethylethanolamine (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkylated quaternary ammonium compounds, alkoxylated quaternary ammonium compounds (AQA), and combinations thereof. i / uuooa i When included in detergent, it will normally contain between approximately 0.2% and approximately 40% by weight of a non-ionic surfactant, for example, between approximately 0.5% and approximately 30%, in particular between approximately 1% and approximately 20%, between approximately 3% and approximately 10%, such as between approximately 3% and approximately 5% or between approximately 8% and approximately 12%.Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), alcohol propoxylates, propoxylated fatty alcohols (PEA), alkoxylated fatty acid alkyl esters, such as propoxylated and / or ethoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkyl polyglucosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides or A-acyl or A-alkyl glucosamine derivatives (glucamides, GA, or fatty acid glucamide, FAGA), as well as products available under the trade names SPAN and TWEEN. and combinations of these. When included in this description, the detergent will typically contain from approximately 0% to approximately 10% by weight of a semipolar surfactant. Non-limiting examples of semipolar surfactants include amine oxides (AOs) such as alkyldimethylamine oxide, N-(coconut alkyl)-N,N-dimethylamine oxide and N(tallow alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, fatty acid alkanolamides and ethoxylated fatty acid alkanolamides, and combinations thereof. When included in detergent, it will normally contain between approximately 0% and approximately 10% by weight of a zwitterionic surfactant. Non-limiting examples of zwitterionic surfactants include betaine, alkyldimethylbetaine, sulfobetaine, and combinations thereof. Adjuvants and co-adjuvants The detergent composition may contain approximately 0–65% by weight, for example, between approximately 5% and approximately 45%, of a detergent improver or enhancer, or a mixture thereof. In dishwashing detergent, the level of detergency improver is typically 40–65%, particularly 50–65%. Improvers and chelating agents soften, for example, the wash water by separating metal ions from the liquid. The adjuvant and / or aid may be, in particular, a chelating agent that forms water-soluble complexes with Ca and Mg. Any adjuvant and / or aid known in the art for use in laundry detergents may be used. Non-limiting examples of detergent improvers include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, stratified silicates (e.g., Hoechst SKS-6), ethanolamines such as 2-aminoethanol-l-ol (MEA), diethanolamine (DEA, also known as iminodiethanol), triethanolamine (TEA, also known as 2,2',2-nitrilotriethanol) and carboxymethyl inulin (CMI), and combinations thereof. The detergent composition may also contain 0–20% by weight, such as approximately 5% to approximately 10%, of a detergent adjuvant, or a mixture thereof. The detergent composition may include an adjuvant alone or in combination with another adjuvant, for example, a zeolytic adjuvant. Non-limiting examples of adjuvants include polyacrylate homopolymers or copolymers thereof, such as polyacrylic acid (PAA) or the copolymer of acrylic acid and maleic acid (PAA / PMA). Other non-limiting examples include citrate, chelating agents such as aminocarboxylates, aminopolycarboxylates, and phosphonates, and alkyl- or alkenylsuccinic acid. Specific additional examples include 2,2',2-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid,N1 / UUOO» I diacetic acid (GLDA), 1-hydroxyethanol-1,1-diphosphonic acid (HEDP), ethylenediaminetetra-(methylenephosphonic acid) (EDTMPA), diethylenetriaminepentakis(methylenephosphonic acid) (DTPMPA or DTMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA) , α-alanine-N, N-diacetic acid (α-ALDA), serine-N, N-diacetic acid (SEDA), isoserine-N, N-diacetic acid (ISDA), phenylalanine-N, N-diacetic acid (PHDA), anthranilic acid N, N-diacetic acid (ANDA), sulfanilic acid-N, Ndiacetic acid (SLDA), taurine-acid N, N-diacetic acid (TUDA) and sulfomethyl-N, N-diacetic acid (SMDA), N-(2-hydroxyethyl)ethylidenediamine-N, Ν', N'-triacetate (HEDTA),diethanolglycine (DEG), diethylenetriamine penta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof. Additional detergent improvers and conditioners are described, for example, in WO 2009 / 102854 and US 5,977,053. The subtilase variants of the invention can also be formulated in a dishwashing composition, preferably an automatic dishwashing (ADW) composition, comprising: a) at least 0.01 mg of active protease variant according to the invention, and b) 10-50% by weight of detergent improver, preferably selected from citric acid, methylglycine-N,N-diacetic acid (MGDA) and / or glutamic acid-N,N-diacetic acid (GLDA) and mixtures thereof, and c) at least one bleaching component. Bleaching systems Detergent compositions can contain approximately 0–50% by weight, such as approximately 0.1% to approximately 25% of a bleaching system. Bleaching systems remove discoloration, often through oxidation, and many bleaching agents also have strong bactericidal properties and are used for disinfection and sterilization. Any bleaching system known in the art for use in laundry detergents can be used. Suitable bleaching system components include bleaching catalysts, photobleachants, bleach activators, hydrogen peroxide sources such as sodium percarbonate and sodium perborates, preformed peracids, and mixtures thereof. Suitable preformed peracids include, but are not limited to, peroxycarboxylic acids and salts, percarbonic acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts, for example, Oxone (R) and mixtures thereof.Non-limiting examples of bleaching systems include peroxide-based bleaching systems, which may comprise, for example, an inorganic salt, including alkali metal salts such as sodium salts of a perborate (usually mono- or tetrahydrate), salts of percarbonates, persulfates, perphosphates, persilicates, combined with a bleaching activator that forms peracids. The term "bleaching activator" herein refers to a compound that reacts with a peroxy bleaching agent such as hydrogen peroxide to form a peracid. The peracid thus formed constitutes the activated bleaching agent. Suitable bleaching activators that may be used herein include those belonging to the class of ester anhydrides, imides, or amides. Suitable examples are tetracetylethylenediamine (TAED), sodium 4-((3,5,5-trimethylhexanoyl)oxy]benzenesulfonate (ISONOBS), diperoxydodecanoic acid, 4-(dodecanoyloxy)benzenesulfonate (LOBS), 4-(decanoyloxy)benzenesulfonate, 4-(decanoyloxy)benzoate (DOBS), 4-(nonanoyloxy)benzenesulfonate (NOBS) and / or those described in WO 98 / 17767. A particular family of bleaching activators of interest was described in EP 624154 and acetyl triethyl citrate (ATC) is particularly preferred in that family. i / uuooa i ATC or a short-chain triglyceride such as triacetin has the advantage of not polluting the environment since it eventually degrades into citric acid and alcohol. Furthermore, triethyl acetyl citrate and triacetin exhibit good hydrolytic stability in the product during storage and are effective bleaching activators. Finally, ATC provides good detergent-enhancing properties to the laundry additive. Alternatively, the bleaching system may comprise peroxyacids, for example, of the amide, imide, or sulfone type. The bleaching system may also comprise peracids such as 6-(phthalimido)peroxyhexanoic acid (PAP). The bleaching system may also include a bleaching catalyst or a booster. Some non-limiting examples of bleaching catalysts that can be used in the compositions of the present invention include manganese oxalate, manganese acetate, manganese-collagen, cobalt-amine, and manganese-triazacyclononane (MnTACN) catalysts; Manganese complexes with 1,4,7-trimethyl-1,4,7-triazacyclononane (Me3-TACN) or 1,2,4,7-tetramethyl-1,4,7-triazacyclononane (Me4-TACN), particularly Me3-TACN, such as the dinuclear manganese complex [(Me3-TACN)Mn(O)3Mn(Me3TACN)](PF6)2, and [2,2',2''-nitrilotris(ethane-1,2-diylazanylidene-KN-methanyllidene)triphenolate i / uuooa i κ3O]manganese(III). The decolorization catalysts can also be other metallic compounds such as iron or cobalt complexes. In some forms, the bleaching component may be an organic catalyst selected from the group consisting of organic catalysts having the following formula: i / uuooa i (iii) and mixtures thereof; wherein each R1 is independently a branched alkyl group containing from 9 to 24 carbon atoms or a linear alkyl group containing from 11 to 24 carbon atoms, preferably each R1 is independently a branched alkyl group containing from 9 to 18 carbon atoms or a linear alkyl group containing from 11 to 18 carbon atoms, more preferably each R1 is independently selected from the group consisting of 2-propylheptyl, 2-butiloctyl, 2-pentylnonyl, 2-hexyldecyl, n-dodecyl, ntetradecyl, n-hexadecyl, n-octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl. Other illustrative bleaching systems are described, for example, in documents WO 2007 / 087258, WO 2007 / 087244, WO 2007 / 087259 and WO 2007 / 087242. Suitable photobleachants may be, for example, sulfonated zinc phthalocyanine. Hydrotropes A hydrotrope is a compound that solubilizes hydrophobic compounds in aqueous solutions (or, conversely, polar substances in a nonpolar environment). In general, hydrotropes have both hydrophilic and hydrophobic characteristics (so-called amphiphilic properties, as they are known from surfactants); however, the molecular structures of hydrotropes generally do not favor spontaneous self-aggregation (see, for example, the review by Hodgdon and Kaler, 2007, Current Opinion in Colloid & Interface Science 12: 121-128). Hydrotropes do not exhibit any critical concentration above which self-aggregation occurs, as is observed for surfactants and lipids that form micellar, lamellar, or other well-defined mesophases. Instead, many hydrotropes exhibit a continuous aggregation process, in which the sizes of the aggregates grow as the concentration increases.However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing polar and nonpolar substances, including mixtures of water, oil, surfactants, and polymers. Hydrotropes have been classically used in various industries, from pharmaceuticals and personal care to food and technical applications. The use of hydrotropes in detergent compositions allows, for example, more concentrated surfactant formulations (as in the method of compacting liquid detergents by separating water) without inducing undesirable phenomena such as phase separation or high viscosity. The detergent may contain 0-5% by weight, such as approximately 0.5% to approximately 5%, or approximately 3% to approximately 5%, of a hydrotrope. A hydrotrope known in the material may be used in detergents. Non-limiting examples of hydrotropes include sodium benzene sulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium eumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycols, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof. Polymers The detergent may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2%, or 0.2-1% of a polymer. Any polymer known in the art for use in detergents may be used. The polymer may function as a detergency enhancer, as mentioned above, or it may provide anti-redeposition, fiber-protecting, soil-releasing, dye-transfer-inhibiting, grease-cleaning, and / or anti-foaming properties. Some polymers may possess more than one of the properties mentioned above and / or more than one of the properties listed below.Illustrative polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethylene glycol) or poly(ethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl-inulin (CMI) and polycarboxylates such as PAA, PAA / PMA, poly-aspartic acid and copolymers of lauryl methacrylate / acrylic acid, hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethylene terephthalate) (PET-POET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO) and polyvinylpyrolidone-vinylimidazole (PVPVI). Additional exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO), and diquaternary ethoxy sulfate. Other illustrative polymers are described, e.g., in WO 2006 / 130575. Salts of the polymers mentioned above are also covered. Tissue coloring agents The detergent compositions of the present invention may also include fabric-coloring agents such as dyes or pigments which, when formulated in detergent compositions, can be deposited on a fabric when the fabric comes into contact with a washing liquid comprising the detergent compositions and thus alter the fabric's color through the absorption / reflection of visible light. Fluorescent bleaching agents emit at least a certain amount of visible light. In contrast, fabric-coloring agents alter the color of a surface by absorbing at least a portion of the visible light spectrum. Suitable fabric-coloring agents include dyes and dye-clay conjugates, and may also include pigments. Suitable dyes include dyes that are low molecular weight molecules and polymeric dyes.Suitable low molecular weight dyes include dyes that are low molecular weight molecules selected from the group consisting of dyes included in the Color Index (CI) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Red and Basic Violet, or mixtures thereof, for example, as described in documents WO2005 / 003274, WO2005 / 003275, WO2005 / 003276 and EP 1876226 (incorporated herein by reference). The detergent composition preferably comprises from approximately 0.00003% by weight to approximately 0.2% by weight, from approximately 0.00008% by weight to approximately 0.05% by weight, or even from approximately 0.0001% by weight to approximately 0.04% by weight of a fabric coloring agent. The composition may comprise from 0.0001% by weight to 0.2% by weight of a color-enhancing agent for the fabric; this may be particularly preferred when the composition is in the form of a unit-dose bag. Suitable color-enhancing agents are also described, e.g., in documents WO 2007 / 087257 and WO 2007 / 087243. Additional enzymes The detergent additive or detergent composition comprising the subtilase variant of the invention may comprise one or more enzymes such as an amylase, arabinase, carbohydrase, cellulase (e.g., endoglucanase), cutinase, galactanase, haloperoxygenase, lipase, mannanase, oxidase, e.g., laccase and / or peroxidase, pectinase, pectin-lyase, protease, xylanase, xanthanase, and xyloglucanase. The properties of the selected enzyme(s) must be compatible with the selected detergent (e.g., optimal for pH, compatibility with other enzymatic and non-enzymatic ingredients, etc.). Cellulases Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein-engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, for example, the fungal cellulases produced by Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum described in US patents 4,435,307, 5,648,263, 5,691,178, 5,776,757, and WO 89 / 09259. Alkaline or neutral cellulases are particularly suitable for color preservation. Examples of such cellulases include those described in documents EP 495257, EP 531372, WO 96 / 11262, WO 96 / 29397, and WO 98 / 08940. Other examples include cellulase variants such as those described in documents WO 94 / 07998, EP 531315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95 / 24471, WO 98 / 12307, and PCT / DK98 / 00299. Examples of cellulases exhibiting endo-beta1,4-glucanase activity (EC 3.2.1.4) are described in WO 02 / 99091. Other examples of cellulases include the cellulases of family 45 described in WO 96 / 29397, and especially variants thereof having substitution, insertion and / or deletion in one or more of the positions corresponding to the following positions in SEC. ID NO.: 8 of WO 02 / 99091: 2, 4, 7, 8, 10, 13, 15, 19, 20, 21, i / uuooa i 25, 26, 29, 32, 33, 34, 35, 37, 40, 42, 42a, 43, 44, 48, 53, > κ 76 C ι\ CC ο α 54, 55, 58, 59, 63, 64, 65, 66, 67, 70, 72, 76, 79, 80, 82, 5 84, 86, 88, 90, 91, 93, 95, 95d, 95h, 95j , 97, 100, 101, 102, 103, 113, 114, 117, 119, 121, 133, 136, 3,3,3 139, 140a, 141, 143a, 145, 146, 147, 150e, 150j, 151, 152, 153, 154,155, 156, 157, 158, 159, 160c, 160e, 160k, 161, 162, 164, 165,168, 170, 171, 172, 173, 175, 176, 178, 181, 183, 184, 185,186, 188, 191, 192, 195, 196, 200, and / or 20, preferably selected from P19A, G20K, Q44K, N48E, Q119H or Q146 R. Commercially available cells include Celluzyme™, and Carezyme™ (Novozymes A / S), Clazinase™, and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation). Protease The composition may include one or more additional proteases, including those of bacterial, fungal, plant, viral, or animal origin, e.g., plant or microbial origin. Microbial origin is preferred. Chemically modified or protein-engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may be, for example, from the SI family, such as trypsin, or from the S8 family, such as subtilisin. A metalloprotease may be, for example, a thermolysin from, for example, the M4 family, or another metalloprotease such as those from the M5, M7, or M8 families. Examples of metalloproteases are neutral metalloproteases such as described in WO 2007 / 044993 (Genencor Int.) such as those derived from Bacillus amyloliquefaciens. Suitable commercially available protease enzymes include those marketed under the brand names Alcalase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Neutrase®, Everlase®, and Esperase® (Novozymes A / S); those sold under the brand names Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect Prime®, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Ultimase®, Opticlean®, and Optimase® (Danisco / DuPont); Axapem™ (Gist-Brocases NV); and BLAP. (sequence shown in Figure 29 of document US5352604) and variants thereof (Henkel AG) and KAP (subtilisin of Bacillus alkalophilus) from Kao. Lipases and Cutinases Suitable lipases and cutinases include those of bacterial or fungal origin. This includes chemically modified mutant enzymes or those with manipulated proteins. Examples include Thermomyces lipase, e.g., from T. lanuquinosus (formerly Humicola lanuginosa) as described in EP 258068 and EP 305216, and Humicola cutinase, e.g., from H. insolens (document WO). 96 / 13580), lipase from Pseudomonas strains (some of these now renamed Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (document EP 218272), P. espacia (document EP 331376), P. sp. SD705 strain (document WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis (document WO 96 / 12012), GDSL-type Streptomyces lipases (document WO 2010 / 065455), Magnaporthe grisea cutinase (document WO 2010 / 107560), Pseudomonas mendocina cutinase (document US 5,389,536), Thermobifida fusca lipase (document WO 2011 / 084412), Geobacillus stearothermophilus lipase (document WO 2011 / 084417), Bacillus subtilis lipase (document WO 2011 / 084599), and Streptomyces griseus lipase (document WO 2011 / 150157) and S. pristinaespiralis (document WO 2012 / 137147) . Other examples are lipase variants such as those described in documents EP 407225, WO 92 / 05249, WO 94 / 01541, WO 94 / 25578, WO 95 / 14783, WO 95 / 30744, WO 95 / 35381, WO 95 / 22615, WO 96 / 00292, WO 97 / 04079, WO 97 / 07202, WO 00 / 34450, WO 00 / 60063, WO 01 / 92502, WO 2007 / 87508 and WO 2009 / 109500. Preferred marketed lipase-type products include Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades). Still other examples are lipases, sometimes referred to as acyltransferases or perhydrolases, e.g., acyltransferases with homology to lipase A from Candida antarctica (document WO 2010 / 111143), acyltransferase from Mycobacterium smegmatis (document WO 2005 / 056782), perhydrolases of the CE 7 family (document WO 2009 / 067279), and variants of the M. smegmatis perhydrolase, in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (document WO 2010 / 100028). Amylases Suitable amylases that can be used in conjunction with the subtilase variants of the invention may be an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein-engineered mutants are included. The amylases include, for example, alpha-amylases obtained from Bacillus, for example, a special strain of Bacillus licheniformis, described in more detail in document GB 1,296,839. Suitable amylases include amylases having SEC. ID NO.: 2 in WO 95 / 10603, or variants having 90% sequence identity with SEC. ID NO.: 3 therein. Preferred variants are described in WO 94 / 02597, WO 94 / 18314, WO 97 / 43424 and SEC. ID NO.: 4 of WO 99 / 19467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, i / uuooa i 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444. Suitable different amylases include amylases having SEC. ID NO.: 6 in WO 02 / 10355 or variants thereof having 90% sequence identity with SEC. ID NO.: 6. Preferred variants of SEC. ID NO.: 6 are those having a deletion at positions 181 and 182 and a substitution at position 193. Other suitable amylases are hybrid alpha-amylases comprising residues 1 to 33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEC. ID NO.: 6 of WO 2006 / 066594 and residues 36-483 of the alpha-amylase from B. licheniformis shown in SEC. ID NO.: 4 of WO 2006 / 066594, or variants having 90% sequence identity thereof. Preferred variants of this hybrid alpha-amylase are those having a substitution, deletion, or insertion at one or more of the following positions: G48, T49, G107, H156, A181, N190, M197, M201, A209, and Q264. Preferred variants of the hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEC. ID NO.: 6 of WO 2006 / 066594 and residues 36-483 of SEC. ID NO.: 4 are those having the following substitutions: M197T; Η156Υ+Α181Τ+Ν190F+A209V+Q264S; either G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S. Other suitable amylases are amylases having the sequence SEC. ID NO.: 6 in WO 99 / 19467 or variants thereof having 90% sequence identity with SEC. ID NO.: 6. Preferred variants of SEC. ID NO.: 6 are those having a substitution, deletion, or insertion at one or more of the following positions: R181, G182, H183, G184, N195, 1206, E212, E216, and K269. Particularly preferred amylases are those having a deletion at positions R181 and G182, or positions H183 and G184. Other additional amylases that may be used are those having SEC. ID NO.: 1, SEC. ID NO.: 3, SEC. ID NO.: 2 or SEC. ID NO.: 7 of WO 96 / 23873 or variants thereof that have 90% sequence identity with SEC. ID NO.: 1, SEC. ID NO.: 2, SEC. ID NO.: 3 or SEC. ID NO.: 7. The preferred variants of SEC. ID NO.: 1, SEC. ID NO.: 2, SEC. ID NO.: 3 or SEC. Sequence ID No. 7 consists of those with a substitution, deletion, or insertion in one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304, and 476, using SEQ ID 2 of WO 96 / 23873 for numbering. The most preferred variants are those with a deletion in two selected positions from 181, 182, 183, and 184, such as 181 and 182, 182 and 183, or positions 183 and 184. The most preferred amylase variants of SEQ ID No. 1, SEQ ID No. 2, or SEQ ID No.: 7 are those that have a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476. Other amylases that may be used are those amylases having SEC. ID NO.: 2 in WO 2008 / 153815, SEC. ID NO.: 10 in WO 01 / 66712, or variants thereof that have 90% sequence identity with SEC. ID NO.: 2 in WO 2008 / 153815 or 90% sequence identity with SEC. ID NO.: 10 in WO 01 / 66712. The preferred variants of SEC. ID NO.: 10 in WO 01 / 66712 are those having a substitution, deletion, or insertion at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211, and 264. Other suitable amylases are those having SEC. ID NO.: 2 of WO 2009 / 061380 or variants having 90% sequence identity with SEC. ID NO.: 2. Preferred variants of SEC. ID NO.: 2 are those having a C-terminal truncation and / or a substitution, deletion, or insertion at one or more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444, and G475. The most preferred variants of SEC. ID NO. 2 refers to variants with a substitution in one or more of the following positions: Q87E,R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E, and G475K, and / or a deletion in position R180 and / or S181 or T182 and / or G183. The most preferred amylase variants of SEC. ID NO. 2 are those with the following substitutions: N128C+K178L+T182G+Y305R+G475K; N128C+K178L+T182G+F202Y+Y305R+D319T+G475K; S125A+N128C+K178L+T182G+Y305R+G475K; either S125A+N128C+T131I+Tl65I+K178L+T182G+Y305R+G475K, wherein the variants are truncated at the C-terminal end and, optionally, further comprise a substitution at position 243 and / or a deletion at position 180 and / or position 181. Other suitable amylases are those having SEC. ID NO. 1 of WO 2013 / 184577 or variants having 90% sequence identity with SEC. ID NO. 1. Preferred variants of SEC. ID NO. 1 are those having a substitution, deletion, or insertion at one or more of the following positions: K176, R178, G179, 1180, G181, E187, N192, M199, 1203, S241, R458, T459, D460, G476, and G477. The most preferred variants of SEC. ID NO.: 1 are those that have the substitution in one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, i / uuooa i S241QADN, R458N, T459S, D460T, G476K and G477K and / or a deletion at position R178 and / or S179 or of T180 and / or G181. The most preferred amylase variants of SEC. ID NO.: 1 comprise the following substitutions: El87P+1203Y+G476K El87P+1203Y+R458N+T459S+D460T+G476K and, optionally, also include a substitution in position 241 and / or a deletion in position 178 and / or position 179. Other suitable amylases are those having the sequence ID No. 1 of WO 2010 / 104675 or variants having 90% sequence identity with the same sequence ID No. 1. Preferred variants of the sequence ID No. 1 are those having a substitution, deletion, or insertion at one or more of the following positions: N21, D97, V128, K177, R179, S180, I1181, G182, M200, L204, E242, G477, and G478. The most preferred variants of SEC. ID NO.: 1 are those having a substitution in one or more of the following positions: N21D, D97N, V128I, K177L, M200L, L204YF, E242QA, G477K and G478K and / or a deletion in position R179 and / or S180 or 1181 and / or G182. The most preferred amylase variants of SEC. ID NO.: 1 comprise the substitutions N21D+D97N+V128I and, optionally, further comprise a substitution in position 200 and / or a deletion in position 180 and / or position 181. i / uuooa i Other suitable amylases are the alpha-amylase that has SEO. ID NO.: 12 in WO 01 / 66712 or a variant that has at least 90% sequence identity with SEO. ID NO.: 12. Preferred amylase variants are those that have a substitution, deletion, or insertion at one or more of the following positions in SEO. ID NO.: 12 in WO 01 / 66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484.The preferred particular amylases include variants having a deletion of D183 and G184 and having the substitutions R118K, N195F, R320K and R458K, and a variant having additional substitutions in one or more selected positions of the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, the most preferred being a variant having additional substitutions in all of these positions. Other examples are amylase variants such as those described in WO 2011 / 098531, WO 2013 / 001078 and WO 2013 / 001087. Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™ (from Novozymes A / S) and Rapidase™, Purastar™ / Effectenz™, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International Inc. / DuPont). Peroxidases / oxidases Suitable peroxidases / oxidases include those of plant, bacterial, or fungal origin. Chemically modified or protein-engineered mutants are included. Examples of useful peroxidases include Coprinus peroxidases, e.g., from C. cinereus, and variants thereof as described in WO 93 / 24618, WO 95 / 10602, and WO 98 / 15257. Commercially available peroxidases include Guardzyme™ (Novozymes A / S). Attached materials Any detergent components known in the art for use in laundry detergents may also be used. Other optional detergent components include anti-corrosive agents, anti-shrinkage agents, anti-soil redeposition agents, anti-wrinkle agents, bactericides, binders, corrosion inhibitors, disintegrating / breakdown agents, dyes, enzyme stabilizers (including boric acid, borates, CMC and / or polyols such as propylene glycol), fabric conditioners including clays, fillers / processing aids, fluorescent bleaching agents / optical brighteners, foam boosters, foam regulators (soap foam), perfumes, soil suspending agents, softeners, soap foam suppressants, tarnish inhibitors, and absorbent agents, either alone or in combination.Any ingredient known to the technique for use in laundry detergents can be used. The choice of such components falls within the expert's expertise. Dispersants: The detergent compositions of the present invention may also contain dispersants. In particular, powdered detergents may comprise dispersants. Suitable water-soluble organic materials include homo- or copolymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by no more than two carbon atoms. Suitable dispersants are described, for example, in Powdered Detergents, Surfactant Science Series, Volume 71, Marcel Dekker, Inc., 1997. Dye Transfer Inhibitors: The detergent compositions of the present invention may also include one or more dye transfer inhibitors. Suitable polymeric dye transfer inhibitors include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, N-vinylpyrrolidone / N-vinylimidazole copolymers, polyvinyloxazolidones, and polyvinylimidazoles, or mixtures thereof. When present in a composition, the dye transfer inhibitors may be present at levels of approximately 0.0001% to approximately 10%, approximately 0.01% to approximately 5%, or even approximately 0.1% to approximately 3% by weight of the composition. Fluorescent bleaching agent: The detergent compositions of the present invention will also preferably contain additional components that can impart color to the articles being cleaned, such as fluorescent bleaching agents or optical brighteners. When present, the brightener is preferably at a level of approximately 0.01% to approximately 0.5%. Any fluorescent bleaching agent suitable for use in a laundry detergent composition may be used in the composition of the present invention. The most frequently used fluorescent bleaching agents are those belonging to the classes of diaminostilbenesulfonic acid derivatives, diarylpyrazoline derivatives, and bisphenyldistyryl derivatives.Examples of fluorescent bleaching agents of the diaminostilbenosulfonic acid derivative type include the sodium salts of: 4,4'-bis-(2-diethanolamino-4-aniline-s-triazin-6-ylamino) stilbene-2,2'-disulfonate; 4,4'-bis-(2,4-dianilino-striazin-6-ylamino) stilbene-2,2'-disulfonate; 4,4'-bis-(2-aniline-4-(N-methyl-N-2-hydroxyethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-2,1,3-triazol-2-yl)stilbene-2,2'-disulfonate; 4,4'-bis-(2-anilino-4(1methyl-2-hydroxyethylamino)-s-triazin-6-ylamino) stilbene. 2,2'-disulfonate and 2-(stilbyl-4-naphtho-1,2':4,5)-1,2,3-trizol-2-sulfonate. The preferred fluorescent bleaching agents are Tinopal DMS and Tinopal CBS, marketed by Ciba-Geigy AG, Basel, Switzerland. Tinopal DMS is the disodium salt of 4,4'-bis(2-morpholino-4-anilino-s-triazin-6-ylamino)stilbenodisulfonate. Tinopal CBS is the disodium salt of 2,2'-bis(phenylstyryl)disulfonate. The commercially available product Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India, is also a preferred fluorescent bleaching agent. Other fluorescent agents suitable for use in the invention include 1,3-diarylpyrazolines and 7-alkylaminocoumarins. Suitable fluorescent brightener concentrations include low concentrations of approximately 0.01, 0.05, approximately 0.1 or even approximately 0.2% by weight up to high concentrations of 0.5 or even 0.75% by weight. Soil-Releasing Polymers: The detergent compositions of the present invention may also include one or more soil-releasing polymers, which facilitate soil removal from fabrics such as cotton- and polyester-based fabrics, particularly the removal of hydrophobic soil from polyester-based fabrics. The soil-releasing polymers may be, for example, anionic or nonionic terephthalate-based polymers, polyvinylcaprolactam and related copolymers, graft vinyl copolymers, polyester polyamides; see, for example, Chapter 7 in Powdered Detergents, Surfactant Science series, Volume 71, Marcel Dekker, Inc. Another type of soil-releasing polymer is amphiphilic alkoxylated grease-cleaning polymers, which comprise a core structure and a plurality of alkoxylate groups attached to that core structure.The core structure may comprise a polyalkyleneimine-type structure or a polyalkanolamine-type structure, as described in detail in WO 2009 / 087523 (which is incorporated herein by reference). In addition, copolymers with random grafts are suitable soil-releasing polymers. Suitable graft copolymers are described in detail in WO 2007 / 138054, WO 2006 / 108856, and WO 2006 / 113314 (which are incorporated herein by reference). Other soil-releasing polymers are substituted polysaccharide structures, especially substituted cellulosic structures such as modified cellulose derivatives as described in EP 1867808 or WO 03 / 040279 (both of which are incorporated herein by reference). Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides, and mixtures thereof.Suitable cellulosic polymers include anionicly modified cellulose, non-ionicly modified cellulose, cationicly modified cellulose, zwitterionicly modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methylcellulose, carboxymethylcellulose, ethylcellulose, hydroxyethylcellulose, hydroxypropyl methylcellulose, carboxymethylcellulose ester, and mixtures thereof. Anti-redeposition agents: The detergent compositions of the present invention may also include one or more anti-redeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyoxyethylene and / or polyethylene glycol (PEG), acrylic acid homopolymers, acrylic acid-maleic acid copolymers, and ethoxylated polyethyleneimines. The cellulosic-based polymers described in the soil-releasing polymers above may also act as anti-redeposition agents. Other suitable adjuvant materials include, but are not limited to, anti-shrink agents, bactericidal anti-crease agents, binders, carriers, colorants, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, foam suppressants, solvents, and structural agents for liquid detergents and / or agents that elasticize the structure. Detergent product formulation The detergent enzyme(s), i.e., a subtilase variant of the invention and optionally one or more additional enzymes, may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising all such enzymes. A detergent additive comprising one or more enzymes may be formulated, for example, as a granule, liquid, suspension, etc. Preferred detergent additive formulations include granules, particularly dust-free granules, liquids, particularly stabilized liquids, or suspensions. The detergent composition of the invention can be in any convenient form, e.g., a bar, a homogeneous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact, or concentrated liquid. Various detergent formulations are available, such as layers (identical or different phases), pouches, and dosing units for washing machines. i / uuooa i The bags can be configured as single-compartment or multi-compartment. They can be of any shape, configuration, and material suitable for containing the composition, e.g., preventing the composition from being released from the bag before contact with water. The bag is made of a water-soluble film that encloses an internal volume. This internal volume can be divided into compartments within the bag. Preferred films are made of polymeric materials, preferably polymers that form a film or sheet. The preferred polymers, copolymers, or derivatives thereof are selected from water-soluble polyacrylates and acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropyl methylcellulose, maltodextrin, polymethacrylates, and most preferably polyvinyl alcohol copolymers and hydroxypropyl methylcellulose (HPMC).Preferably, the polymer content in the film, for example, PVA, is at least approximately 60%. The preferred average molecular weight will generally be from approximately 20,000 to approximately 150,000. The films may also consist of blended compositions comprising mixtures of water-soluble and hydrolytically degradable polymers such as polylactic acid and polyvinyl alcohol (known by the trade name M8630 and marketed by Chris Craft Inc. Production of Gary, Indiana, USA) plus plasticizers such as glycerol, ethylene glycol, propylene glycol, sorbitol, and mixtures thereof. The bags may comprise a solid laundry detergent composition or partial components and / or a liquid cleaning composition or partial components separated by the water-soluble film.The compartment for liquid components may have a different composition than the compartments containing solids. See, e.g., document US 2009 / 0011970. Detergent ingredients can be physically separated from one another using compartments in water-soluble bags or in different layers of tablets. This prevents negative interactions between components during storage. The different dissolution profiles of each compartment can also result in delayed dissolution of selected components in the washing solution. A liquid or gel detergent that is not dispensed in unit doses may be aqueous and will normally contain at least 20% and up to 95% water by weight, such as up to approximately 70% water, up to approximately 65% ​​water, up to approximately 55% water, up to approximately 45% water, or up to approximately 35% water. Other types of liquids, including but not limited to alkanols, amines, diols, ethers, and polyols, may be included in an aqueous liquid or gel. An aqueous liquid or gel detergent may contain 0–30% of an organic solvent. A liquid or gel detergent may also be non-aqueous. Laundry soap bars The enzymes of the invention can be added to laundry soap bars and used for handwashing clothes, fabrics, and / or textiles. The term laundry soap bar includes laundry tablets, soap bars, combo tablets, syndet tablets, and detergent tablets. Typically, the types of bars differ in the type of surfactant they contain, and the term laundry soap bar includes those containing fatty acid soaps and / or synthetic soaps. Laundry soap bars are solid and therefore not a liquid, gel, or powder at room temperature. The laundry soap bar may contain one or more additional enzymes, protease inhibitors such as peptide aldehydes (or hydrosulfite adduct or hemiacetal adduct), boric acid, borate, borax and / or phenylboronic acid derivatives such as 4-formylphenylboronic acid, one or more synthetic soaps or surfactants, polyols such as glycerin, pH-controlling compounds such as fatty acids, citric acid, acetic acid and / or formic acid, and / or a salt of a monovalent cation and an organic anion where the monovalent cation may be, for example, Na+, K+ or NH4+ and the organic anion may be, for example, formate, acetate, citrate or lactate, so that the salt of a monovalent cation and an organic anion may be, for example, sodium formate. The laundry soap bar may also contain complexing agents such as EDTA and HEDP, perfumes and / or different types of fillers, surfactants, e.g., anionic synthetic surfactants, detergency enhancers, polymeric soil release agents, detergent chelating agents, stabilizing agents, fillers, dyes, colorants, dye transfer inhibitors, alkoxylated polycarbonates, foam suppressants, structuring agents, binders, bleaching agents, bleaching activators, clay soil suppression agents, anti-redeposition agents, polymeric dispersing agents, brighteners, fabric softeners, perfumes and / or other compounds known in the art. The laundry soap bar can be processed in conventional equipment to produce a laundry soap bar such as, but not limited to: mixers, extruders (e.g., a two-stage vacuum extruder), cutters, logo stampers, cooling tunnels, and packaging machines. A premix containing a soap, the enzyme of the invention, optionally one or more additional enzymes, a protease inhibitor, and a salt of a monovalent cation and an organic anion can be prepared, and the mixture then ground. The enzyme and the optional additional enzymes can be added simultaneously with the protease inhibitor, for example, in liquid form. In addition to the mixing and compression stages, the process may further comprise the stages of milling, extrusion, cutting, stamping, cooling, and / or wrapping. Granulated detergent formulations Granular enzymes, comprising an enzyme-containing core and optionally one or more coatings, are commonly used in granular (powder) detergents.The various methods for preparing the core are known in the art and include, for example, a) spray drying of a liquid solution containing enzyme, b) production of layered products with an enzyme coated as a layer around a preformed inert core particle, for example, using a fluidized bed apparatus, c) adsorption of an enzyme onto and / or within the surface of a preformed core, d) extrusion of a paste containing enzymes, e) suspension of a powder containing enzymes in molten wax and spray-drying to produce pelleted products, f) pelleting in a mixer by adding a liquid containing enzymes to a dry powder composition of pelleting components, g) size reduction of enzyme-containing cores by grinding or crushing larger particles, pellets, etc., and h) fluidized bed pelleting. i / uuooa i Enzyme-containing kernels can be dried, for example, using a fluid bed dryer or other methods known for drying pellets in the feed or enzyme industry, to result in a water content of, in general, 0.1 to 10% w / w water. The enzyme-containing cores are optionally coated to improve storage stability and / or reduce dust formation. One type of coating frequently used for enzyme granules in detergents is a salt coating, generally an inorganic salt coating, which can be applied, for example, as a salt solution using a fluidized bed. Other coating materials that can be used include polyethylene glycol (PEG), methylhydroxypropylcellulose (MHPC), and polyvinyl alcohol (PVA). The granules may contain more than one coating, for example, a salt coating followed by an additional coating of a material such as PEG, MHPC, or PVA. The present invention therefore also relates to enzyme granules / particles comprising the subtilase of the invention. In one embodiment, the granule comprises a core, and optionally one or more coatings (outer layers) surrounding the core. The core can have a diameter, measured as the equivalent spherical diameter (volume-based average particle size), of 20 to 2000 pm, particularly 50 to 1500 pm, 100 to 1500 pm or 250 to 1200 pm. In one embodiment, the core comprises one or more polypeptides having the protease activity of the present invention. The core may include additional materials such as fillers, fibrous materials (cellulose or synthetic fibers), stabilizing agents, solubilizing agents, suspending agents, viscosity regulating agents, lightweight spheres, plasticizers, salts, lubricants, and fragrances. The core may include a binder, such as a synthetic polymer, wax, fat, or carbohydrate. The core may include a salt of a multivalent cation, a reducing agent, an antioxidant, a catalyst for peroxide decomposition and / or an acid buffer component, typically as a homogeneous mixture. The core may include an inert particle with the enzyme adsorbed onto it, or applied to the surface, for example, by fluidized bed coating. The core can have a diameter of 20-2000 pm, particularly 50-1500 pm, 100-1500 pm or 250-1200 pm. The core may be surrounded by at least one coating, for example, to improve stability in the i / uuooa i 100 storage, to reduce dust formation during handling, or to color the granule. The optional coating(s) may include a salt coating or other suitable coating materials, such as polyethylene glycol (PEG), methylhydroxypropylcellulose (MHPC), and polyvinyl alcohol (PVA). The coating may be applied in an amount of at least 0.1% by weight of the core, for example, at least 0.5%, at least 1%, at least 5%, at least 10%, or at least 15%. The amount may be at most 100%, 70%, 50%, 40%, or 30%. The coating preferably has a thickness of at least 0.1 pm, particularly at least 0.5 pm, at least 1 pm, or at least 5 pm. In some embodiments, the coating thickness is less than 100 pm, such as less than 60 pm or less than 40 pm. The coating must encapsulate the nuclear unit, forming a substantially continuous layer. A substantially continuous layer is understood to be a coating with few or no openings, so that the nuclear unit it encapsulates / envelops has few or no uncoated areas. In particular, the layer or coating must have a uniform thickness. The coating may also contain other materials as known in the art, e.g., fillers, release agents, pigments, dyes, plasticizers and / or other materials. 101 binders, such as titanium dioxide, kaolin, calcium carbonate or talc. A salt coating may comprise at least 60% by weight of a salt, for example, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight. To provide acceptable protection, the salt coating has a thickness of at least 0.1 pm, for example, at least 0.5 pm, at least 1 pm, at least 2 pm, at least 4 pm, at least 5 pm, or at least 8 pm. In one particular modality, the thickness of the salt coating is below 100 pm, such as below 60 pm, or below 40 pm. Salt can be added from a saline solution where the salt is completely dissolved or from a saline suspension where the fine particles are less than 50 pm, such as less than 10 pm or less than 5 pm. The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water-soluble, in particular having a solubility of at least 0.1 g in 100 g of water at 20°C, preferably at least 0.5 g per 100 g of water, for example, at least 1 g per 100 g of water, or at least 5 g per 100 g of water. The salt can be an inorganic salt, e.g., sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate salts, or salts of simple organic acids (less than 10 i / uuooa i 102 carbon atoms, e.g., 60 or fewer carbon atoms) such as citrate, malonate, or acetate. Examples of cations in these salts include alkali or alkaline earth metal ions, the ammonium ion, or ions of metals from the first transition series, such as sodium, potassium, magnesium, calcium, zinc, or aluminum. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate, or gluconate. In particular, one can use salts of alkali or alkaline earth metals such as sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate, or salts of simple organic acids such as citrate, malonate or acetate. The salt in the coating may have a constant moisture content at 20°C exceeding 60%, particularly exceeding 70%, 80%, or 85%, or it may be another hydrated form of such a salt (e.g., anhydrated). The salt coating may be as described in WO 00 / 01793 or WO 2006 / 034710. Specific examples of suitable salts are NaCl (CH2o°c=76%), Na2CO3(CH20°c=92%), NaN03(CH20°c=73%), Na2HPO4(CH2o°c=95%), Na3PO4(CH25'c=92%), NH4C1 (CH20°c = 7 9.5%), (NH4)2HPO4i / uuooa i 103 (CH2o°c = 93.0%), NH4H2PO4 (CH2o°c = 93.1%), (NH4)2SO4 (CH2o°c=81.1%) ), KCl (CH2o°c=85%) ), K2HPO4(CH2o°c=92%) , KH2PO4 (CH2o°c=96.5%) ), KNO3(CH2o°c=93.5%) , Na2SO4(CH2o°c=93%) , K2SO4(CH2o°c=98%) , KHSO4 (CH2o°c=8.6%) , MgSO4(CH2o°c=90%) , ZnSO4(CH2o°c=90%) and sodium citrate (CH2o°c=86%). Other examples include NaH2PO4, (NH4)H2PO4, CuSO4, Mg(NOs)2and magnesium acetate. The salt may be in an anhydrous form, or it may be a hydrated salt, i.e., a hydrated crystalline salt with one or more waters of crystallization bound together, as described in WO 99 / 32595. Specific examples include anhydrous sodium sulfate (Na2SO4), anhydrous magnesium sulfate (MgSO4), magnesium sulfate heptahydrate (MgSO4·7H2O), zinc sulfate heptahydrate (ZnSO4·7H2O), sodium dibasic phosphate heptahydrate (Na2HPO4·7H2O), magnesium nitrate hexahydrate (Mg(NO3)2(6H2O)), sodium citrate dihydrate, and magnesium acetate tetrahydrate. Preferably, the salt is applied as a salt solution, e.g., using a fluidized bed. Coating materials can be waxy or film-forming. Examples of waxy coating materials include poly(ethylene oxide) (polyethylene glycol, PEG) products with average molecular weights of 1000 to 20000; and ethoxylated nonylphenols, which have 16 to 50 units. 104 of ethylene oxide; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are from 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono-, di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are provided in GB 1483591. The granules may optionally have one or more additional coatings. Examples of suitable coating materials are polyethylene glycol (PEG), methylhydroxypropylcellulose (MHPC), and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are described in WO 93 / 07263 and WO 97 / 23606. The core can be prepared by granulating a mixture of the ingredients, e.g., by a method comprising pelletizing techniques such as crystallization, precipitation, vat coating, fluidized bed coating, fluidized bed agglomeration, rotary spraying, extrusion, compression, spherification, size reduction methods, drum pelletizing and / or high shear pelletizing. Methods for preparing the core can be found in Handbook of Powder Technology; Particle size enlargement by CE Capes; volume 1; 1980; Elsevier. The preparation methods i / uuooa i 105 include known feed and pellet formulation technologies, e.g.: (a) Spray-dried products, wherein a solution containing liquid enzymes is atomized in a spray-drying tower to form small droplets which, during their downward journey to the drying tower, dry to form a particulate material containing enzymes. Very small particles can be produced in this way (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; vol. 71; pp. 140-142; Marcel Dekker). (b) Layered products, wherein the enzyme is in the form of a layer coating a preformed inert nuclear particle, wherein a solution containing the enzyme is atomized, typically in a fluidized bed apparatus where the preformed nuclear particles are fluidized, and the solution containing the enzyme adheres to the nuclear particles and dries to leave a layer of dried enzyme on the surface of the nuclear particle. Particles of a desired size can be obtained in this way if a useful nuclear particle of the desired size can be found. This type of product is described in, e.g., WO 97 / 23606. (c) Absorbed nuclear particles, where instead of having the enzyme as a coating over the nucleus, the enzyme is absorbed onto and / or into the interior of the surface of the nucleus. i / uuooa i 106 A process of this type is described in document WO 97 / 39116. (d) Extruded or granulated products, where a paste containing the enzyme is pressed into pellets or extruded under pressure through a small opening and cut into particles that are subsequently dried. Such particles are usually of considerable size because the material in which the extrusion opening is made (usually a plate with perforated holes) sets a limit on the pressure drop that can be allowed across the extrusion opening. In addition, very high extrusion pressures when using a small opening increase heat generation in the enzyme paste, which is harmful to the enzyme (Michael S. Showell (editor); Powdered detergent; Surfactant Science Series; 1998; vol. 71; pages 140 to 142; Marcel Dekker). (e) Agglomerated products, wherein a powder containing the enzyme is suspended in molten wax and the suspension is sprayed, e.g., through a rotating disc atomizer, into a cooling chamber where the microdroplets solidify rapidly (Michael S. Showell (editor); Powdered Detergent; Surfactant Science Series; 1998; vol. 71; pp. 140-142; Marcel Dekker). The resulting product is one in which the enzyme is uniformly distributed throughout the inert material rather than concentrated on its surface. U.S. Patents Nos. 4,016,040 and 4,713,245 describe i / uuooa i 107 this technique. (f) Mixer pelleting products, wherein an enzyme-containing liquid is added to a dry powder composition of conventional pelleting components. The liquid and powder are mixed in a suitable ratio, and as moisture from the liquid is absorbed into the dry powder, the dry powder components begin to adhere and agglomerate, accumulating particles and forming granules comprising the enzyme. Such a process is described in U.S. Patent No. 4,106,991 and related documents EP 170360, EP 304332, EP 304331, WO 90 / 09440, and WO 90 / 09428. In a particular product of this process, several high-shear mixers can be used as granulators. The granules, consisting of enzyme, fillers, binders, etc., are mixed with cellulose fibers to reinforce the particles, producing what is called T-granule.Reinforced particles are more robust and release less enzymatic dust. (g) Size reduction, wherein the nuclei are produced by milling or crushing larger particles, minigranules, tablets, briquettes, etc., containing the enzyme. The desired nucleus particle fraction is obtained by sieving the milled or crushed product. Oversized and undersized particles may be recycled. Size reduction is described in Martin Rhodes (editor); Principles of l / UUOO» I 108 Powder Technology; 1990; Chapter 10; John Wiley & Sons. (h) Fluidized bed pelletizing. Fluidized bed pelletizing involves suspending particles in an air stream and spraying a liquid onto the fluidized particles through nozzles. The particles struck by the spray microdroplets become moistened and sticky. The sticky particles collide with other particles and adhere to them to form a pellet. (i) The cores may be subjected to drying, such as in a fluid bed dryer. Those skilled in the art may use other methods known for drying granules in the feed or enzyme industries. Drying preferably takes place at a product temperature of 25 to 90°C. For some enzymes, it is important that the enzyme cores contain a low amount of water before coating with salt. If water-sensitive enzymes are coated with salt before the excess water is removed, the water will be trapped within the core and may adversely affect the enzyme's activity. After drying, the cores preferably contain 0.1–10% w / w water. Dust-free granules can be produced, for example, as described in U.S. Patent Nos. 4,106,991 and 4,661,452, and can be optionally coated using methods known in the art. The granules may also contain one or more enzymes 109 additional granules. Each enzyme will then be present in more granules, ensuring a more uniform distribution of the enzymes and also reducing the physical segregation of different enzymes due to different particle sizes. Methods for producing multi-enzyme cogranulates are described in the ip.com description IPCOM000200739D. Another example of enzyme formulation using cogranulates is described in WO 2013 / 188331. The enzyme can also be a protected enzyme prepared according to the method described in document EP 238,216. In one embodiment, the granule further comprises one or more additional enzymes, for example, hydrolase, isomerase, ligase, lyase, oxidoreductase, and transferase. The one or more additional enzymes are preferably selected from the group consisting of acetylxylane esterase, acylglycerol lipolase, amylase, alpha-amylase, beta-amylase, arabinofuranosidase, cellobiohydrolases, cellulase, feruloyl esterase, galactanase, alpha-galactosidase, beta-galactosidase, beta-glucanase, beta-glucosidase, lysophospholipase, lysozyme, alpha-mannosidase, beta-mannosidase (mannanase), phytase, phospholipase A1, phospholipase A2, phospholipase D, protease, pullulanase, pectinoesterase, triacylglycerol lipase, xylanase, beta-xylosidase, or any combination thereof. For further information on enzyme granules and their production, see document WO i / uuooa i 110 2013 / 007594, as well as, for example, documents WO 2009 / 092699, EP 1705241, EP 1382668, WO 2007 / 001262, US 6,472,364, WO 2004 / 074419 and WO 2009 / 102854. Uses The present invention also relates to methods for using subtilase variants according to the invention or compositions thereof in the washing of textiles and fabrics, such as domestic laundry and industrial laundry. The invention also relates to methods for using variants according to the invention or compositions thereof in cleaning hard surfaces such as floors, tables, walls, ceilings, etc., as well as surfaces of hard objects such as cars (car washing) and dishes (dishwashing). The subtilase variants of the present invention can be added and thus become a component of a detergent composition. Therefore, one aspect of the invention relates to the use of a subtilase variant in a cleaning process such as washing and / or cleaning hard surfaces. The detergent composition of the present invention can be formulated, for example, as a detergent composition for hand or machine washing clothes that includes a laundry additive composition suitable for pretreating stained fabrics and an added fabric softener composition. 111 in rinsing, or it can be formulated as a detergent composition that can be used in general domestic hard surface cleaning operations, or it can be formulated for hand or machine dishwashing operations. The cleaning or care process for textile articles can be, for example, a process for washing clothes, washing dishes, or cleaning hard surfaces such as bathroom tiles, floors, tabletops, drains, sinks, and basins. The laundry processes can be, for example, domestic laundry, but they can also be industrial laundry. Furthermore, the invention relates to a process for washing fabrics and / or garments, where the process comprises treating the fabrics with a washing solution containing a detergent composition and at least one protease variant of the invention. The cleaning or care process for textile articles can be carried out, for example, by machine washing or manually. The washing solution can be, for example, an aqueous washing solution containing a detergent composition. In one aspect, the subtilase variants of the invention are used in a cleaning process, for example, a washing process, comprising a short washing cycle, generally a washing cycle of no more than approximately 30 minutes, such as no more than approximately 20 minutes, for example, no more than i / uuooa i 112 approximately 15 minutes or no more than approximately 10 minutes. It has been surprisingly discovered that the subtilase variants of the invention are remarkably effective in short wash cycles lasting, for example, only approximately 10 to 20 minutes. This may, for example, be useful in top-loading washing machines that frequently have short wash cycles or for hand washing clothes. In another aspect, the subtilase variants of the invention are used in a cleaning process, for example, a laundry process, where the wash water is used for more than one load of laundry. In this case, the wash water containing a detergent with a subtilase of the invention can be used in a first wash cycle for a first load of laundry, and then reused one or more times for additional wash cycles with new loads of laundry. Detergents containing a subtilase variant of the invention have been found to substantially maintain washing performance on protease-sensitive stains even after three or more wash cycles. This can be useful, for example, for hand-washed laundry and / or in water-scarce regions. In recent years, there has been a growing interest in replacing components in detergents that are derived from petrochemicals with renewable biological components such as enzymes and polypeptides, without i / uuooa i 113. Compromising washing performance. When the components of detergent compositions change, new enzymatic activities or new enzymes with alternative and / or improved properties compared to previously used detergent enzymes such as proteases, lipases, and amylases are needed to achieve improved or similar washing performance compared to traditional detergent compositions. The invention further relates to the use of subtilase variants of the invention in a process for removing proteinaceous stains. Proteinaceous stains may be stains such as food stains, for example, baby food, cocoa, eggs, or milk, or other stains such as tallow, blood, ink, or paste, or a combination thereof. Washing method The present invention provides a method for washing a fabric, tableware, or a hard surface with a detergent composition comprising a protease variant of the invention. A cleaning method comprises contacting an object with a detergent composition comprising a protease variant of the invention under conditions suitable for cleaning the object. In a preferred embodiment, the detergent composition is used in a laundry or dishwasher process. i / uuooa i 114 Another embodiment relates to a method for removing stains from fabric or tableware, comprising contacting the fabric or tableware with a composition comprising a protease of the invention under conditions suitable for cleaning the object. In the cleaning method of the invention, the object to be cleaned can be any suitable object, such as fabric or a hard surface, such as tableware, a floor, table, wall, etc. Compositions and methods for treating fabrics (e.g., for removing sizing from a textile) using one or more of the proteases of the invention are also contemplated. The protease can be used in any fabric treatment method that is well known in the art (see, e.g., US Patent 6,077,316). For example, in one aspect, the feel and appearance of a fabric are improved by a method comprising contacting the fabric with a protease in a solution. In another aspect, the fabric is treated with the solution under pressure. The detergent compositions of the present invention are suitable for use in laundry and hard surface washing applications, including dishwashing. Accordingly, the present invention includes a method for washing fabric or washing dishes, comprising contacting the fabric / dishes to be washed with a solution comprising the detergent composition according to the invention. The fabric may comprise any fabric that is washable in a suitable environment. 115. Normal user conditions. The tableware may include any tableware such as earthenware, cutlery, ceramic material, plastics such as melamine, metals, porcelain, glass, and acrylic materials. The solution preferably has a pH of approximately 5.5 to approximately 11.5. Compositions with concentrations of approximately 100 ppm, preferably 500 ppm, to approximately 15,000 ppm in solution may be used. Water temperatures typically range from approximately 5°C to approximately 95°C, including approximately 10°C, approximately 15°C, approximately 20°C, approximately 25°C, approximately 30°C, approximately 35°C, approximately 40°C, approximately 45°C, approximately 50°C, approximately 55°C, approximately 60°C, approximately 65°C, approximately 70°C, approximately 75°C, approximately 80°C, approximately 85°C, and approximately 90°C.The water-to-tissue ratio is typically from approximately 1:1 to approximately 30:1. The enzyme(s) of the detergent composition of the invention can be stabilized using conventional stabilizing agents and protease inhibitors, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, different salts such as NaCl; KCl; lactic acid, formic acid, boric acid or a boric acid derivative, e.g., an aromatic borate ester, or a phenylboronic acid derivative 116 such as 4-formylphenylboronic acid, or an aldehyde peptide such as di-, tri- or tetrapeptide aldehydes or aldehyde analogues (either of the form B1-B0-R, wherein R and H, CH3, CX3, CHX2, or CH2X (X=halogen, B0 is a single amino acid residue (preferably with an optionally substituted aliphatic or aromatic side chain); and B1 consists of one or more amino acid residues (preferably one, two or three), optionally comprising an N-terminal protecting group, or as described in WO 2009 / 118375, WO 98 / 13459) or a protein-type protease inhibitor such as RASI, BASI, WASI (bifunctional alpha-amylase / subtilisin inhibitors from rice, barley and wheat) or CI2 or SSI. The composition may be formulated as as described, e.g., in documents WO 92 / 19709, WO 92 / 19708 and US 6,472,364.In some embodiments, the enzymes used in this description are stabilized by the presence of water-soluble sources of zinc (II), calcium (II) and / or magnesium (II) ions in the finished compositions that provide these types of ions to the enzymes, as well as other metal ions (e.g., barium (II), scandium (II), iron (II), manganese (II), aluminum (III), tin (II), cobalt (II), copper (II), nickel (II) and oxovanadium (IV)). The detergent compositions provided in this invention are generally formulated such that, during use in aqueous cleaning operations, the wash water has a pH of approximately 5.0 to approximately 12.5, such i / uuooa i 117 as from approximately 5.0 to approximately 11.5, or from approximately 6.0 to approximately 10.5. In some forms, granular or liquid laundry products are formulated to have a pH of approximately 6 to approximately 8. Techniques for controlling pH at recommended use levels include the use of buffers, alkalis, acids, etc., and are commonly used by the expert in the technique. The present invention is further described by the following examples, which should not be interpreted as limiting the scope of the invention. EXAMPLES Materials and methods Suc-AAPF-pNA activity assay Proteolytic activity can be determined using a method that employs Suc-AAPF-PNA as a substrate. Suc-AAPF-PNA is an abbreviation for N-Succinyl-Alanine-Alanine-Proline-Phenylalanine-p-Nitroanilide and is a blocked peptide that can be cleaved by endoproteases. After cleavage, a free PNA molecule is released, which is yellow and can therefore be measured by visible spectrophotometry at a wavelength of 405 nm. The Suc-AAPF-PNA substrate is manufactured by Bachem (cat. no. L1400, dissolved in DMSO). The protease sample to be analyzed is diluted in i / uuooa i 118 residual activity buffer (Tris 100 mM pH 8.6). The assay is performed by transferring 30 μA of diluted enzyme samples to a 96-well microtiter plate and adding 70 μA of substrate treatment solution (0.72 mg / ml in Tris 100 mM at pH 8.6). The solution is mixed at room temperature and the absorbance is measured every 20 seconds for 5 minutes at an OD of 405 nm. The slope (absorbance per minute) of the time-dependent absorption curve is directly proportional to the activity of the protease in question under the given set of conditions. The protease sample is diluted to a level where the slope is linear. Example 1: Preparation γ purification of polypeptides The mutation and introduction of expression cassettes into Bacillus subtilis were performed using standard methods known to the practitioner. All DNA manipulations were carried out by PCR (e.g., as described in Sambrook et al., 2001, supra) using traditional methods familiar to the practitioner. Recombinant B. subtilis constructs encoding subtilase polypeptides were inoculated and cultured in a complex medium (TBgly) under antibiotic selection for 24 h at 37°C. Shaker flasks containing a rich medium (PS-1: 100 g / L sucrose (Danisco cat. no. 109-0429), 40 g / L bark i / uuooa i 119 of soybean meal, 10g / l of Na2HPO4.12H2O (Merck cat. no. 106579), 0.1ml / L Dowfax63N10 (Dow) at a ratio of 1:100 with overnight culture. The shaker flask culture was carried out for 4 days with shaking at 30°C at 270 rpm. Purification of the culture supernatants was performed as follows: The culture broth was centrifuged at 26,000 x g for 20 minutes, and the supernatant was carefully decanted from the pellet. The supernatant was filtered through a 0.2 µm Nalgene filtration unit to remove any remaining host cells. The pH of the 0.2 µm filtrate was adjusted to pH 8 with 3 M Tris base, and the pH-adjusted filtrate was applied to a Hypercel MEP column (Pall Corporation) equilibrated with 20 mM Tris / HCl, 1 mM CaCl₂, pH 8.0. After washing the column with the equilibration buffer, the column was eluted in stages with 20 mM CH₃COOH / NaOH, 1 mM CaCl₂, pH 4.5. The column fractions were analyzed to determine protease activity using the Suc-AAPF-pNA assay at pH 9 and the peak fractions were pooled.The pH of the MEP Hypercel column pool was adjusted to pH 6 with 20% (v / v) CH3COOH or 3 M Tris base, and the pH-adjusted pool was diluted with deionized water to the same conductivity as MES / NaOH 20 mM, CaC12 2 mM, pH 6.0. The diluted pool was applied to an SP-Sepharose® Fast Flow column (GE Healthcare) equilibrated in MES / NaOH 20 mM, CaC12 2 mM, pH 6.0. 120 After washing the column with the equilibration buffer, the protease variant was eluted with a linear NaCl gradient (0–0.5 M) in the same buffer over five column volumes. Column fractions were analyzed for protease activity using the Suc-AAPF-pNA assay at pH 9, and active fractions were analyzed by SDS-PAGE. Fractions showing only a single band on the Coomassie-stained SDS-PAGE gel were pooled as the purified preparation and used for further experiments. Example 2: Stability tests at different pH values The stability of the variants of the invention was tested in an accelerated stability test under two different sets of conditions: 1) in a low pH stress buffer (4.0), and 2) in a high pH stress buffer (10.5) with LAS (linear alkylbenzene sulfonate). Stability at low pH This assay at a low pH of 4.0 and in the absence of detergent is designed to simulate the conditions during the production of an enzymatic granule and in the granule before addition to a detergent composition. The purified protease samples were diluted with Triton X-100 0.01% to 0.04 and 0.02 mg / ml. A low pH stress buffer (0.1M citric acid, 2mM CaCl₂, 2mM MgSO₄, pH 4.0) was then mixed with the diluted protease. 121 in the well of a 96-well microtiter plate. After incubation at 37°C in an Eppendorf thermomixer with shaking for 0, 60, and 150 min, 20 μA were transferred to a new microtiter plate and mixed with 180 μA of Suc-AAPF-pNA substrate solution (Suc-AAPF-pNA 0.4 mg / ml in 0.1 M Tris, pH 8.6). Activity was determined by linear regression of the initial increase in absorbance at 405 nm, measured every 20 seconds for 3 minutes using a plate reader (SpectraMax® Plus). The half-life (TU) is calculated from the linear regression of log(activity) versus incubation time. The measured half-life of a reference protease having SEC. ID NO.: 1 with the substitutions S9R, P14H, R19L, and N62D is set to 1, and the half-life enhancement factors (TU IF) of other proteases under test are calculated as the half-life of a variant relative to the half-life of the reference protease. High pH stability with LAS This assay at a high pH of 10.5 and in the presence of LAS was designed to simulate the conditions in a detergent composition, where the enzyme is in close contact with the detergent components. The purified protease samples were diluted with Triton X-100 0.01% to 0.04 and 0.02 mg / ml. A high pH stress buffer (180 μA) was then mixed in. 122 0.1 M, 2 mM CaCl2, 2 mM MgSO4 pH 10.5, 0.5% LAS (Thonyl P85 NaLAS) with 20 μA diluted protease in the well of a 96-well microtiter plate. After incubation at 37 °C in an Eppendorf donor thermomixer with shaking for 0, 60, and 150 min, 20 μA were transferred to a new microtiter plate and mixed with 180 μA of Suc-AAPF-pNA substrate solution (0.4 mg / ml Suc-AAPF-pNA in 0.1 M Tris pH 8.6). Activity was determined by linear regression of the initial increase in absorbance at 405 nm measured every 20 seconds for 3 min using a plate reader (SpectraMax® Plus). The half-life (TU) is calculated from the linear regression of log(activity) versus incubation time. The measured half-life of a reference protease having SEC. ID NO.: 1 with the substitutions S9R, P14H, R19L, and N62D is set to 1, and the half-life enhancement factors (TA IF) of other proteases under test are calculated as the half-life of a variant relative to the half-life of the reference protease. The half-life improvement factors of the variants of the invention in both low pH and high pH + LAS stress buffer are provided in Table 1 below, where it can be seen that the variants of the invention have excellent stability under low pH and high pH + LAS conditions compared to the reference protease. I RQQnn / l 7Π7 / Β / Y 123 Table 1: Half-life improvement factor (1½ IF) of variants of the invention Variante T1 / 2 IF pH bajo T% IF pH alto + LAS Referencia (SEC. ID NO.: 1 +S9RP14H R19L N62D) 1.0 1.0 S3T S9R R19L N62DA194P 8.8 3.2 S3T S9R R19L N62D A194P Q245R S259D 9.2 9.6 S3T S9R R19L N43R N62D A194P R275Q 12.5 3.5 S3T S9R R19L N62D P131* A194P 16.8 5.6 S3T S9R R19L N62D P131* A194P Q245R S259D 20.1 18.7 S3T S9R R19L N43R N62D P131* A194P R275Q 19.8 12.8 S3T S9R R19L N43R N62D N76D A194P 15.3 7.4 S3T S9R R19L N43R N62D N76D P131* Α194P 24.8 7.6 S3T S9R R19L N62D Q245R S259D 7.5 5.8 S3T S9R R19L N43R N62D R275Q 8.7 2.5 S3T S9R R19L N62DP131* 13.5 4.2 S3T S9R R19L N62D P131* Q245R S259D 9.9 6.7 S3T S9R R19L N43R N62D P131* R275Q 16.0 5.7 S3T S9R R19L N43R N62D N76D 19.8 5.9 S3T S9R R19L N43R N62D N76D Q245R S259D 23.5 15.9 S3T S9R R19L N43R N62D N76D P131* 16.9 9.0 S9R Α15T G61E N62D V68A Α194P V205I Q245R N261D 7.9 1.3 S9R Α15T G61E V68A Α194P V205I Q245R S259D N261D 6.2 1.6 S9RR19L N43R N62D R275Q 4.9 1.6 S9RR19L N62DP131* 7.3 1.9 S3A S9R R19L N62D Q245R S259D 2.9 2.1 S3A S9RR19L N62DA194P 3.5 1.2 S9R R19L N43R N62D Q245R S259D R275Q 5.9 5.3 S9R R19L N62D P131* Q245R S259D 9.2 7.5. 124 S9R R19L N43R N62D A194P R275Q 6.8 2.6 S9RR19L N62D P13Γ A194P 10.7 5.2 S9RR19L N43R N62D N76D 12.8 5.0 S3A S9R R19L N43R N62D Q245R S259D R275Q 4.0 3.0 S3A S9R R19L N62D P131* Q245R S259D 6.2 6.8 S3A S9R R19L N62D A194P Q245R S259D 4.0 3.4 S3A S9R R19L N43R N62D P131* R275Q 6.6 2.2 S3A S9R R19L N43R N62D A194P R275Q 4.6 1.8 S3A S9R R19L N62D P131* A194P 7.4 3.0 S3A S9R R19L N43R N62D N76D 8.7 3.5 S9R R19L N43R N62D P131* Q245R S259D R275Q 12.9 8.8 S9R R19L N43R N62D A194P Q245R S259D R275Q 7.1 7.3 S9R R19L N62D P131* A194P Q245R S259D 11.3 11.4 S9R R19L N43R N62D N76D Q245R S259D 14.4 14.3 S9R R19L N43R N62D P131* A194P R275Q 14.4 6.2 S9R R19L N43R N62D N76D P131* 24.7 9.9 S9R R19L N43R N62D N76D A194P 16.9 8.7 S3A S9R R19L N62D P131* A194P Q245R S259D 9.1 4.8 S3A S9R R19L N43R N62D N76D Q245R S259D 10.9 9.4 S3A S9R R19L N43R N62D P131* A194P R275Q 9.8 4.5 S3A S9R R19L N43R N62D N76D P131 * 17.8 8.2 S3A S9R R19L N43R N62D N76D A194P 12.6 8.4 S9R R19L N43R N62D N76D P131* Q245R S259D 16.8 17.7 S9R R19L N43R N62D N76D A194P Q245R S259D 12.6 18.7 S9R R19L N43R N62D N76D P131* A194P 16.6 9.8. Example 3: Automatic Mechanical Stress Test (AMSA) The washing performance of the selected proteases was initially tested using the automated mechanical stress assay (AMSA). AMSA is a washing assay. The 125 small-scale method is used to mimic full-scale washing, allowing many proteases to be tested simultaneously due to the small well size and solution volume. In AMSA, the detergent solution containing the protease is brought into contact with the tissue by vigorously shaking the test plate in a regular, oscillating motion to apply mechanical stress. For a more detailed description, see WO 02 / 42740, especially the section Special Modalities of the Method on pages 23 to 24. The AMSA experiments were performed under the experimental conditions listed in Table 2 below with the model laundry detergent for emerging markets (powder) listed in Table 3. The standard fabric samples Chocolate milk with carbon black (PC03) and Blood, milk, ink, extra heated (EMPA117EH) were obtained from Center For Testmaterials BV (CFT, Stoomloggerweg 11, 3133 KT Vlaardingen, The Netherlands) and Swissatest Testmaterialien AG (Mövenstrasse 12, 9015 St. Gallen, Switzerland), respectively. i / uuooa i Table 2: Experimental conditions of the AMSA Laundry detergent model for emerging market (powder) Detergent dosage 2.0 g / L Water hardness 9°dH Ratio 2:1:4.5 (Ca2+:Mg2+: CO32) 126 Water hardness pH 10.2 Protease concentration Enzymatic protein 0.26 and 0.52 mg / L (10 and 20 nM) Test solution volume 160 pL Washing time 20 minutes Washing temperature 25°C Tissue samples Chocolate milk with carbon black (PC03, CFT) Blood, milk, ink, extra heated (EMPA117EH, Swissatest) ι / uuooa i Table 3: List of ingredients for model laundry detergent for emerging market (powder) Ingredient Content (w / w %) * LAS, sodium salt 15.0% Non-ionic surfactant (alcohol ethoxylate; AEO) 2.0% Soda ash 2 0.1% Hydrated sodium silicate 9.9% Zeolite 4A + PCA (copoly(acrylic acid / maleic acid), sodium salt) 12.1% 1.3% Sodium sulfate 31.4% 127 * The amounts in Table 3 correspond to the amount of active compound in the ingredients. The remainder, approximately 8%, consists of the inactive part of the ingredients, mainly water. After AMSA washing, the fabric samples were rinsed in water, dried, and scanned using a flatbed scanner (Epson Expression 10000XL). The cleanliness of the textile samples, and consequently the wash performance of the individual protease, was determined by calculating the intensity of the reflected light from the scanned images. A specially designed software application (Novozymes Color Vector Analyzer) was used. The program retrieves 24-bit pixel values ​​from the image and converts them into red, green, and blue (RGB) values. The intensity value is calculated by adding the RGB values ​​together as vectors and then taking the length of the resulting vector using this formula: Intensity = y / r2+ g2+ b2. Table 4 below provides information on the washing performance of variants of the invention in AMSA on the two stains EMPA117EH and PC-03 at two different protease concentrations, expressed as relative washing performance compared to that of the reference protease with SEC. ID NO.: 1. The relative washing performance values ​​in Table 4 were calculated 1) obtaining an improvement in the value of i / uuooa i 128 intensity in relation to a blank sample by deducting the calculated intensity value of a blank sample, i.e. a stain washed with the model detergent without an enzyme, from the intensity value calculated for a variant of the reference protease, and then 2) dividing the washing performance of the variants (improvement in intensity value in relation to the blank sample) by the washing performance of the reference (improvement in intensity value in relation to the blank sample), in other words: (Tntensity-variant - Intensity-white) / (In tensi dudreference Intensity-white) The AMSA wash results in Table 4 below show that the variants of the invention have a substantially improved wash performance over EMPA117EH compared to the reference protease. Similarly, for PC-03, the wash performance of the variants of the invention is, in most cases, better than that of the reference protease. i / uuooa i Table 4: Relative washing performance in AMSA; improvement over blank in relation to SEC. ID NO.: 1 EMPA117EH PC-03 Variant 10 nM 20 nM 10 nM 20 nM Reference (Savinase®; SEQ ID NO.: 1) 1.00 1.00 1.00 1.00 S3T S9R R19L N62DA194P 1.49 1.40 1.33 1.23 S3T S9R R19L N62D A194P Q245R S259D 1.54 1.52 1.58 1.50 S3T S9R R19L N43R N62D Α194P R275Q 1.46 1.38 1.46 1.33 S3T S9R R19L N62D P131 * A194P 1.51 1.38 1.04 1.07 S3T S9R R19L N62D P131* A194P Q245R S259D 1.49 1.40 1.00 1.13 S3T S9R R19L N43R N62D P131 * Α194P R275Q 1.49 1.33 0.96 1.00 S3T S9R R19L N43R N62D N76D A194P 1.51 1.38 1.42 1.30 S3T S9R R19L N43R N62D N76D P131 * A194P 1.54 1.48 1.04 1.13 S3T S9R R19L N62D Q245R S259D 1.60 1.52 1.46 1.30 S3T S9R R19L N43R N62D R275Q 1.43 1.36 1.33 1.27 S3T S9R R19L N62DP131* 1.57 1.52 1.17 1.20 S3T S9R R19L N62D P131 * Q245R S259D 1.74 1.64 1.75 1.63 S3T S9R R19L N43R N62D P131* R275Q 1.51 1.45 1.21 1.17 S3T S9R R19L N43R N62D N76D 1.49 1.43 1.46 1.37 S3T S9R R19L N43R N62D N76D Q245R S259D 1.60 1.50 1.46 1.40 S3T S9R R19L N43R N62D N76D P131* 1.51 1.43 1.04 1.17 S9R Α15T G61E N62D V68A Α194P V205I Q245R N261D 1.83 1.69 1.58 1.40 S9R Α15T G61E V68A Α194P V205I Q245R S259D N261D 1.63 1.50 1.33 1.23 S9RR19L N43R N62D R275Q 1.49 1.40 1.46 1.33 S9RR19L N62DP131* 1.60 1.50 1.17 1.13 S3A S9R R19L N62D Q245R S259D 1.60 1.52 1.50 1.43 S3A S9RR19L N62DA194P 1.46 1.36 1.33 1.30 S9R R19L N43R N62D Q245R S259D R275Q 1.54 1.45 1.42 1.27 S9R R19L N62D P131* Q245R S259D 1.66 1.57 1.08 1.20 S9R R19L N43R N62D A194P R275Q 1.43 1.36 1.29 1.23 S9RR19L N62D P131* A194P 1.49 1.45 1.17 1.23. ι / uuooa i 130 S9RR19L N43R N62D N76D 1.49 1.40 1.46 1.37 S3A S9R R19L N43R N62D Q245R S259D R275Q 1.49 1.40 1.46 1.37 S3A S9R R19L N62D P131* Q245R S259D 1.51 1.43 1.08 1.13 S3A S9R R19L N62D A194P Q245R S259D 1.51 1.43 1.42 1.30 S3A S9R R19L N43R N62D P131* R275Q 1.40 1.36 1.00 1.07 S3A S9R R19L N43R N62D A194P R275Q 1.43 1.33 1.38 1.33 S3A S9RR19L N62D P131* A194P 1.54 1.45 1.17 1.20 S3A S9R R19L N43R N62D N76D 1.49 1.38 1.46 1.33 S9R R19L N43R N62D P13VQ245R S259D R275Q 1.43 1.38 0.96 1.03 S9R R19L N43R N62D A194P Q245R S259D R275Q 1.57 1.45 1.46 1.37 S9R R19L N62D P131* A194P Q245R S259D 1.49 1.43 1.13 1.17 S9R R19L N43R N62D N76D Q245R S259D 1.63 1.48 1.42 1.33 S9R R19L N43R N62D P131* A194P R275Q 1.49 1.40 1.08 1.13 S9R R19L N43R N62D N76D P131* 1.51 1.52 1.00 1.13 S9R R19L N43R N62D N76D A194P 1.49 1.40 1.42 1.33 S3A S9R R19L N62D P131* A194P Q245R S259D 1.51 1.48 1.13 1.20 S3A S9R R19L N43R N62D N76D Q245R S259D 1.63 1.55 1.50 1.43 S3A S9R R19L N43R N62D P131 * A194P R275Q 1.49 1.40 1.08 1.10 S3A S9R R19L N43R N62D N76D P131 * 1.46 1.43 0.92 1.03 S3A S9R R19L N43R N62D N76D A194P 1.49 1.40 1.46 1.33 S9R R19L N43R N62D N76D P131* Q245R S259D 1.57 1.48 1.08 1.13 S9R R19L N43R N62D N76D A194P Q245R 1.54 1.40 1.38 1.30. ι / uuooa i 131 S259D S9R R19L N43R N62D N76D P131* A194P 1.51 1.43 1.04 1.10 i / uuooa i Ejemplo 4: Lavado with a tergotómetro (TOM) The washing performance of the selected proteases was further tested in a medium-scale tergotometer wash assay (TOM), which allows for the testing of more tissue samples. A TOM essentially consists of a large, temperature-controlled water bath containing up to 16 open metal beakers submerged within it. Each beaker constitutes a small, top-loading washing machine, and during an experiment, each will contain a solution of a specific detergent / enzyme system with both stained and unstained fabrics for evaluation. A rotating stirring arm inside each beaker is used to create mechanical stress, typically at 120 rpm.The TOM provides a link between small-scale experiments, such as AMSA, and slower and more expensive large-scale washing experiments in normal-sized washing machines. TOM experiments were conducted under the experimental conditions listed in Table 5 using the model laundry detergent for emerging markets (powder) as listed in Table 3 above. Standard fabric samples were obtained from both the Center For Testmaterials BV (CFT, 132 Stoomloggerweg 11, 3133 KT Vlaardingen. Netherlands) as Swissatest Testmaterialien AG (Movenstrasse 12, 9015 St. Gallen, Switzerland). Table 5: Experimental conditions of TOM Laundry detergent model for emerging market (powder) Detergent dosage 2.0 g / L Water hardness 9°dH Water hardness ratio 2:1:4.5 (Ca2+:Mg2+:CO32) pH 10.2 Protease concentration 0.13 mg of enzyme protein / L (5 nM) Test solution volume 1 L Stirring speed 120 rpm Washing time 20 minutes Washing temperature 25°C Fabric samples Chocolate milk with carbon black (PC-03, CFT) Blood, milk, ink (PC-05, CFT) Blood, milk, ink (EMPA116, Swissatest) Blood, milk, ink, extra-heated (EMPA117EH, Swissatest) 133 After TOM washing, the tissue samples were rinsed in water and dried. The cleanliness of the tissue samples, and therefore the wash performance of the individual protease, was determined by measuring light emission at 460 nm using a Macbeth Color-Eye 7000 spectrophotometer. The measured remission values ​​were used to calculate the Delta remission value (ARem), which is defined in this invention as the result of a reflectance or remission measurement of a fabric sample at a certain wavelength, in this case 460 nm, minus the remission value of a reference sample, which in this example is a sample washed with the same detergent without an enzyme (blank). The TOM assay results are shown in Table 6 below. Table 7 shows the same results, but with the wash performance values ​​for SEC. ID NO.: 1 set to 1, and with the relative wash performance values ​​of the variants calculated in comparison to SEC. ID NO.: 1. i / uuooa i Table 6: Washing performance in TOM test. Delta remission compared to blank Stain: Variant: PC-03 PC-05 EMPA116 EMPA117EH White (no enzyme) 0 0 0 0 Reference) (SEC. ID NO.: 1) 2.54 4.81 6.71 6.00 Reference 2 (SEC. ID NO.: 1 + S9R1+R+1+19L) 6.64 8.96 9.67 15.15 134 S3T+S9R+R19L+N62D+A194P 5.85 9.91 9.96 14.85 S3T+S9R+R19L+N62D+A194P+ Q245R+S259D 6.98 8.67 8.88 15.328 S3T+S9R+R19L+N62D+A194P+ R275RHHHH 6.77 9.87 9.07 15.27 ινΐΛ / a / zuz i / uuooa i Table 7: Relative washing performance in TOM assays of variants compared to the reference (SEC. ID NO.: 1) based on Table 6 Stain: Variant: PC-03 PC-05 EMPA116 EMPA117EH White (no enzyme) 0 0 0 0 Reference 1 (SEC. ID NO.: 1) 1.00 1.00 2.61 1.86 1.44 2.53 S3T+S9R+R19L+N62D+A194P 2.30 2.06 1.48 2.48 S3T+S9R+R19L+N62D+A194P+ Q245R+S259L+N62D+A194P+ Q245R+S259L+2.275D+ S3T+S9R+R19L+N62D+A194P+ R275RHHHH 2.67 2.05 1.35 2.55 The TOM assay data in Tables 6 and 7 show that the protease variants of the invention have a substantially improved washing performance relative to the protease of SEC. ID NO.: 1 and on par with that of the high-performance but unstable variant of SEC. ID NO.: 1 with the substitutions S9R+P14H+R19L+N62D. 135 Example 5: Washing performance in short wash cycles, conditions for Latin America The washing performance of a variant of the invention on a set of stains consisting of 8 different protease-sensitive stains was tested in the TOM test described in Example 4, under Latin American conditions with a Brazilian powder laundry detergent base without enzymes. The test was performed with a wash temperature of 25°C, without soaking, and a main wash cycle of 12, 15, or 20 min with agitation at 100 cycles / min. The water hardness was 5.6°dH (Ca2+ / Mg2+ / HCO3~ ratio 2:1:4.5), with a detergent dosage of 2.5 g / L. The protease dosage was 10 nM. The set of stains consisted of 8 protease-sensitive stains, marketed by Center For Testmaterials BV (CFT, Stoomloggerweg 11, 3133 KT Vlaardingen, Netherlands) as well as Swissatest Testmaterialien AG (Móvenstrasse 12, 9015 St. Gallen, Switzerland). After washing, the performance of the protease wash on the tested samples was determined by measuring the light emission at 460 nm, as described in Example 4, and calculating a Delta emission value of a tissue sample minus the emission value of a reference sample washed with the same detergent but without an enzyme (blank). Table 8 below shows the sum of the 8 Delta values ​​compared to the blank for i / uuooa protease i 136 reference (SEC. ID NO.: 1) and a protease of the invention (SEC. ID NO.: 1 + S3T+S9R+R19L+ N62D+A194P) determined in short washing cycles of 12, 15 and 20 minutes, respectively. Table 8: Sum of delta values ​​compared to blank for 8 protease-sensitive stains i / uuooa i 12 min. 15 min. 20 min. Reference (SEQ ID NO.: 1) 65 81 87 S3T+S9R+R19L+N62D+A194P 83 98 97 Example 6: Washing performance in dirty wash water, Chinese conditions The washing performance of a variant of the invention on a stain set consisting of 7 different protease-sensitive stains was tested in the TOM test described in Example 4, under Chinese conditions with a Chinese laundry powder detergent marketed by Liby. The test was performed at a wash temperature of 25°C, without soaking, with three wash cycles of 20 minutes each in the same solution. After the first and second wash cycles, the washed stain samples were removed and discarded, and new stain samples were added for a new wash cycle in the same (dirty) wash water. After the 137 Third wash cycle, the samples were rinsed and dried as described in example 4, and the remission was measured. The water hardness was 14°dH (Ca2+ / Mg2+ / HCO3~ ratio 3:2:0), with a detergent dose of 2 g / L. The test was performed with two different protease doses, 9 nM and 12 nM. The stain set consisted of 7 protease-sensitive stains, marketed by Center For Testmaterials BV (CFT, Stoomloggerweg 11, 3133 KT Vlaardingen, The Netherlands) and Swissatest Testmaterialien AG (Mövenstrasse 12, 9015 St. Gallen, Switzerland). After the third wash cycle, the protease wash performance on the third set of stain samples was determined by measuring light emission at 460 nm as described in Example 4, and calculating a Delta emission value as the emission measure of an exemplary sample minus the emission value of a reference sample washed with the same detergent but without an enzyme (blank). Table 9 below shows the sum of the 7 Delta values ​​compared to the blank for the reference protease (SEC. ID NO.: 1) and a protease of the invention (SEC. ID NO.: 1 + S3T+S9R+R19L+ N62D+A194P) determined on the third set of test samples washed in dirty water in which two i / uuooa i washing cycles have already been performed. 138 Table 9: Sum of delta values ​​compared to blank i / uuooa i for 7 protease-sensitive stains protease 9 nM protease 12 nM Reference (SEC. ID NO.: 1) 18 21 S3T+S9R+R19L+N62D+A194P 36 43 Example 7: Washing performance in dirty wash water, conditions for Southeast Asia The washing performance of a variant of the invention on a stain set consisting of 8 different protease-sensitive stains was tested in the TOM test described in Example 4 under Southeast Asian conditions with an enzyme-free Indonesian laundry detergent powder base. The test was conducted at a wash temperature of 25°C, without soaking, and consisted of three wash cycles. Each cycle consisted of a 20-minute main wash in the same wash solution with 30 g of ballast. After each of the first and second wash cycles, the washed stain samples were removed and discarded, and new stain samples were added for a further soaking and washing cycle in the same (dirty) wash water. After the third wash cycle, the samples were rinsed and dried as described in Example 4. Remission was measured at 139. The water hardness was 5.6°dH (Ca2+ / Mg2+ / HCO3~ ratio 2:1:4.5), with a detergent dose of 2 g / L. The test was performed with three different protease doses: 3.4 nM, 4.4 nM, and 5.7 nM. The stain set consisted of 8 protease-sensitive stains, marketed by Center For Testmaterials BV (CFT, Stoomloggerweg 11, 3133 KT Vlaardingen, The Netherlands) and Swissatest Testmaterialien AG (Mövenstrasse 12, 9015 St. Gallen, Switzerland). After the third wash cycle, the protease wash performance on the third set of stain samples was determined by measuring light emission at 460 nm as described in Example 4, and calculating a Delta emission value as the emission measure of an exemplary sample minus the emission value of a reference sample washed with the same detergent but without an enzyme (blank). Table 10 below shows the sum of the 8 Delta values ​​compared to the blank for the reference protease (SEC. ID NO.: 1) and a protease of the invention (SEC. ID NO.: 1 + S3T+S9R+R19L+ N62D+A194P) determined on the third set of test samples washed in dirty water in which two i / uuooa i washing cycles have already been performed. 140 Table 10: Sum of delta values ​​compared to blank i / uuooa i for 8 protease-sensitive stains protease 3.4 nM protease 4.4 nM protease 5.7 nM Reference (SEC. ID NO.: 1) 45 54 57 S3T+S9R+R19L+N62D+A194P 70 78 79 It is hereby stated that, as of this date, the best method known to the applicant for putting the aforementioned invention into practice is the one that is clear from the present description of the invention.

Claims

1. A subtilase variant comprising the substitutions X9R+X19L+X62D, characterized in that (a) the position numbers correspond to positions in the polypeptide of SEQ. ID NO.: 2; (b) the variant has protease activity; and (c) the variant has at least 80% but less than 100% sequence identity with the polypeptide of SEQ. ID NO.: 1; and provided that the variant does not comprise a histidine residue at position 14.

2. The subtilase variant according to claim 1, characterized in that it comprises the substitutions S9R+R19L+N62D, and further comprising at least one alteration selected from the group consisting of S3T, S3A, N43R, V68A, N76D, P131*, A194P, V205I, Q245R, S259D, N261D and R275Q, wherein the position numbers correspond to the positions of the polypeptide of SEC. ID NO.:

2.

3. The subtilase variant of claim 2, characterized because it comprises a set of alterations selected from the group comprising: i / uuooa i 142 • S3T+S9R+R19L+N62D+A194P; • S3T+S9R+R19L+N62D+A194P+Q245R+S259D; • S3T+S9R+R19L+N43R+N62D+A194P+R275Q; • S3T+S9R+R19L+N62D+P131*+A194P; • S3T+S9R+R19L+N62D+P131*+A194P+Q245R+S259D; • S3T+S9R+R19L+N43R+N62D+P131*+A194P+R275Q; • S3T+S9R+R19L+N43R+N62D+N76D+A194P; • S3T+S9R+R19L+N43R+N62D+N76D+P131*+A194P. • S3T+S9R+R19L+N62D+Q245R+S259D; • S3T+S9R+R19L+N43R+N62D+R275Q; • S3T+S9R+R19L+N62D+P131*; • S3T+S9R+R19L+N62D+P131*+Q245R+S259D; • S3T+S9R+R19L+N43R+N62D+P131*+R275Q; • S3T+S9R+R19L+N43R+N62D+N76D; • S3T+S9R+R19L+N43R+N62D+N76D+Q245R+S259D; • S3T+S9R+R19L+N43R+N62D+N76D+P131*; • S9R+A15T+G61E+N62D+V68A+A194P+V205I+Q245R+ N261D; • S9R+A15T+G61E+V68A+A194P+V205I+Q245R+S259D+ N261D; • S9R+R19L+N43R+N62D+R275Q; • S9R+R19L+N62D+P131*; • S3A+S9R+R19L+N62D+Q245R+S259D; • S3A+S9R+R19L+N62D+A194P;• S9R+R19L+N43R+N62D+Q245R+S259D+R275Q; • S9R+R19L+N62D+P131*+Q245R+S259D; 143 • S9R+R19L+N43R+N62D+A194P+R275Q; • S9R+R19L+N62D+P131*+A194P: • S9R+R19L+N43R+N62D+N76D; • S3A+S9R+R19L+N43R+N62D+Q245R+S259D+R275Q; • S3A+S9R+R19L+N62D+P131*+Q245R+S259D; • S3A+S9R+R19L+N62D+A194P+Q245R+S259D; • S3A+S9R+R19L+N43R+N62D+P131*+R275Q; • S3A+S9R+R19L+N43R+N62D+A194P+R275Q; • S3A+S9R+R19L+N62D+P131*+A194P; • S3A+S9R+R19L+N43R+N62D+N76D; • S9R+R19L+N43R+N62D+P131*+Q245R+S259D+R275Q; • S9R+R19L+N43R+N62D+A194P+Q245R+S259D+R275Q; and • S9R+R19L+N62D+P131*+Al94P+Q245R+S259D.; 4. The subtilase variant according to claim 3, characterized in that it comprises or consists of SEC. ID NO.: 1 with one of the sets of alterations.

5. The subtilase variant of any of the preceding claims, characterized in that it comprises the substitutions X3T+X9R+X19L+X62D+X194P.

6. The subtilase variant according to claim 5, characterized in that it comprises the substitutions S3T+S9R+R19L+N62D+A194P.

7. The subtilase variant according to claim 5 or 6, characterized in that it comprises or consists of SEC. ID NO.: 1 with the substitutions l / UUOO» I 144 S3T+S9R+R19L+N62D+A194P.

8. The subtilase variant of any of claims 5 to 7, characterized in that it further comprises at least one alteration selected from the group consisting of N43R, N76D, P131*, Q245R, S259D and R275Q, wherein the position numbers correspond to the positions of the polypeptide of SEC. ID NO.:

2.

9. The subtilase variant according to claim 8, characterized in that it comprises the substitutions Q245R+S259D.

10. The subtilase variant according to claim 9, characterized in that it comprises or consists of SEC. ID NO.: 1 with the substitutions S3T+S9R+R19L+N62D+A194P+Q245R+S259D.

11. The subtilase variant of any of the preceding claims, characterized in that it has a sequence identity of at least 85%, for example, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96% or at least 97%, but less than 100% with the polypeptide of SEC. ID NO.:

1.

12. The subtilase variant of any of the preceding claims, characterized in that it has improved stability compared to a reference protease having SEC. ID NO.: 1 with the substitutions S9R+P14H+R19L+N62D; for example, wherein the variant has improved stability compared to the reference protease when tested in a low pH assay and / or the high pH assay described in Example 2 of this invention.

13. The subtilase variant of any of the preceding claims, characterized in that it has improved washing performance over EMPA117EH compared to the polypeptide of SEC. ID NO.: 1, for example, when tested in the AMSA assay with a protease concentration of 10 nM or 20 nM as described in Example 3 of the present invention.

14. A granule characterized in that it comprises: (a) a core comprising the subtilase variant of any of claims 1 to 13, and optionally (b) a coating consisting of one or more layers surrounding the core.

15. A detergent composition characterized in that it comprises a subtilase variant according to any of claims 1 to 13 or the granule according to claim 14, and at least one detergent component.

16. Use of a subtilase variant according to any of claims 1 to 13, the granule according to claim 14 or the detergent composition according to claim 15 in a cleaning process, such as washing clothes or cleaning hard surfaces, such as washing dishes.

17. A cleaning method, for example, for cleaning dirty clothes or hard surfaces, such as washing dishes, characterized in that it comprises bringing an object into contact with a variant of subtilase according to any of claims 1 to 13, the granule according to claim 14, or the detergent composition according to claim 15 under conditions suitable for cleaning the object.

18. A method for obtaining a subtilase variant, characterized in that it comprises: (a) providing a host cell comprising a polynucleotide encoding a variant of a precursor protease comprising the mutations X9R+X19L+X62D compared to SEQ. ID NO.: 1, wherein the position numbers correspond to the polypeptide positions of SEQ. ID NO.: 2, wherein the variant has protease activity and a sequence identity with SEQ. ID NO.: 1 of at least 80% but less than 100%, and provided that the variant does not comprise a histidine residue at position 14; (b) culturing the host cell under certain conditions suitable for expression of the variant; and (c) recovering the variant.