SERINE PROTEASES OF THE BACILLUS GIBSONII-CLADE

The present disclosure relates to serine proteases cloned from , and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1Bacillus GibsoniiBacillus Gibsonii. A recombinant polypeptide or an active fragment thereof of the -clade , wherein the recombinant polypeptide or active fragment thereof has proteolytic activity and comprises an amino acid sequence having at least 70% identity to the amino acid sequence of SEQ ID NO:4 , 7 , 11 , 15 , 19 , 23 , 49 , 50 , 51 , 52 , 57 , 59 , 61 , 63 , 65 , 67 , 69 , 71 , 73 , 75 , 77 , 79 , 81 , or 83 , wherein said -clade comprises a DXGIXXHSDLXXXGGASXXXXXPTTADLNXHGTH (SEQ ID NO:47) or DXGIXXHSDLXXXGGASXXXXXXTTADLXXHGTH (SEQ ID NO:90) motif , wherein the initial D is the active site Aspartic acid residue and the penultimate H is the active site Histidine , and X is any amino acid , with the proviso that the amino acid sequence does not comprise NCBI Accession Nos. CAE48421 or CAS91385.2. (canceled)3Bacillus Gibsonii. The recombinant polypeptide or active fragment thereof of claim 1 , wherein the -clade comprises SEQ ID NO:47.4Bacillus Gibsonii. The recombinant polypeptide or active fragment thereof of claim 1 , wherein the -clade comprises SEQ ID NO:90.58-. (canceled)9. The recombinant polypeptide or active fragment thereof of claim 1 , with the proviso that the amino acid sequence does not comprise NCBI accession Nos. CAE48421 claim 1 , CAS91385 claim 1 , or AGS78407.10B. gibsonii. The recombinant polypeptide or active fragment thereof of claim 1 , with the proviso that the -clade does not comprise NCBI accession Nos. CAE48421 claim 1 , CAS91385 claim 1 , CAV33594 claim 1 , or AGS78407.11. The recombinant polypeptide or active fragment thereof of claim 1 , wherein the polypeptide has protease activity in the presence of a surfactant.12. (canceled)13. The recombinant polypeptide or active fragment thereof of ...

SERINE PROTEASES OF BACILLUS SPECIES

The present disclosure relates to serine proteases cloned from and , and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1Bacillus akibai/clarkii. A recombinant polypeptide of a -clade subtilisin , or an active fragment thereof , wherein the recombinant polypeptide or the active fragment thereof has proteolytic activity.2. The recombinant polypeptide or the active fragment thereof of claim 1 , wherein the recombinant polypeptide or the active fragment thereof comprises an amino acid sequence of SEQ ID NO:42 claim 1 , 43 claim 1 , 44 claim 1 , 45 claim 1 , 46 claim 1 , 47 claim 1 , or 48.3. The recombinant polypeptide or the active fragment thereof of claim 2 , further comprising an amino acid sequence having at least 70% or 72% identity to an amino acid sequence of SEQ ID NO:3 claim 2 , 6 claim 2 , 11 claim 2 , 14 claim 2 , 17 claim 2 , 20 claim 2 , 23 claim 2 , 26 claim 2 , 29 claim 2 , 32 claim 2 , 35 claim 2 , 38 claim 2 , 41 or 84.46-. (canceled)7. The recombinant polypeptide of claim 1 , wherein the polypeptide has protease activity in the presence of a surfactant.8. The recombinant polypeptide of claim 7 , wherein the protease activity comprises casein hydrolysis.9. The recombinant polypeptide of claim 7 , wherein the polypeptide retains at least 50% of its maximal protease activity at a pH range of 8 to 12 and/or a temperature range of 50° C. to 75° C.10. (canceled)11. The recombinant polypeptide of claim 1 , wherein the polypeptide has cleaning activity in a detergent composition.12. The recombinant polypeptide of claim 11 , wherein the detergent composition is an automatic dish washing detergent.13. The recombinant polypeptide of claim 12 , wherein the cleaning activity comprises hydrolysis of an egg yolk substrate.14. The recombinant polypeptide of claim 11 , wherein the detergent composition is a laundry detergent.1516-. (canceled ...

Compositions and Methods Comprising LG12-CLADE Protease Variants

The present invention provides serine protease enzymes produced from LG12-clade enzymes. In addition, the present invention provides compositions comprising these protease enzymes. In some embodiments, the present invention provides cleaning compositions comprising at least one of these protease enzymes. 1. An LG12-clade variant subtilisin enzyme or an active fragment thereof comprising an amino acid modification to a parent LG12-clade subtilisin enzyme.2Bacillus. An LG12-clade variant subtilisin enzyme or an active fragment thereof comprising an amino acid modification to a parent LG12-clade subtilisin enzyme , wherein the modification is at a productive position of the LG12-clade variant subtilisin enzyme selected from the group consisting of 27 , 40 , 43 , 78 , 98 , 130 , 131 , 158 , 166 , 182 , 237 , 239 , 242 , 245 , and 251 , wherein the amino acid positions of the LG12-clade subtilisin variant are numbered by correspondence with the amino acid sequence of sp. LG12sprC subtilisin set forth in SEQ ID NO:3.3. An LG12-clade variant subtilisin enzyme or an active fragment thereof comprising an amino acid modification to a parent LG12-clade subtilisin enzyme , wherein the modification is at a productive position of the LG12-clade variant subtilisin enzyme , wherein at least 50% of the modifications tested at the productive position meet at least one of the following criteria:a) a position wherein the minimum performance indices (PI) relative to the parent LG12-clade subtilisin enzyme for: 1) at least one cleaning assay selected from PAS-38 microswatch cleaning at pH9 or pH10; and EMPA-116 microswatch cleaning at pH6, pH8, or pH10; 2), activity on suc-AAPF-pNA; 3) protein expression; and 4) at least one stability assay selected from detergent stability and thermostability, are greater than or equal to 0.9, and in addition have a PI for any one of these that is greater than or equal to 1.0;b) a position wherein the minimum performance indices (PI) relative to the ...

Combinatorial variants of glucoamylase with improved specific activity and/or thermostability

Presently provided are variant glucoamylases displaying altered properties, such as improved thermostability and/or specific activity. Also disclosed are DNA sequences coding for the variants, vectors and host cells incorporating the DNA sequence, enzyme compositions, and methods of using the variants in various applications.

Glucoamylase variants with altered properties

The present invention relates to variants of a parent glucoamylase having altered properties (e.g., improved thermostability and/or specific activity). In particular, the present invention provides compositions comprising the variant glucoamylases, including starch hydrolyzing compositions, animal feed compositions and cleaning compositions. The invention also relates to DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells.

Lipid acyltransferase proteins and methods of making them

In one aspect of the present invention there is provided a method for preparing a variant lipid acyltransferase enzyme comprising expressing in a host organism a nucleotide sequence which has at least 90% identity with a nucleotide sequence encoding a parent lipid acyltransferase and comprises at least one modification (suitably at least two modifications) at a position(s) which corresponds in the encoded amino acid sequence to an amino acid(s) located in a) the canyon region of the enzyme (i.e. preferably amino acid residues 31, 27, 85, 86, 119, and 120); and/or b) insertion site 1 (i.e. amino acid residues 22-36) and/or c) insertion site 2 (i.e. amino acid residues 74-88), wherein the canyon region, insertion site 1 and/or insertion site 2 are defined as that region which when aligned based on primary or tertiary structure corresponds to the canyon region, insertion site 1 or insertion site 2 (or the corresponding amino acid residues taught above) of the enzyme shown herein as SEQ ID ...

Cellulase variants with improved expression, activity and stability, and use thereof

The present disclosure relates to cellulase variants. In particular the present disclosure relates to cellulase variants having improved expression, activity and/or stability. Also described are nucleic acids encoding the cellulase variants, compositions comprising the cellulase variants, and methods of use thereof.

Glucoamylase variants

The present invention relates to glucoamylase variants, and especially relates to variants of a starch binding domain (SBD) of glucoamylase. The present invention also relates to the variant having altered properties (e.g., improved thermostability and/or specific activity) compared to a corresponding parent glucoamylase. The present invention also relates to enzyme compositions comprising a variant glucoamylase, DNA constructs comprising polynucleotides encoding the variants and methods of producing the variant glucoamylases in host cells.

Three-dimensional structure of isoprene synthase and its use thereof for generating variants

The present invention provides a three-dimensional structures of P. tremuloides isoprene synthase and P. alba isoprene synthase. The invention also provides methods of using the three dimensional structure to design isoprene synthases with improved activity for increased isoprene production in microbial host cells. Biosynthetically produced isoprene of the present invention finds use in the manufacture of rubber and elastomers.

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Ce17A (formerly Trichoderma reesei cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Beta-glucosidase I variants with improved properties

The present disclosure is generally directed to enzymes and in particular beta-glucosidase variants. Also described are nucleic acids encoding beta-glucosidase variants, compositions comprising beta-glucosidase variants, methods of using beta-glucosidase variants, and methods of identifying additional useful beta-glucosidase variants.

SERINE PROTEASES OF BACILLUS SPECIES

The present disclosure relates to serine proteases cloned from spp., and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1B. agaradhaerens. A -clade of subtilisins comprising one or more motifs selected from(i) DXGIXXXHPDLXXXXXGGXSXXXXXXXXDGNXHGTH (SEQ ID NO:16) motif, wherein the initial D is the active site Aspartic acid, the penultimate H is the active site Histidine, and X is any amino acid;(ii) D(S/T)GIDRSHPDLSXXXXGGXSXXXXXXXXDGNGHGHT (SEQ ID NO:17) motif, wherein the initial D is the active site Aspartic acid, the penultimate H is the active site Histidine, and X is any amino acid; and(iii) DSGIDRSHPDLSANVRGGYSVFGDSPYNDGNGHGTH (SEQ ID NO:18) motif, wherein the initial D is the active site Aspartic acid and the penultimate H is the active site Histidine.2B. agaradhaerens. The -clade of claim 1 , wherein the clade further comprises an alanine at position 160 claim 1 , wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino sequence set forth in SEQ ID NO:3 and are based on conserved linear sequence numbering.3B. agaradhaerens. The -clade of claim 1 , wherein the clade further comprises an amino acid sequence having at least 70% amino acid sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs: 3 claim 1 , 10 claim 1 , 12 claim 1 , and 14.4B. agaradhaerens. The -clade of claim 1 , wherein the subtilisin has protease activity.5. (canceled)6B. agaradhaerens. A recombinant polypeptide or an active fragment thereof of the -clade claim 5 , wherein the recombinant polypeptide or active fragment thereof comprises a DXGIXXXHPDLXXXXXGGXSXXXXXXXXDGN XHGTH (SEQ ID NO: 16) motif claim 5 , wherein the initial D is the active site Aspartic acid claim 5 , the penultimate H is the active site Histidine claim 5 , and X is any amino acid.7. The recombinant polypeptide or an ...

Variants of glucoamylase

The present invention relates to combinatorial variants of a parent glucoamylase that have altered properties for reducing the synthesis of condensation products during hydrolysis of starch. Accordingly, the variants of a parent glucoamylase are suitable such as for use within brewing and glucose syrup production. Also disclosed are DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells.

Variants of glucoamylase

The present invention relates to combinatorial variants of a parent glucoamylase that have altered properties for reducing the synthesis of condensation products during hydrolysis of starch. Accordingly the variants of a parent glucoamylase are suitable such as for use within brewing and glucose syrup production. Also disclosed are DMA constructs encoding the variants and methods of producing the glucoamylase variants in host cells.

Composition comprising various proteorhodopsins and/or bacteriorhodopsins and use thereof

The present invention provides a solid material comprising an immobilized mixture of two or more proteorhodopsins, two or more bacteriorhodopsins, or one or more bacteriorhodopsin and one or more proteorhodopsins. The proteorhodopsins are selected from the group consisting of all-trans-retinal-containing proteorhodopsins and retinal analog-containing proteorhodopsins; all of which have absorption spectra that do not overlap. The bacteriorhodopsins are selected from the group consisting of all-trans-retinal-containing bacteriorhodopsins and retinal analog-containing bacteriorhodopsins; all of which have absorption spectra that do not overlap. The present invention also provides an optical information carrier, such as an optical data storage material and a fraud-proof optical data carrier, comprising the above-described solid material and a substrate selected from the group consisting of glass, paper, metal, fabric material, and plastic material, wherein said solid material is deposited on said substrate. The present invention further provides security ink comprising one or more hydrophilic polymers and a mixture of various photochromic materials.

CELLULASE VARIANTS WITH IMPROVED EXPRESSION, ACTIVITY AND STABILITY, AND USE THEREOF

The present disclosure relates to cellulase variants. In particular the present disclosure relates to cellulase variants having improved expression, activity and/or stability. Also described are nucleic acids encoding the cellulase variants, compositions comprising the cellulase variants, and methods of use thereof. 1. A cellulase variant , wherein the variant is a mature form having cellulase activity and comprising a substitution at one or more positions selected from the group consisting of: 5 , 18 , 19 , 28 , 30 , 32 , 35 , 38 , 79 , 80 , 89 , 100 , 102 , 103 , 104 , 105 , 111 , 117 , 119 , 121 , 125 , 126 , 133 , 137 , 138 , 139 , 140 , 141 , 143 , 150 , 158 , 162 , 177 , 180 , 181 , 182 , 185 , 186 , 188 , 190 , 191 , 192 , 193 , 196 , 201 , 207 , 225 , 226 , 228 , 229 , 230 , 233 , 234 , 236 , 240 , 243 , 245 , 251 , 252 , 258 , 267 , 268 , 274 , 292 , 293 , 303 , 304 , 306 , 307 , 313 , 319 , 322 , 328 , 331 , 338 , 340 , 346 , 361 , 362 , 363 , 364 , 365 , 371 , 384 , 394 , 396 , 400 , 406 , 407 , 414 , 417 , 422 , 427 , 431 , 433 , 436 , 440 , 441 , 443 , 444 , 445 and 447 , wherein the positions are numbered by correspondence with the amino acid sequence of a reference cellobiohydrolase II (CBH2) set forth as SEQ ID NO:3.2. The cellulase variant of claim 1 , wherein the variant comprises a further substitution at one or more further positions selected from:(i) a first group consisting of 63, 77, 129, 146, 147, 151, 153, 157, 161, 189, 194, 197, 203, 204, 208, 211, 237, 239, 244, 247, 254, 277, 281, 285, 288, 289, 294, 327, 339, 344, 356, 378, 382 and 405; or(ii) a second group consisting of 94, 98, 107, 120, 134, 144, 154, 178, 179, 206, 210, 214, 231, 232, 266, 272, 275, 291, 312, 316, 323, 343, 360, 380, 381, 386, 399, 410, 413, 416, 426, and 429,wherein the further positions are numbered by correspondence with the amino acid sequence of the reference cellobiohydrolase II (CBH2) set forth as SEQ ID NO:3.3. A cellulase variant claim 1 , wherein said ...

Combinatorial variants of glucoamylase with improved specific activity and/or thermostability

Presently provided are variant glucoamylases displaying altered properties, such as improved thermostability and/or specific activity. Also disclosed are DNA sequences coding for the variants, vectors and host cells incorporating the DNA sequence, enzyme compositions, and methods of using the variants in various applications.

PROTEIN

The present invention relates to a method for preparing a variant lipolytic enzyme comprising expressing in a host organism a nucleotide sequence which has at least 90% identity with a nucleotide sequence encoding a fungal lipolytic enzyme and comprises at least one modification at a position which corresponds in the encoded amino acid sequence to a) the introduction of at least one glycosylation site in the amino acid sequence compared with the original fungal lipolytic enzyme; b) the introduction of at least one amino acid at a surface position and at a location in an external loop distal to the active site of the enzyme which is more hydrophilic; or c) a substitution or insertion at one or more of positions disclosed herein or a deletion at one or more positions disclosed herein. The invention also relates to polypeptide produced by the method and to novel nucleic acids. 157-. (canceled)58. A method for preparing a variant lipolytic enzyme comprising expressing in a host organism a nucleotide sequence which has at least 90% identity with a nucleotide sequence encoding a fungal lipolytic enzyme and comprises at least one modification at a position which corresponds in the encoded amino acid sequence to the introduction of at least one glycosylation site (or one additional glycosylation site) in the amino acid sequence compared with the original fungal lipolytic enzyme wherein each amino acid position corresponds to the position of the amino acid sequence when aligned with SEQ ID No. 2; wherein when the nucleotide sequence has at least 90% identity with a nucleotide sequence encoding the fungal lipolytic enzyme shown in SEQ ID No. 22 or SEQ ID No. 23 the modification is not a substitution at position 63 and the deletion is not at position 311-312; wherein the nucleotide sequence has at least 90% identity with SEQ ID No. 1 , with SEQ ID No. 24 , or with a nucleotide sequence shown in positions 23-106 of SEQ ID No. 24 , or with a nucleotide sequence shown in ...

Lipid acyltransferase proteins and methods of making them

The present invention provides a method for preparing a variant lipid acyltransferase enzyme by expressing a nucleotide sequence encoding a lipid acyltransferase which may comprise at least one modification at a position(s) which corresponds in the encoded amino acid sequence to an amino acid(s) located in a) the canyon region of the enzyme (i.e. preferably amino acid residues 31, 27, 85, 86, 119, and 120); and/or b) insertion site 1 (i.e. amino acid residues 22-36) and/or c) insertion site 2 (i.e. amino acid residues 74-88), wherein the canyon region, insertion site 1 and/or insertion site 2 are defined as that region which when aligned based on primary or tertiary structure corresponds to the canyon region, insertion site 1 or insertion site 2 (or the corresponding amino acid residues taught above) of the enzyme shown herein as SEQ ID No. 16 or 6 in a host organism.

VARIANTS OF GLUCOAMYLASE

The present invention relates to combinatorial variants of a parent glucoamylase that have altered properties for reducing the synthesis of condensation products during hydrolysis of starch. Accordingly the variants of a parent glucoamylase are suitable such as for use within brewing and glucose syrup production. Also disclosed are DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells. 34-. (canceled)5. The glucoamylase variant according to claim 1 , wherein the glucoamylase variant has at least 85% claim 1 , 90% claim 1 , 95% claim 1 , 98% claim 1 , or 99.5% sequence identity with SEQ ID NO: 1 or 2.67-. (canceled)8. The glucoamylase variant of claim 1 , comprising SEQ ID NO: 1098 or SEQ ID NO: 1099.9. (canceled)10. The glucoamylase variant according to claim 1 , wherein the glucoamylase variant has a starch binding domain that has at least 96% claim 1 , 97% claim 1 , 98% claim 1 , 99% claim 1 , or 99.5% sequence identity with the starch binding domain of SEQ ID NO: 1 claim 1 , 2 claim 1 , 11 claim 1 , 385 claim 1 , 386 claim 1 , 387 claim 1 , 388 claim 1 , 389 claim 1 , or 390.11. The glucoamylase variant according to claim 1 , wherein the glucoamylase variant has a catalytic domain that has at least 80% claim 1 , 85% claim 1 , 90% claim 1 , 95% claim 1 , or 99.5% sequence identity with the catalytic domain of SEQ ID NO: 1 claim 1 , 2 claim 1 , 3 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , or 9.1217-. (canceled)18. The glucoamylase variant according to claim 1 , which glucoamylase exhibit a reduced ratio between isomaltose synthesis and starch hydrolysis activity (IS/SH ratio) as compared to the parent glucoamylase.19. (canceled)20. The glucoamylase variant according to claim 1 , which glucoamylase exhibit an enhanced real degree of fermentation as compared to the parent glucoamylase.2125-. (canceled)26. A polynucleotide encoding a glucoamylase variant according to .27. A vector comprising the ...

COMPOSITION COMPRISING VARIOUS PROTEORHODOPSINS AND/OR BACTERIORHODOPSINS AND USE THEREOF

The present invention provides a solid material comprising an immobilized mixture of two or more proteorhodopsins, two or more bacteriorhodopsins, or one or more bacteriorhodopsin and one or more proteorhodopsins. The proteorhodopsins are selected from the group consisting of all-trans-retinal-containing proteorhodopsins and retinal analog-containing proteorhodopsins; all of which have absorption spectra that do not overlap. The bacteriorhodopsins are selected from the group consisting of all-trans-retinal-containing bacteriorhodopsins and retinal analog-containing bacteriorhodopsins; all of which have absorption spectra that do not overlap. The present invention also provides an optical information carrier, such as an optical data storage material and a fraud-proof optical data carrier, comprising the above-described solid material and a substrate selected from the group consisting of glass, paper, metal, fabric material, and plastic material, wherein said solid material is deposited on said substrate. The present invention further provides security ink comprising one or more hydrophilic polymers and a mixture of various photochromic materials. 1. A solid material comprising an immobilized mixture of one or more bacteriorhodopsins and one or more proteorhodopsins.2. The solid material according to claim 1 , wherein said proteorhodopsins are all-trans-retinal-containing proteorhodopsins and said bacteriorhodopsins are all-trans-retinal-containing bacteriorhodopsins.3. The solid material according to claim 1 , wherein all of said bacteriorhodopsins and proteorhodopsins have different absorption spectra.4. The solid material according to claim 1 , wherein said proteorhodopsins are all-trans-retinal-containing proteorhodopsins or retinal analog-containing proteorhodopsins.5. The solid material according to claim 1 , wherein said solid material comprises one or more hydrophilic polymers that are capable of forming a homogeneous phase with said proteorhodopsins or said ...

BETA-GLUCOSIDASE I VARIANTS WITH IMPROVED PROPERTIES

The present disclosure is generally directed to enzymes and in particular beta-glucosidase variants. Also described are nucleic acids encoding beta-glucosidase variants, compositions comprising beta-glucosidase variants, methods of using beta-glucosidase variants, and methods of identifying additional useful beta-glucosidase variants. 1. A beta-glucosidase 1 (BGL1) variant having at least two improved activities over wild type BGL1 selected from the group consisting of:(a) pre-treated corn stover (PCS) hydrolysis activity,(b) cellobiase activity,(c) protein expression,(d) beta-glucosidase activity measured by a cellobiase activity in the presence of ammonia pretreated corncob (CC) or by a CC hydrolysis activity,(e) thermostability,(f) phosphoric acid swollen cellulose (PASC) hydrolysis activity, and(g) hydrolytic activity in the presence of glucose,wherein the BGL1 variant is any variant as shown in Tables 4-8, 3-2, 4-2 and 4-3.2. A BGL1 variant according to having improved (b) and (d) activities over wild type BGL1 claim 1 , wherein the BGL1 variant is L266A claim 1 , I567E claim 1 , S283F claim 1 , S283P claim 1 , T258E claim 1 , T258I claim 1 , T258K claim 1 , T258Q claim 1 , P536T claim 1 , P536W claim 1 , I532Y claim 1 , Y530T claim 1 , P607D claim 1 , Q406M claim 1 , Q406S claim 1 , V602T claim 1 , G300M claim 1 , A630S claim 1 , A630T claim 1 , T180H claim 1 , T180M claim 1 , A450M claim 1 , I444E claim 1 , I444F claim 1 , I444N claim 1 , I444W claim 1 , I444Y claim 1 , V500Q claim 1 , A633I claim 1 , S482P claim 1 , A667V claim 1 , A485L claim 1 , A485W claim 1 , Y678R claim 1 , V603G claim 1 , L266C claim 1 , I567F claim 1 , S624P claim 1 , P607L claim 1 , G606I claim 1 , G606K claim 1 , G606L claim 1 , G606M claim 1 , G606Q claim 1 , G606V claim 1 , G605E claim 1 , I444V claim 1 , A633V claim 1 , A655W claim 1 , Y678H claim 1 , V522Y claim 1 , G554F claim 1 , L266N claim 1 , F556L claim 1 , S550I claim 1 , S550T claim 1 , S550V claim 1 , T258L claim 1 , ...

Multiply-Substituted Protease Variants

Novel enzyme variants including protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 27, 45, 170, 181, 251 and 271 of subtilisin. Additional variants comprising at least one additional substitution at a position selected from 1, 14, 49, 61, 87, 100, 102, 118, 128, 204 and 258 of subtilisin are also described. 1. A protease variant of a precursor protease , said variant comprising one or more modifications at a charged amino acid residue position , said variant being characterized by having the same net electrostatic charge as said precursor protease.2. The protease variant of claim 1 , wherein said charged amino acid residue position is selected from the group consisting of aspartic acid claim 1 , glutamic acid claim 1 , lysine and arginine.3Bacillus amyloliquefaciens. The protease variant of claim 1 , wherein said variant comprises an amino acid sequence having a substitution at one or more residue positions equivalent to residue positions selected from the group consisting of 27 claim 1 , 45 claim 1 , 170 claim 1 , 181 claim 1 , 251 and 271 of subtilisin as set forth in SEQ ID NO. 2.4. The protease variant of claim 3 , wherein said variant comprising a substitution at one or more positions corresponding to 27 claim 3 , 45 claim 3 , 170 claim 3 , 181 claim 3 , 251 and 271 is a substitution selected from K27T claim 3 , R45N claim 3 , R170S claim 3 , D181N claim 3 , K251G and E271T.5Bacillus amyloliquefaciens. The protease variant of claim 3 ...

Three-dimensional structure of isoprene synthase and its use thereof for generating variants

The present invention provides a three-dimensional structures of P. tremuloides isoprene synthase and P. alba isoprene synthase. The invention also provides methods of using the three-dimensional structure to design isoprene synthases with improved activity for increased isoprene production in microbial host cells. Biosynthetically produced isoprene of the present invention finds use in the manufacture of rubber and elastomers.

ISOPRENE SYNTHASE VARIANTS FOR IMPROVED MICROBIAL PRODUCTION OF ISOPRENE

The present invention provides methods and compositions comprising at least one isoprene synthase enzyme with improved catalytic activity and/or solubility. In particular, the present invention provides variant plant isoprene synthases for increased isoprene production in microbial host cells. Biosynthetically produced isoprene of the present invention finds use in the manufacture of rubber and elastomers. 156-. (canceled)57. An isolated host cell comprising a heterologous polynucleotide sequence encoding an isoprene synthase variant in operable combination with a promoter , wherein said isoprene synthase variant comprises one or more amino acid substitution(s) at one or more amino acid residues corresponding to a poplar isoprene synthase having the sequence of SEQ ID NO: 120 , wherein said substitution(s) are selected from the group consisting of V10M , F12S , T15A , E18G , V58I , V58F , L70Q , L70R , L70V , L70T , T71P , V79L , E89D , G94A , S119F , F120L , G127R , E175V , T212I , S257A , R262G , A266G , F280L , N297K , F305L , L319M , E323K , A328T , D342E , A359T , K366N , E368D , L374M , S396T , V4185 , K438N , H440R , T442A , I449V , A469S , K500R , K505Q , G507S , S509N , F511Y , and N532K; andwherein the variant is capable of more effectively converting dimethylallyl diphosphate (DMAPP) to isoprene, as compared to an isoprene synthase variant without a substitution.58. The host cell of wherein at least one amino acid substitution is a L70R substitution.59. The host cell of wherein at least one amino acid substitution is a G507S substitution.60. The host cell of wherein the variant comprises one of more amino acid substitutions selected from the group consisting of G127R/F511Y claim 57 , L70Q/G94A/R262G/F305L claim 57 , F12S/T15A/E18G/N297K claim 57 , S396T/T442I claim 57 , V10M/E323K claim 57 , F120L/A266G claim 57 , K438N/K500R claim 57 , V79L/S509N claim 57 , E175V/S257A/E368D/A469S claim 57 , T71P/L374M claim 57 , F280L/H440R claim 57 , E89D/H440R claim ...

VARIANTS OF GLUCOAMYLASE

The present invention relates to combinatorial variants of a parent glucoamylase that have altered properties for reducing the synthesis of condensation products during hydrolysis of starch. Accordingly the variants of a parent glucoamylase are suitable such as for use within brewing and glucose syrup production. Also disclosed are DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells. 34-. (canceled)5. The glucoamylase variant according to claim 1 , wherein the glucoamylase variant has at least 85% claim 1 , 90% claim 1 , 95% claim 1 , 98% claim 1 , or 99.5% sequence identity with SEQ ID NO: 1 or 2.67-. (canceled)8. The glucoamylase variant of claim 1 , comprising SEQ ID NO: 1098 or SEQ ID NO: 1099.9. (canceled)10. The glucoamylase variant according to claim 1 , wherein the glucoamylase variant has a starch binding domain that has at least 96% claim 1 , 97% claim 1 , 98% claim 1 , 99% claim 1 , or 99.5% sequence identity with the starch binding domain of SEQ ID NO: 1 claim 1 , 2 claim 1 , 11 claim 1 , 385 claim 1 , 386 claim 1 , 387 claim 1 , 388 claim 1 , 389 claim 1 , or 390.11. The glucoamylase variant according to claim 1 , wherein the glucoamylase variant has a catalytic domain that has at least 80% claim 1 , 85% claim 1 , 90% claim 1 , 95% claim 1 , or 99.5% sequence identity with the catalytic domain of SEQ ID NO: 1 claim 1 , 2 claim 1 , 3 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , or 9.1217-. (canceled)18. The glucoamylase variant according to claim 1 , which glucoamylase exhibit a reduced ratio between isomaltose synthesis and starch hydrolysis activity (IS/SH ratio) as compared to the parent glucoamylase.19. (canceled)20. The glucoamylase variant according to claim 1 , which glucoamylase exhibit an enhanced real degree of fermentation as compared to the parent glucoamylase.2125-. (canceled)26. A polynucleotide encoding a glucoamylase variant according to .27. A vector comprising the ...

COMPOSITION COMPRISING VARIOUS PROTEORHODOPSINS AND/OR BACTERIORHODOPSINS AND USE THEREOF

The present invention provides a solid material comprising an immobilized mixture of two or more proteorhodopsins, two or more bacteriorhodopsins, or one or more bacteriorhodopsin and one or more proteorhodopsins. The proteorhodopsins are selected from the group consisting of all-trans-retinal-containing proteorhodopsins and retinal analog-containing proteorhodopsins; all of which have absorption spectra that do not overlap. The bacteriorhodopsins are selected from the group consisting of all-trans-retinal-containing bacteriorhodopsins and retinal analog-containing bacteriorhodopsins; all of which have absorption spectra that do not overlap. The present invention also provides an optical information carrier, such as an optical data storage material and a fraud-proof optical data carrier, comprising the above-described solid material and a substrate selected from the group consisting of glass, paper, metal, fabric material, and plastic material, wherein said solid material is deposited on said substrate. The present invention further provides security ink comprising one or more hydrophilic polymers and a mixture of various photochromic materials. 1. A solid material comprising an immobilized mixture of one or more bacteriorhodopsins and one or more proteorhodopsins.2. The solid material according to claim 1 , wherein said proteorhodopsins are all-trans-retinal-containing proteorhodopsins and said bacteriorhodopsins are all-trans-retinal-containing bacteriorhodopsins.3. The solid material according to claim 1 , wherein all of said bacteriorhodopsins and proteorhodopsins have different absorption spectra.4. The solid material according to claim 1 , wherein said proteorhodopsins are all-trans-retinal-containing proteorhodopsins or retinal analog-containing proteorhodopsins.5. The solid material according to claim 1 , wherein said solid material comprises one or more hydrophilic polymers that are capable of forming a homogeneous phase with said proteorhodopsins or said ...

GLUCOAMYLASE VARIANTS

The present invention relates to glucoamylase variants. In particular, the invention relates to variants in the starch binding domain (SBD) of a glucoamylase. The invention also relates to variants having altered properties (e.g., improved thermostability and/or increased specific activity) as compared to a corresponding parent glucoamylase. The present invention also provides enzyme compositions comprising the variant glucoamylases; DNA constructs comprising polynucleotides encoding the variants; and methods of producing the glucoamylase variants in host cells. 122-. (canceled)23. An isolated glucoamylase variant comprising a catalytic domain and a starch binding domain (SBD) , a) said catalytic domain comprising at least 85% sequence identity to the amino acid sequence of SEQ ID NO:3 and b) said SBD comprising one or more amino acid substitutions at a position corresponding to position: 3 , 4 , 5 , 11 , 12 , 13 , 18 , 21 , 27 , 28 , 29 , 30 , 35 , 37 , 41 , 43 , 45 , 46 , 47 , 48 , 49 , 50 , 55 , 56 , 57 , 59 , 61 , 71 , 73 , 77 , 79 , 87 , 89 , and 93 of SEQ ID NO: 11 or said SBD comprising one or more amino acid substitutions in an equivalent position to SEQ ID NO: 11 of a parent glucoamylase SBD; wherein the equivalent position in a parent glucoamylase is determined by sequence identity and said parent glucoamylase has at least 80% amino acid sequence identity and less than 100% amino acid sequence identity with SEQ ID NO: 11.24. The isolated glucoamylase variant of claim 23 , wherein the catalytic domain has at least 90% sequence identity to the amino acid sequence of SEQ ID NO:3.25. The isolated glucoamylase variant of claim 23 , wherein the catalytic domain has at least 95% sequence identity to the amino acid sequence of SEQ ID NO:3.26. The isolated glucoamylase variant of claim 23 , wherein said SBD comprises one or more amino acid substitutions at a position corresponding to position: 3 claim 23 , 4 claim 23 , 5 claim 23 , 11 claim 23 , 12 claim 23 , 13 ...

GLUCOSYLTRANSFERASE AMINO ACID MOTIFS FOR ENZYMATIC PRODUCTION OF LINEAR POLY ALPHA-1,3-GLUCAN

Reactions comprising water, sucrose, and one or more glucosyltransferase enzymes are disclosed herein. Glucosyltransferase enzymes used in these reactions comprise certain motifs allowing production of insoluble poly alpha-1,3-glucan having at least 95% alpha-1,3 glycosidic linkages. 1. A reaction solution comprising water , sucrose , and a glucosyltransferase enzyme , wherein said glucosyltransferase enzyme comprises a catalytic domain comprising the following three motifs:(i) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:78,(ii) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:79, and(iii) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:80;wherein said glucosyltransferase enzyme does not comprise residues 54-957 of SEQ ID NO:65, residues 55-960 of SEQ ID NO:30, residues 55-960 of SEQ ID NO:4, residues 55-960 of SEQ ID NO:28, or residues 55-960 of SEQ ID NO:20;{'sub': 'w', 'and wherein the glucosyltransferase enzyme produces insoluble poly alpha-1,3-glucan having at least 95% alpha-1,3 glycosidic linkages and a weight average degree of polymerization (DP) of at least 100.'}2. The reaction solution of claim 1 , wherein the catalytic domain comprises an amino acid sequence that is at least 90% identical to amino acid positions 54-957 of SEQ ID NO:65.3. The reaction solution of claim 2 , wherein:(A) the position of the amino acid sequence that is at least 90% identical to SEQ ID NO:78 aligns with amino acid positions 231-243 of SEQ ID NO:65;(B) the position of the amino acid sequence that is at least 90% identical to SEQ ID NO:79 aligns with amino acid positions 396-425 of SEQ ID NO:65; and/or(C) the position of the amino acid sequence that is at least 90% identical to SEQ ID NO:80 aligns with amino acid positions 549-567 of SEQ ID NO:65.4. The reaction solution of claim 1 , wherein motif (i) comprises SEQ ID NO:78 claim 1 , motif (ii) comprises SEQ ID NO ...

Modified glucosyltransferases for producing branched alpha-glucan polymers

Glucosyltransferase enzymes are disclosed herein that produce branched alpha-glucan polymer. Also disclosed, for example, are polynucleotides encoding these enzymes, as well as methods of producing branched alpha-glucan polymer.

ALPHA-AMYLASE COMBINATORIAL VARIANTS

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

ALPHA-AMYLASE COMBINATORIAL VARIANTS

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing. 1. A recombinant variant of a parent α-amylase comprising pair-wise amino acid substitutions at amino acid residues corresponding to G476 and G477 in SEQ ID NO: 1 , wherein each glycine residue present in the parent α-amylase is independently substituted with an amino acid residue other than glycine , and wherein the variant exhibits improved starch hydrolysis activity compared to the parent.2. The variant of claim 1 , further comprising a mutation at an amino acid residue corresponding to E187 or S241 claim 1 , using SEQ ID NO: 1 for numbering.3. The variant α-amylase of any of the preceding claims claim 1 , further comprising at least one mutation at an amino acid residue corresponding to an amino acid residue selected from the group consisting of N126 claim 1 , Y150 claim 1 , F153 claim 1 , L171 claim 1 , T180 claim 1 , and claim 1 , I203.4. The variant α-amylase of any of the preceding claims claim 1 , further comprising a deletion of at least one amino acid residue corresponding to R178 claim 1 , G179 claim 1 , T180 claim 1 , and G181 claim 1 , using SEQ ID NO: 1 for numbering.5. The variant α-amylase of any of the preceding claims claim 1 , further comprising deletions of amino acid residues corresponding to R178 and G179 claim 1 , or T180 and G181.6. The variant α-amylase of any of the preceding claims claim 1 , further comprising a mutation in an amino acid residue corresponding to an amino acid residue selected from the group consisting of E132 claim 1 , Q167 claim 1 , T180 claim 1 , and A277 claim 1 , using SEQ ID NO: 1 for numbering.7. The variant α-amylase of any of the preceding claims claim 1 , ...

ALPHA-AMYLASE COMBINATORIAL VARIANTS

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

COMPOSITIONS AND METHODS COMPRISING THERMOLYSIN PROTEASE VARIANTS

The present invention provides serine protease—thermoslysine—variants produced there from. Specifically, the present invention provides serine protease variants having one or more substitutions as compared to a reference serine protease. In addition, the present invention provides compositions comprising these serine protease variants. In some embodiments, the present invention provides cleaning compositions comprising at least one of these serine protease variants. 12-. (canceled)3. A thermolysin enzyme variant or an active fragment thereof comprising an amino acid modification to a parent thermolysin enzyme , wherein the modification is a productive position , wherein the modifications tested at the productive position meet the following criteria: a position wherein the minimum performance indices (PI) relative to Thermolysin parent for at least three of the parameters of expression , detergent stability , thermostability , PAS-38 microswatch cleaning activity , or activity on Abz-AGLA-Nba are greater than or equal to 1 , andwherein the productive position is selected from the group consisting of (i) 278, 283, 180, 244, 48 and 63, or (ii) T278R, Q283E, A180E, I244T, T48E and F63C, wherein the amino acid positions of the thermolysin variant are numbered by correspondence with the amino acid sequence of thermolysin set forth in SEQ ID NO: 3.4. (canceled)5. A thermolysin enzyme variant or an active fragment thereof comprising an amino acid modification to a parent thermolysin enzyme , wherein the modification is at a productive position , wherein at least one modification of the modifications tested at the productive position meet the following criteria:a position wherein the minimum performance indices (PI) relative to Thermolysin parent for at least all of the parameters of expression, detergent stability, thermostability, PAS-38 microswatch cleaning activity, or activity on Abz-AGLA-Nba are greater than or equal to 0.5 and no more than one of the parameters is ...

NOVEL METALLOPROTEASES

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof. 1. A metalloprotease polypeptide comprising a calcium binding region.2Bacillus thermoproteolyticus. The polypeptide of claim 1 , wherein the polypeptide comprises a modification in at least one amino acid residue in one of the calcium binding regions claim 1 , Ca1-2 claim 1 , Ca3 and Ca4 claim 1 , (including residues 55-66 claim 1 , 136 claim 1 , 138 claim 1 , 177-190 claim 1 , and 193-200) of the polypeptide claim 1 , wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino acid sequence of metalloprotease set forth in SEQ ID NO: 13.3. The polypeptide of claim 2 , wherein the polypeptide comprises a modification in at least one amino acid residue in a calcium binding region 1-2 of residues 177-190 claim 2 , 136 and 138 of the polypeptide.4. The polypeptide of any of the above claims claim 2 , wherein the polypeptide comprises an amino acid at position 184 selected from the group consisting of lysine claim 2 , threonine claim 2 , alanine claim 2 , glutamic acid and aspartic acid.5. The polypeptide of any of the above claims claim 2 , wherein the amino acid at position 185 is an amino acid other than aspartic acid.6. The polypeptide of claim 5 , wherein the amino acid at position 185 is a non-negatively charged residue.7. The polypeptide of any of or claim 5 , wherein the amino acid at position 185 is a neutrally charged residue.8. The polypeptide of any of - claim 5 , wherein the amino acid at position 185 is an asparagine or serine.9. The polypeptide of any of the above claims claim 5 , wherein the amino acid at position 187 is a non-negatively charged residue.10. The polypeptide of claim 9 , wherein the amino acid at position 187 is a neutrally charged residue.11. The polypeptide of any of or claim 9 , wherein the amino acid at position 187 is a ...

ALPHA-AMYLASE COMBINATORIAL VARIANTS

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing. 1. A recombinant variant of a parent α-amylase comprising:a mutation at an amino acid residue corresponding to E187 or S241; andat least one mutation at an amino acid residue corresponding to an amino acid residue selected from the group consisting of N126, Y150, F153, L171, T180, and, I203;wherein the variant α-amylase or the parent α-amylase has at least 60% amino acid sequence identity relative to SEQ ID NO: 1, which is used for numbering; andwherein the variant has increased thermostability, detergent stability, starch liquifaction activity, and/or cleaning performance compared to the parent α-amylase or a reference α-amylase differing from the variant α-amylase only by the absence of the mutations.2. The variant α-amylase of claim 1 , comprising at least two mutations at amino acid residues corresponding N126 claim 1 , Y150 claim 1 , F153 claim 1 , L171 claim 1 , and claim 1 , I203 claim 1 , using SEQ ID NO: 1 for numbering.3. The variant α-amylase of claim 1 , further comprising a deletion of at least one amino acid residue corresponding to R178 claim 1 , G179 claim 1 , T180 claim 1 , and G181 claim 1 , using SEQ ID NO: 1 for numbering.4. The variant α-amylase of claim 1 , further comprising deletions of amino acid residues corresponding to R178 and G179 claim 1 , or T180 and G181.5. The variant α-amylase of claim 1 , further comprising a mutation at an amino acid residue corresponding to G476 and/or G477 claim 1 , using SEQ ID NO: 1 for numbering.6. The variant α-amylase of claim 1 , further comprising a mutation in an amino acid residue corresponding to an amino acid residue selected from the group ...

SERINE PROTEASES OF BACILLUS SPECIES

The present disclosure relates to serine proteases cloned from spp., and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1. A recombinant polypeptide or an active fragment thereof in the WHY-clade , wherein the polypeptide or active fragment thereof comprises a DTGIDXXHXXLX NLVXTSLGXSXVGGXXXDVXGH motif , wherein the initial D is the active site Aspartic acid , the terminal H is the active site Histidine , and X is any amino acid , with the proviso that the polypeptide does not comprise the amino acid sequence of WO2012175708-0002 , WO2012175708-0004 , WO2012175708-0006 , WP010283106 , or WP006679321.2. The recombinant polypeptide or active fragment thereof of claim 1 , further comprising an amino acid sequence having at least 70% identity to the amino acid sequence of SEQ ID NO:3 claim 1 , SEQ ID NO:4 claim 1 , SEQ ID NO:7 claim 1 , SEQ ID NO:10 claim 1 , SEQ ID NO:11 claim 1 , SEQ ID NO:14 claim 1 , SEQ ID NO:15 claim 1 , SEQ ID NO:22 claim 1 , SEQ ID NO:25 claim 1 , SEQ ID NO:28 claim 1 , SEQ ID NO:31 claim 1 , SEQ ID NO:34 claim 1 , SEQ ID NO:37 claim 1 , SEQ ID NO:40 claim 1 , SEQ ID NO:43 claim 1 , or SEQ ID NO:44.3. The recombinant polypeptide or active fragment thereof of claim 1 , wherein the recombinant polypeptide or active fragment thereof has proteolytic activity.45-. (canceled)6. The recombinant polypeptide or active fragment thereof of claim 1 , wherein the polypeptide or active fragment thereof comprises a DTGIDXXHXXLXaNLVXTSLGXSXVGGXbXXcDVXGH motif claim 1 , wherein the initial D is the active site Aspartic acid claim 1 , the terminal H is the active site Histidine claim 1 , and X claim 1 , Xa claim 1 , Xb claim 1 , and Xc are any amino acid claim 1 , provided that when Xa is arginine claim 1 , Xb and Xc are not glycine.7. The recombinant polypeptide or active fragment thereof of claim 6 , wherein the VXG sequence of the ...

NOVEL METALLOPROTEASES

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof. 1. A metalloprotease polypeptide comprising a calcium binding region.2Bacillus thermoproteolyticus. The polypeptide of claim 1 , wherein the polypeptide comprises a modification in at least one amino acid residue in one calcium binding region selected from Ca1-2 claim 1 , Ca3 and Ca4 claim 1 , wherein said calcium binding region comprises residues 55-66 claim 1 , 136 claim 1 , 138 claim 1 , 177-190 claim 1 , and 193-200 claim 1 , wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino acid sequence of metalloprotease set forth in SEQ ID NO: 13.3Bacillus thermoproteolyticus. The polypeptide of claim 2 , wherein the polypeptide comprises a modification in at least one amino acid residue in the calcium binding region Ca1-2 of residues 177-190 claim 2 , 136 and 138 claim 2 , wherein the amino acid at position 184 is selected from the group consisting of lysine claim 2 , threonine claim 2 , alanine claim 2 , glutamic acid and aspartic acid; at position 185 is an amino acid other than aspartic acid claim 2 , a non-negatively charged residue claim 2 , a neutrally charged residue claim 2 , an asparagine claim 2 , or a serine; at position 187 is a non-negatively charged residue claim 2 , neutrally charged residue claim 2 , leucine claim 2 , methionine claim 2 , or aspartic acid; at position 188 is a leucine claim 2 , valine or methionine; at position 190 is a residue other than glutamic acid or is aspartic acid; at position 177 is a neutrally charged residue claim 2 , aspartic acid or glutamine; at position 178 is a residue selected from the group consisting of glycine claim 2 , serine claim 2 , arginine claim 2 , alanine claim 2 , asparagine claim 2 , and threonine; and/or at position 136 is an aspartic acid or serine claim 2 , wherein the amino acid positions ...

AMYLASE WITH MALTOGENIC PROPERTIES

The present teachings provide an amylase with maltogenic properties. Nucleic acids encoding the maltogenic amylase and variants thereof, expression vectors, formulations, and host cells are also provided. Additional embodiments of the present teachings provide various methods of use and methods of manufacturing. 1. An isolated nucleic acid comprising the nucleotide sequence of SEQ ID NO: 1 or of a degenerate variant of SEQ ID NO: 1.2. An isolated nucleic acid comprising a sequence that encodes a polypeptide consisting of the amino acid sequence of SEQ ID NO: 3.3. An isolated nucleic acid comprising a sequence that hybridizes under stringent conditions to a hybridization probe the nucleotide sequence of which consists of SEQ ID NO: 1 , or the complement of SEQ ID NO: 1.4. An isolated nucleic acid comprising a sequence at least 66% , 67% , 68% , 69% , 70% , 75% , 80% , 85% , 90% , 95% , 98% , 99% , or 99.5% identical to SEQ ID NO: 1.5. The isolated nucleic acid of wherein the nucleic acid encodes a polypeptide that has starch hydrolysis activity.6. An isolated nucleic acid comprising a sequence that encodes a polypeptide at least 66% claim 4 , 67% claim 4 , 68% claim 4 , 69% claim 4 , 70% claim 4 , 75% claim 4 , 80% claim 4 , 85% claim 4 , 90% claim 4 , 95% claim 4 , 98% claim 4 , 99% claim 4 , or 99.5% identical to SEQ ID NO: 3 claim 4 , wherein the polypeptide has starch hydrolysis activity.7. An isolated nucleic acid comprising a sequence that encodes a polypeptide comprising the sequence of SEQ ID NO: 3 claim 4 , or SEQ ID NO: 3 with up to 50 conservative amino acid substitutions claim 4 , wherein the polypeptide has starch hydrolysis activity.8. A purified polypeptide claim 4 , the amino acid sequence of which comprises a sequence at least 66% claim 4 , 67% claim 4 , 68% claim 4 , 69% claim 4 , 70% claim 4 , 75% claim 4 , 80% claim 4 , 85% claim 4 , 90% claim 4 , 95% claim 4 , 98% claim 4 , 99% claim 4 , or 99.5% identical to SEQ ID NO: 3.9. A purified ...

AprL-CLADE PROTEASE VARIANTS AND USES THEREOF

The present disclosure provides AprL-clade protease enzymes, including variant AprL-clade protease enzymes, nucleic acids encoding same, and compositions and methods related to the production and use thereof, including an AprL-clade variant subtilisin enzyme that has improved stability and/or soil removal compared to a parent AprL-clade subtilisin enzyme. 1. An AprL-clade variant subtilisin enzyme or an active fragment thereof comprising one or more amino acid modification to a parent AprL-clade subtilisin enzyme , wherein the modification is selected from: (i) A001C , A001D , A001E , A001Q , A001S , L010M , L010Q , S100G , S102K , S102R , Y103F , Y103M , S104D , G105M , G105R , S108F , S108H , S108K , S108R , E111Q , T114D , T115D , T115E , T115F , T115K , T115Q , N116E , K012C , K012F , K012H , K012M , K012N , K012Q , K012Y , V120S , M123C , M123I , L125I , G127A , G127D , G127I , G127M , G127S , G127T , G127V , A128E , A128H , A128K , A128P , A128R , A128S , A128T , S129H , S129Q , S129R , S129T , S129V , T132C , T132D , T132E , T132K , T132N , T132P , Q136A , Q136C , Q136K , Q136R , V138C , A143D , A143N , G145S , V147L , V148A , V148C , V148M , V148Q , K015A , K015C , K015E , K015I , K015M , K015S , K015T , K015V , S155D , S155F , S155K , S155N , S155R , S157D , S158D , S158I , S158K , S158R , N160C , N160D , N160I , N160M , N160R , T161C , T161D , T161E , T161K , T161Q , T161R , G165A , G165E , G165Q , G165R , G165S , Q017H , A018D , A018E , S181Q , N182D , S183A , S183G , N184C , N184E , N184Q , A186C , S187D , S187E , S187P , Q019D , Q019E , A193D , A193R , A202D , A202E , A202K , A202Q , A202V , G203A , G203C , G203E , G203N , G203Q , Y205E , T210C , T210E , T210I , T210P , T210V , A214E , T215C , L216C , L216H , L216K , L216M , N217S , L234E , L234F , L234Q , L234S , S235D , S235E , P238T , N239A , N239D , N239H , N239M , N239S , N239T , A024E , A024Q , L240D , S241E , S241N , S241Q , S241V , A242G , A242N , S243E , S243Q , S243V , Q244C , Q244E , V245A , ...

GLUCOSYLTRANSFERASE AMINO ACID MOTIFS FOR ENZYMATIC PRODUCTION OF LINEAR POLY ALPHA-1,3-GLUCAN

Reactions comprising water, sucrose, and one or more glucosyltransferase enzymes are disclosed herein. Glucosyltransferase enzymes used in these reactions comprise certain motifs allowing production of insoluble poly alpha-1,3-glucan having at least 95% alpha-1,3 glycosidic linkages. 1. A reaction solution comprising water , sucrose , and a glucosyltransferase enzyme , wherein said glucosyltransferase enzyme comprises a catalytic domain comprising the following three motifs:(i) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:78,(ii) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:79, and(iii) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:80;{'sub': 'w', 'wherein said glucosyltransferase enzyme does not comprise residues 54-957 of SEQ ID NO:65, residues 55-960 of SEQ ID NO:30, residues 55-960 of SEQ ID NO:4, residues 55-960 of SEQ ID NO:28, or residues 55-960 of SEQ ID NO:20; and wherein the glucosyltransferase enzyme produces insoluble poly alpha-1,3-glucan having at least 95% alpha-1,3 glycosidic linkages and a weight average degree of polymerization (DP) of at least 100.'}2. The reaction solution of claim 1 , wherein the catalytic domain comprises an amino acid sequence that is at least 90% identical to amino acid positions 54-957 of SEQ ID NO:65.3. The reaction solution of claim 2 , wherein:(A) the position of the amino acid sequence that is at least 90% identical to SEQ ID NO:78 aligns with amino acid positions 231-243 of SEQ ID NO:65;(B) the position of the amino acid sequence that is at least 90% identical to SEQ ID NO:79 aligns with amino acid positions 396-425 of SEQ ID NO:65; and/or(C) the position of the amino acid sequence that is at least 90% identical to SEQ ID NO:80 aligns with amino acid positions 549-567 of SEQ ID NO:65.4. The reaction solution of claim 1 , wherein motif (i) comprises SEQ ID NO:78 claim 1 , motif (ii) comprises SEQ ID ...

VARIANTS OF CELLOBIOHYDROLASES

Disclosed are a number of homologs and variants of Cel7A (formerly cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted. 1. (canceled)2. An isolated variant of a parent cellobiohydrolase (CBH) enzyme , wherein said variant has cellulase activity , has at least 80% sequence identity to SEQ ID NO:3 , and , wherein said variant comprises an amino acid substitution selected from the group consisting of: F418M , T246S , T255V , and combinations thereof , wherein the position of each amino acid substitution corresponds to SEQ ID NO:3.35-. (canceled)6. The isolated variant of claim 2 , wherein said variant further comprises an amino acid substitution selected from the group consisting of: T246P and T246V.7. The isolated variant of claim 2 , wherein said variant further comprises an amino acid substitution selected from the group consisting of: T255D claim 2 , T255I claim 2 , T255K claim 2 , T255P claim 2 , and T255R.8. The isolated variant of claim 2 , wherein said variant further comprises an amino acid substitution selected from the group consisting of: D241N claim 2 , G234D claim 2 , S92T claim 2 , T41I claim 2 , G234D claim 2 , P194V claim 2 , N200G or N200R claim 2 , N49P claim 2 , Y247D claim 2 , T356L claim 2 , and combinations thereof.9. The isolated variant claim 2 , wherein said parent CBH polypeptide is a fungal cellobiohydrolase 1 (CBH1).10Hypocrea jecorina, Hypocrea schweinitzii, Hypocrea orientalis, Trichoderma pseudokoningii, Trichoderma konilangbra, Trichoderma citrinoviride, Trichoderma harzanium, Aspergillus aculeatus, Aspergillus niger, Penicillium janthinellum, Humicola grisea, Scytalidium thermophilumPodospora anderina.. The isolated variant of claim 9 , wherein said fungal CBH1 is from claim 9 , or1114-. (canceled)15. A host cell ...

VARIANTS OF CELLOBIOHYDROLASES

Disclosed are a number of homologs and variants of Cel7A (formerly cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted. 1. (canceled)2. An isolated variant of a parent cellobiohydrolase (CBH) enzyme , wherein said variant has cellulase activity , has at least 80% sequence identity to SEQ ID NO:3 , and wherein said variant comprises an amino acid substitution selected from the group consisting of: D241N , G234D , P194V , T255I , T255K , T255R , and combinations thereof , wherein the position of each amino acid substitution corresponds to SEQ ID NO:3.39-. (canceled)10. The isolated variant of claim 2 , wherein said variant further comprises an amino acid substitution selected from the group consisting of: F418M claim 2 , T246S or T246P or T246V claim 2 , Y247D claim 2 , N49P claim 2 , N200G or N200R claim 2 , T356L claim 2 , S92T claim 2 , T41I claim 2 , and combinations thereof.11. The isolated variant of claim 2 , wherein said parent CBH polypeptide is a fungal cellobiohydrolase 1 (CBH1).12Hypocrea jecorina, Hypocrea schweinitzii, Hypocrea orientalis, Trichoderma pseudokoningii, Trichoderma konilangbra, Trichoderma citrinoviride, Trichoderma harzanium, Aspergillus aculeatus, Aspergillus niger, Penicillium janthinellum, Humicola grisea, Scytalidium thermophilumPodospora anderina.. The isolated variant of claim 2 , wherein said fungal CBH1 is from claim 2 , or13. (canceled)1416-. (canceled)17. A host cell comprising a polynucleotide sequence encoding a variant of a parent CBH polypeptide according to .18. The host cell of claim 17 , wherein said host cell is a fungal cell or a bacterial cell.19. The host cell of claim 18 , wherein said host cell is selected from the group consisting of:{'i': Trichoderma reesei, Trichoderma longibrachiatum, Trichoderma ...

NOVEL METALLOPROTEASES

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof. 1. A metalloprotease polypeptide comprising a calcium binding region.2Bacillus thermoproteolyticus. The polypeptide of claim 1 , wherein the polypeptide comprises a modification in at least one amino acid residue in one of the calcium binding regions claim 1 , Ca1-2 claim 1 , Ca3 and Ca4 claim 1 , (including residues 55-66 claim 1 , 136 claim 1 , 138 claim 1 , 177-190 claim 1 , and 193-200) of the polypeptide claim 1 , wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino acid sequence of metalloprotease set forth in SEQ ID NO: 13.3. The polypeptide of claim 2 , wherein the polypeptide comprises a modification in at least one amino acid residue in a calcium binding region 1-2 of residues 177-190 claim 2 , 136 and 138 of the polypeptide.4. The polypeptide of any of the above claims claim 2 , wherein the polypeptide comprises an amino acid at position 184 selected from the group consisting of lysine claim 2 , threonine claim 2 , alanine claim 2 , glutamic acid and aspartic acid.5. The polypeptide of any of the above claims claim 2 , wherein the amino acid at position 185 is an amino acid other than aspartic acid.6. The polypeptide of claim 5 , wherein the amino acid at position 185 is a non-negatively charged residue.7. The polypeptide of any of or claim 5 , wherein the amino acid at position 185 is a neutrally charged residue.8. The polypeptide of any of - claim 5 , wherein the amino acid at position 185 is an asparagine or serine.9. The polypeptide of any of the above claims claim 5 , wherein the amino acid at position 187 is a non-negatively charged residue.10. The polypeptide of claim 9 , wherein the amino acid at position 187 is a neutrally charged residue.11. The polypeptide of any of or claim 9 , wherein the amino acid at position 187 is a ...

AprL-CLADE PROTEASE VARIANTS AND USES THEREOF

The present disclosure provides AprL-clade protease enzymes, including variant AprL-clade protease enzymes, nucleic acids encoding same, and compositions and methods related to the production and use thereof, including an AprL-clade variant subtilisin enzyme that has improved stability and/or soil removal compared to a parent AprL-clade subtilisin enzyme.

VARIANT ALPHA AMYLASES WITH ENHANCED ACTIVITY ON STARCH POLYMERS

Described are variants of alpha-amylase enzymes for use in industrial processes, such as liquefaction of starch. The alpha-amylase variants have increased specific activity allowing the more rapidly reduction of peak viscosity during liquefaction processes. The alpha-amylase is modified by introducing into the amino sequence of a parent Family 13 alpha-amylase polypeptide a mutation at an amino acid residue in the starch-binding groove; wherein the starch-binding groove is formed by amino acid residues in the alpha-helix preceding the first beta-strand in the A domain, the loop between the sixth alpha-helix and the seventh beta-strand in the A domain, the loop between the seventh alpha-helix and the eighth beta-strand in the A domain, and the loop connecting the A domain and the C domain; and wherein the mutation alters the binding of starch to the variant alpha amylase polypeptide compared to the parental alpha amylase polypeptide. 1. A method for producing a variant α-amylase polypeptide , comprising:introducing into the amino sequence of a parent Family 13 α-amylase polypeptide a mutation at an amino acid residue in the starch-binding groove;wherein the starch-binding groove is formed by amino acid residues in the α-helix preceding the first β-stand in the A domain, the loop between the sixth α-helix and the seventh β-strand in the A domain, the loop between the seventh α-helix and the eighth β-strand in the A domain, and the loop connecting the A domain and the C domain; andwherein the mutation alters the binding of starch to the variant α-amylase polypeptide compared to the parental α-amylase polypeptide.2. The method of claim 1 , wherein the starch-binding groove corresponds to amino acid residues 1-6 claim 1 , 36 claim 1 , 38 claim 1 , 91-97 claim 1 , 224-226 claim 1 , 249-257 claim 1 , 278-282 claim 1 , 309-320 claim 1 , 354-359 claim 1 , 391 claim 1 , and 395-402 claim 1 , referring to SEQ ID NO: 2 for numbering claim 1 , amino acid residues 1-6 claim 1 , ...

GLUCOAMYLASE VARIANTS WITH ALTERED PROPERTIES

The present disclosure relates to variants of a parent glucoamylase having altered properties (e.g., improved thermostability and/or specific activity). In particular, the present disclosure provides compositions comprising the variant glucoamylases, including starch hydrolyzing compositions and cleaning compositions. The disclosure also relates to DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells. 1. A glucoamylase variant comprising two or more amino acid substitutions corresponding to position 61 , 73 , 417 , 430 , 431 , 503 , 511 , 535 , 539 , or 563 of SEQ ID NO: 2 , or an equivalent position in a parent glucoamylase , wherein the glucoamylase variant has at least 80% sequence identity with SEQ ID NO: 1 , 2 , 3 , 5 , 6 , 7 , 8 , or 9.2. The glucoamylase variant of claim 1 , wherein the parent glucoamylase has a catalytic domain that has at least 80% sequence identity with SEQ ID NO: 1 claim 1 , 2 claim 1 , 3 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , or 9 claim 1 , or a starch binding domain that has at least 80% sequence identity with SEQ ID NO: 1 or 2.3. The glucoamylase variant of claim 1 , wherein the glucoamylase variant has at least 85% sequence identity with SEQ ID NO: 1 claim 1 , 2 claim 1 , 3 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , or 9.4. The glucoamylase variant of claim 1 , wherein the glucoamylase variant has at least 90% sequence identity with SEQ ID NO: 1 claim 1 , 2 claim 1 , 3 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , or 9.5. The glucoamylase variant of claim 1 , wherein the glucoamylase variant has at least 95% sequence identity with SEQ ID NO: 1 claim 1 , 2 claim 1 , 3 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , or 9.6. The glucoamylase variant of claim 1 , wherein the glucoamylase variant has at least 99.5% sequence identity with SEQ ID NO: 1 claim 1 , 2 claim 1 , 3 claim 1 , 5 claim 1 , 6 claim 1 , 7 claim 1 , 8 claim 1 , or 9. ...

BETA-GLUCOSIDASE I VARIANTS WITH IMPROVED PROPERTIES

The present disclosure is generally directed to enzymes and in particular beta-glucosidase variants. Also described are nucleic acids encoding beta-glucosidase variants, compositions comprising beta-glucosidase variants, methods of using beta-glucosidase variants, and methods of identifying additional useful beta-glucosidase variants. 1. A beta-glucosidase 1 (BGL1) variant having at least two improved activities over wild type BGL1 selected from the group consisting of:(a) pre-treated corn stover (PCS) hydrolysis activity,(b) cellobiase activity,(c) protein expression,(d) beta-glucosidase activity measured by a cellobiase activity in the presence of ammonia pretreated corncob (CC) or by a CC hydrolysis activity,(e) thermostability,(f) phosphoric acid swollen cellulose (PASO) hydrolysis activity, and(g) hydrolytic activity in the presence of glucose,wherein the BGL1 variant is any variant as shown in Tables 4-8, 3-2, 4-2 and 4-3.2. A BGL1 variant according to having improved (b) and (d) activities over wild type BGL1 claim 1 , wherein the BGL1 variant is L266A claim 1 , I567E claim 1 , S283F claim 1 , S283P claim 1 , T258E claim 1 , T258I claim 1 , T258K claim 1 , T258Q claim 1 , P536T claim 1 , P536W claim 1 , I532Y claim 1 , Y530T claim 1 , P607D claim 1 , Q406M claim 1 , Q406S claim 1 , V602T claim 1 , G300M claim 1 , A630S claim 1 , A630T claim 1 , T180H claim 1 , T180M claim 1 , A450M claim 1 , I444E claim 1 , I444F claim 1 , I444N claim 1 , I444W claim 1 , I444Y claim 1 , V500Q claim 1 , A633I claim 1 , S482P claim 1 , A667V claim 1 , A485L claim 1 , A485W claim 1 , Y678R claim 1 , V603G claim 1 , L266C claim 1 , I567F claim 1 , S624P claim 1 , P607L claim 1 , G606I claim 1 , G606K claim 1 , G606L claim 1 , G606M claim 1 , G606Q claim 1 , G606V claim 1 , G605E claim 1 , I444V claim 1 , A633V claim 1 , A655W claim 1 , Y678H claim 1 , V522Y claim 1 , G554F claim 1 , L266N claim 1 , F556L claim 1 , S550I claim 1 , S550T claim 1 , S550V claim 1 , T258L claim 1 , ...

ALPHA-AMYLASES FROM EXIGUOBACTERIUM, AND METHODS OF USE, THEREOF

Disclosed are compositions and methods relating to alpha-amylase from a subset of . The compositions and methods are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing. 1Exiguobacterium. A recombinant Group II-like α-amylase having α-amylase activity and comprising at least two of the following structural features:{'sub': 1', '1, '(i) the amino acid sequence XNLRGKGIG at residues corresponding to positions 89-97, where Xis S or T;'}(ii) the amino acid sequence ADSLGL at residues corresponding to positions 223-228;{'sub': 2', '2, '(iii) the amino acid sequence QXTGK at residues corresponding to positions 253-257, where Xis A or T;'}(iv) the amino acid sequence GYTH at residues corresponding to positions 281-284; and/or;{'sub': 3', '4', '3', '4, '(v) the amino acid sequence VXDRXK at residues corresponding to positions 419-224, where Xis T, S, or A and Xis A or T;'}wherein any one of SEQ ID NOs: 1-4, 9-11, and 15-17 are used for numbering;wherein the recombinant α-amylase does not have an amino acid sequence identical to any of SEQ ID NOs: 1, 3, 11 or, 15; andwherein optionally the recombinant α-amylase has at least 95% amino acid sequence identity to SEQ ID NO: 4 or at least 96% amino acid sequence identity to SEQ ID NO: 11.2. The α-amylase of claim 1 , comprising:(i) an amino acid sequence having at least 80% amino acid sequence identity to the amino acid sequence of any one of SEQ ID NOs: 1-4, 9-11, and 15-17;(ii) an amino acid sequence derived from a parental α-amylase having at least 80% amino acid sequence identity to the amino acid sequence of any one of SEQ ID NOs: 1-4, 9-11, and 15-17 by amino acid substitution, deletion or insertion;(iii) an amino acid sequence that differs from the amino acid sequence of any one of SEQ ID NOs: 1-4, 9-11, and 15-17 by one ...

ISOPRENE SYNTHASE VARIANTS FOR IMPROVED MICROBIAL PRODUCTION OF ISOPRENE

The present invention provides methods and compositions comprising at least one isoprene synthase enzyme with improved catalytic activity and/or solubility. In particular, the present invention provides variant plant isoprene synthases for increased isoprene production in microbial host cells. Biosynthetically produced isoprene of the present invention finds use in the manufacture of rubber and elastomers. 18-. (canceled)9P. alba. An isolated isoprene synthase variant , wherein the variant comprises one or more amino acid substitution(s) at one or more amino acid residue(s) of a wild type isoprene synthase , wherein said one or more amino acid residue(s) correspond to amino acid residues of isoprene synthase having the sequence of SEQ ID NO:120 , wherein said amino acid substitution(s) are selected from the group consisting of V10M , F12S , T15A , E18G , V58I , V58F , L70Q , L70R , L70V , L70T , T71P , V79L , E89D , G94A , S119F , F120L , G127R , E175V , T212I , S257A , R262G , A266G , F280L , N297K , F305L , L319M , E323K , A328T , D342E , A359T , K366N , E368D , L374M , S396T , V418S , K438N , H440R , T442A , I449V , A469S , K500R , K505Q , G507S , S509N , F511Y , and N532K; and wherein the isoprene synthase variant has increased isoprene synthase activity compared to the wild type isoprene synthase.10. The isolated isoprene synthase variant of claim 9 , wherein increased isoprene synthase activity is indicated by a host cell comprising the isoprene variant growing at a faster rate in the presence of dimethylallyl pyrophosphate (DMAPP) compared to a host cell comprising the wild type isoprene synthase.11. The isolated isoprene synthase variant of claim 9 , wherein the isoprene synthase is a poplar isoprene synthase variant.12P. alba. The isolated poplar isoprene synthase variant of claim 11 , wherein the wild type isoprene synthase is isoprene synthase of SEQ ID NO:120.13. The isolated poplar isoprene synthase variant of claim 11 , comprising the L70R substitution ...

SERINE PROTEASES OF BACILLUS SPECIES

The present disclosure relates to serine proteases cloned from spp., and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1. A recombinant polypeptide or an active fragment thereof in the WHY-clade.2. A recombinant polypeptide or an active fragment thereof , comprising an amino acid sequence having at least 70% identity to the amino acid sequence of SEQ ID NO:3 , SEQ ID NO:4 , SEQ ID NO:7 , SEQ ID NO:10 , SEQ ID NO:11 , SEQ ID NO:14 , SEQ ID NO:15 , SEQ ID NO:22 , SEQ ID NO:25 , SEQ ID NO:28 , SEQ ID NO:31 , SEQ ID NO:34 , SEQ ID NO:37 , SEQ ID NO:40 , SEQ ID NO:43 , or SEQ ID NO:44.3. The recombinant polypeptide or active fragment thereof of or , wherein the recombinant polypeptide or active fragment thereof has proteolytic activity.4. The recombinant polypeptide or active fragment thereof of any of the above claims , wherein the polypeptide or active fragment thereof comprises a DTGIDXXHXXLXNLVXTSLGXS XVGGXXXDVXGH motif , wherein the initial D is the active site Aspartic acid , the terminal H is the active site Histidine , and X is any amino acid.5. The recombinant polypeptide or active fragment thereof of any of the above claims , with the proviso that the polypeptide does not comprise the amino acid sequence of WO2012175708-0002 , WO2012175708-0004 , WO2012175708-0006 , WP010283106 , or WP006679321.6. The recombinant polypeptide or active fragment thereof of any one of or , wherein the polypeptide or active fragment thereof comprises a DTGIDXXHXXLXNLVXTSLGXS XVGGXXXDVXGH motif , wherein the initial D is the active site Aspartic acid , the terminal H is the active site Histidine , and X , Xa , Xb , and Xc are any amino acid , provided that when Xa is arginine , Xb and Xc are not glycine.7. The recombinant polypeptide or active fragment thereof of any one of - , wherein the VXG sequence of the motif is a VQG.8. The recombinant polypeptide ...

VARIANTS OF CELLOBIOHYDROLASES

Disclosed are a number of homologs and variants of Ce17A (formerly cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted. 1. An isolated variant of a parent cellobiohydrolase (CBH) enzyme , wherein said variant has cellulase activity , comprises at least one amino acid substitution , has at least 80% sequence identity to SEQ ID NO:3 , and has at least one improved property over said parent CBH enzyme selected from: (a) expression (Protein Content Determination) , (b) PASC Hydrolysis Assay , (c) PASC Hydrolysis Assay in the Presence of EG2 , (d) PASC Hydrolysis Assay After Heat Incubation , (e) Whole Hydrolysate PCS (whPCS) Assay , (f) Dilute Ammonia Corn Cob (daCC) Assay , and (g) dilute ammonia corn stover (daCS) assay; and wherein the at least one amino acid substitution is at a position selected from the group consisting of: A414 , G22 , R394 , T417 , P227 , T255 , V403 , F280 , E337 , P258 , T332 , T296 , N49 , Y493 , S196 , G430 , T246 , Y247 , N307 , T356 , Y466 , S357 , Q27 , S387 , L318 , T389 , Y303 , Y370 , K287 , T285 , N350 , D249 , F338 , S113 , Y492 , S398 , T226 , Y371 , A316 , K346 , G340 , S342 , D368 , M374 , D179 , E236 , Y474 , G391 , F418 , F311 , R251 , T281 , V104 , L326 , A224 , and E385 , wherein the position of each amino acid substitution corresponds to SEQ ID NO:3.23-. (canceled)4. The isolated variant of claim 1 , wherein said at least one amino acid substitution is selected from the group consisting of:an amino acid substitution at position A414 selected from the group consisting of: F, N, L, M, W, R, G, K, I, H, Q, D, C, and T;an amino acid substitution at position G22 selected from the group consisting of: D, E, H, P, T, F, C, A, W, L, Y, I, Q, M, K, and S; an amino acid substitution at position R394 selected from the ...

Perhydrolase

The present invention provides methods and compositions comprising at least one perhydrolase enzyme for cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions for generation of peracids. The present invention finds particular use in applications involving cleaning, bleaching and disinfecting. 1166-. (canceled)168. The composition of claim 167 , wherein said perhydrolase has at least 90% amino acid sequence identity to the amino acid sequence set forth in SEQ ID NO: 97.169Mesorhizobium loti. The composition of claim 168 , wherein said perhydrolase is Mlo I (Q98MY5) and comprises the amino acid sequence as set out in SEQ ID NO: 97.170. A cleaning composition according to any one of claims 167 , comprising:a) at least 0.0001 weight percent of said perhydrolase;b) a molecule comprising an ester moiety; andc) optionally, an adjunct ingredient.171. The cleaning composition of claim 170 , wherein said composition comprises:a) at least 0.0001 weight percent of said perhydrolase; i) a per-salt;', 'ii) an organic peroxyacid;', 'iii) urea hydrogen peroxide;', 'iv) a carbohydrate and carbohydrate oxidase mixture, and', 'v) mixtures thereof;, 'b) a material selected from the group consisting of: a peroxygen source, hydrogen peroxide and mixtures thereof, said peroxygen source being selected from the group consisting ofc) from about 0.01 to about 50 weight percent of a molecule comprising an ester moiety; andd) optionally, an adjunct ingredient.172. The cleaning composition of claim 170 , wherein said adjunct ingredient is selected from the group consisting of: surfactants claim 170 , builders claim 170 , chelating agents claim 170 , dye transfer inhibiting agents claim 170 , deposition aids claim 170 , dispersants claim 170 , enzymes claim 170 , and enzyme stabilizers claim 170 , catalytic materials claim 170 , bleach activators claim 170 , bleach boosters claim 170 , preformed peracids claim 170 , ...

CELLULASE VARIANTS WITH IMPROVED EXPRESSION, ACTIVITY AND STABILITY, AND USE THEREOF

The present disclosure relates to cellulase variants. In particular the present disclosure relates to cellulase variants having improved expression, activity and/or stability. Also described are nucleic acids encoding the cellulase variants, compositions comprising the cellulase variants, and methods of use thereof. 1. A cellulase variant , wherein the variant is a mature form having cellulase activity and comprising a substitution at one or more positions selected from the group consisting of: 5 , 18 , 19 , 28 , 30 , 32 , 35 , 38 , 79 , 80 , 89 , 100 , 102 , 103 , 104 , 105 , 111 , 117 , 119 , 121 , 125 , 126 , 133 , 137 , 138 , 139 , 140 , 141 , 143 , 150 , 158 , 162 , 177 , 180 , 181 , 182 , 185 , 186 , 188 , 190 , 191 , 192 , 193 , 196 , 201 , 207 , 225 , 226 , 228 , 229 , 230 , 233 , 234 , 236 , 240 , 243 , 245 , 251 , 252 , 258 , 267 , 268 , 274 , 292 , 293 , 303 , 304 , 306 , 307 , 313 , 319 , 322 , 328 , 331 , 338 , 340 , 346 , 361 , 362 , 363 , 364 , 365 , 371 , 384 , 394 , 396 , 400 , 406 , 407 , 414 , 417 , 422 , 427 , 431 , 433 , 436 , 440 , 441 , 443 , 444 , 445 and 447 , wherein the positions are numbered by correspondence with the amino acid sequence of a reference cellobiohydrolase II (CBH2) set forth as SEQ ID NO:3.2. The cellulase variant of claim 1 , wherein the variant comprises a further substitution at one or more further positions selected from:(i) a first group consisting of 63, 77, 129, 146, 147, 151, 153, 157, 161, 189, 194, 197, 203, 204, 208, 211, 237, 239, 244, 247, 254, 277, 281, 285, 288, 289, 294, 327, 339, 344, 356, 378, 382 and 405; or(ii) a second group consisting of 94, 98, 107, 120, 134, 144, 154, 178, 179, 206, 210, 214, 231, 232, 266, 272, 275, 291, 312, 316, 323, 343, 360, 380, 381, 386, 399, 410, 413, 416, 426, and 429,wherein the further positions are numbered by correspondence with the amino acid sequence of the reference cellobiohydrolase II (CBH2) set forth as SEQ ID NO:3.36-. (canceled)7. The cellulase variant of claim 1 ...

COMPOSITIONS AND METHODS COMPRISING LG12-CLADE PROTEASE VARIANTS

The present disclosure provides LG12-clade enzyme variants, compositions comprising these enzyme variants, and method of using these enzymes and compositions, as well as the polynucleotides encoding these enzymes, the vectors comprising these polynucleotides, and the host cells transformed with such vectors. 1. A protease variant , or a recombinant polypeptide or an active fragment thereof comprising an amino acid sequence comprising two or more substitutions at one or more positions selected from:(i) 1, 3, 7, 9, 19, 24, 27, 30, 38, 40, 43, 45, 48, 52, 53, 57, 72, 76, 78, 79, 86, 87, 88, 89, 90, 91, 93, 97, 99, 100, 101, 103, 104, 106, 107, 111, 114, 115, 116, 117, 118, 120, 122, 123, 124, 128, 129, 130, 131, 133, 134, 136, 139, 140, 141, 143, 144, 145, 147, 148, 149, 150, 153, 156, 158, 159, 160, 166, 181, 182, 185, 188, 194, 209, 212, 213, 215, 216, 217, 222, 224, 228, 234, 236, 238, 240, 242, 245, 246, 248, 251, 252, 256, 265, 267, 269, 270, 271, 272, 273, and 275;(ii) 1, 3, 9, 19, 24, 27, 30, 38, 40, 43, 45, 48, 52, 53, 57, 72, 76, 78, 79, 86, 87, 88, 89, 90, 91, 93, 97, 99, 100, 101, 103, 104, 106, 107, 111, 114, 115, 116, 117, 118, 120, 122, 123, 124, 128, 129, 130, 131, 133, 134, 136, 139, 140, 141, 143, 144, 145, 147, 148, 149, 150, 153, 156, 158, 159, 160, 166, 181, 182, 185, 188, 194, 209, 212, 213, 215, 216, 217, 222, 224, 228, 234, 236, 238, 240, 242, 245, 246, 248, 251, 252, 256, 265, 267, 271, 272, and 275;(iii) 1, 7, 9, 27, 38, 40, 45, 48, 52, 53.76, 78, 91, 100, 114, 117, 118, 122, 128, 129, 130, 140, 147, 149, 156, 158, 159, 160, 166, 181, 182, 194, 209, 217, 222, 228, 234, 236, 238, 245, 248, 256, 269, 270, 271, 272, 273, and 275;(iv) 1, 24, 30, 38, 40, 48, 52, 53, 76, 78, 79, 86, 87, 88, 89, 91, 93, 97, 100, 103, 104, 106, 111, 114, 115, 116, 117, 118, 120, 122, 124, 128, 129, 130, 131, 133, 134, 136, 139, 141, 143, 144, 147, 148, 149, 150, 153, 156, 158, 159, 166, 182, 185, 194, 209, 212, 213, 216, 217, 222, 224, 236, 238, 248, 251, 252, 256, 272 ...

BACILLUS GIBSONII-CLADE SERINE PROTEASES

Disclosed herein is one or more subtilisin variant, nucleic acid encoding same, and compositions and methods related to the production and use thereof, including one or more -clade subtilisin variant that has improved stability and/or soil removal compared to one or more reference subtilisin. 1. An isolated subtilisin variant comprising an amino acid sequence comprising two , three , or four or more variations versus SEQ ID NO:85 at positions selected from:(i) 1, 4, 9, 21, 24, 27, 36, 37, 39, 42, 43, 44, 47, 54, 55, 56, 74, 80, 85, 87, 99, 102, 114, 117, 119, 121, 126, 128, 131, 143, 144, 158, 159, 160, 169, 182, 188, 190, 197, 198, 212, 224, 231, 232, 237, 242, 245, 246, 254, 255, 256, and 257;(ii) 37, 39, 47, 56, 80, 85, 87, 99, 114, 126, 128, and 242;(iii) 39, 99, 126, and 128;(iv) 39 in combination with one or more variation at a position selected from 37, 47, 56, 80, 85, 87, 99, 114, 126, 128, and 242;(v) 56 in combination with one or more variation at a position selected from 37, 39, 47, 80, 85, 87, 99, 114, 126, 128, and 242;(vi) 114 in combination with one or more variation at a position selected from 37, 39, 47, 56, 80, 85, 87, 99, 126, 128, and 242;(vii) 126 in combination with one or more variation at a position selected from 37, 39, 47, 56, 80, 85, 87, 99, 114, 128, and 242;(viii) 242 in combination with one or more variation at a position selected from 37, 39, 47, 56, 80, 85, 87, 99, 114, 126, and 128;(ix) 99+128 in combination with one or more variation at a position selected from 39, 56, 114, 126 and 242;(x) 39+242 in combination with one or more variation at a position selected from 37, 47, 56, 80, 85, 87, 99, 114, 126, and 128; or(xi) 39+99+128 in combination with one or more variation at a position selected from 37, 47, 56, 80, 85, 87, 114, 126, and 242;with the proviso that one or more of said two, three, or four or more variations is non-naturally occurring;wherein the amino acid positions of the variant are numbered by correspondence with the ...

Serine proteases of bacillus species

The present disclosure relates to serine proteases cloned from Bacillus Akibai and Bacillus Clarkii , and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications.

SERINE PROTEASES OF THE BACILLUS GIBSONII-CLADE

The present disclosure relates to serine proteases cloned from , and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1Bacillus GibsoniiBacillus Gibsonii. A recombinant polypeptide or an active fragment thereof of the -clade , wherein the recombinant polypeptide or active fragment thereof has proteolytic activity and comprises an amino acid sequence having at least 70% identity to the amino acid sequence of SEQ ID NO:4 , 7 , 11 , 15 , 19 , 23 , 49 , 50 , 51 , 52 , 57 , 59 , 61 , 63 , 65 , 67 , 69 , 71 , 73 , 75 , 77 , 79 , 81 , or 83 , wherein said -clade comprises a DXGIXXHSDLXXXGGASXXXXXPTTADLNXHGTH (SEQ ID NO:47) or DXGIXXHSDLXXXGGASXXXXXXTTADLXXHGTH (SEQ ID NO:90) motif , wherein the initial D is the active site Aspartic acid residue and the penultimate H is the active site Histidine , and X is any amino acid , with the proviso that the amino acid sequence does not comprise NCBI Accession Nos. CAE48421 or CAS91385.2. (canceled)3Bacillus Gibsonii. The recombinant polypeptide or active fragment thereof of any claim 1 , wherein the -clade comprises SEQ ID NO:47.4Bacillus Gibsonii. The recombinant polypeptide or active fragment thereof of claim 1 , wherein the -clade comprises SEQ ID NO:90.58-. (canceled)9. The recombinant polypeptide or active fragment thereof of claim 1 , with the proviso that the amino acid sequence does not comprise NCBI accession Nos. CAE48421 claim 1 , CAS91385 claim 1 , or AGS78407.10B. gibsonii. The recombinant polypeptide or active fragment thereof of claim 1 , with the proviso that the -clade does not comprise NCBI accession Nos. CAE48421 claim 1 , CAS91385 claim 1 , CAV33594 claim 1 , or AGS78407.11. The recombinant polypeptide or active fragment thereof of claim 1 , wherein the polypeptide has protease activity in the presence of a surfactant.12. (canceled)13. The recombinant polypeptide or active fragment thereof ...

VARIANTS OF CELLOBIOHYDROLASES

Disclosed are a number of homologs and variants of Cel7A (formerly cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted. 1. (canceled)2. An isolated variant of a parent cellobiohydrolase (CBH) enzyme , wherein said variant has cellulase activity , has at least 80% sequence identity to SEQ ID NO:3 , and wherein said variant comprises an amino acid substitution selected from the group consisting of: Y247D , N49P , T246V , N200G , and combinations thereof , wherein the position of each amino acid substitution corresponds to SEQ ID NO:3.3. The isolated variant of claim 2 , wherein said variant comprises a Y247D substitution.4. The isolated variant of claim 2 , wherein said variant comprises a N49P substitution.5. The isolated variant of claim 2 , wherein said variant comprises a T246V substitution.6. The isolated variant of claim 2 , wherein said variant comprises a N200G substitution.7. The isolated variant of claim 2 , wherein said variant further comprises an amino acid substitution selected from the group consisting of: T246S and T246P.8. The isolated variant of claim 2 , wherein said variant further comprises an N200R amino acid substitution.9. The isolated variant of claim 2 , wherein said variant further comprises an amino acid substitution selected from the group consisting of: F418M claim 2 , T255D or T255I or T255K or T255P or T255R or T255V claim 2 , D241N claim 2 , G234D claim 2 , P194V claim 2 , T356L claim 2 , S92T claim 2 , T41I claim 2 , and combinations thereof.10. The isolated variant of claim 2 , wherein said parent CBH polypeptide is a fungal cellobiohydrolase 1 (CBH1).11Hypocrea jecorina, Hypocrea schweinitzii, Hypocrea orientalis, Trichoderma pseudokoningii, Trichoderma konilangbra, Trichoderma citrinoviride, Trichoderma harzanium, ...

GLUCOAMYLASE VARIANTS WITH ALTERED PROPERTIES

The present invention relates to variants of a parent glucoamylase having altered properties (e.g., improved thermostability and/or specific activity). In particular, the present invention provides compositions comprising the variant glucoamylases, including starch hydrolyzing compositions, animal feed compositions and cleaning compositions. The invention also relates to DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells. 126-. (canceled)27. A glucoamylase variant comprising a substitution at a residue position corresponding to position 208 of SEQ ID NO: 2 or 3 and/or an equivalent position in a parent glucoamylase , wherein the equivalent position is determined by sequence identity and said parent glucoamylase has at least 80% sequence identity and less than 100% sequence identity with SEQ ID NOs: 1 , 2 , 3 , 5 , 6 , 7 , 8 , or 9.28. The glucoamylase variant of claim 27 , wherein the parent glucoamylase is SEQ ID NO: 1 claim 27 , 2 or 3.29. The glucoamylase variant of claim 27 , wherein the equivalent position is determined by structural identity to SEQ ID NO: 3.30TrichodermaAspergillus. The glucoamylase variant of claim 27 , wherein the parent glucoamylase is obtained from a spp. or an spp.31. The glucoamylase variant of claim 27 , wherein the variant comprises a substitution corresponding to Q208N.32. The glucoamylase variant of claim 31 , further comprising a substitution at the position corresponding to position 12 and/or position 315.33. The glucoamylase variant of claim 32 , wherein the substitution is I12L/R and/or Y315W.34. The glucoamylase variant of claim 32 , further comprising a substitution at a position corresponding to position 314.35. The glucoamylase variant of claim 27 , wherein said variant exhibits increased thermostability as compared to the parent glucoamylase.36. The glucoamylase variant of claim 27 , wherein said variant exhibits increased specific activity compared to the parent ...

ENGINEERED GLUCOSYLTRANSFERASES

Disclosed herein are glucosyltransferases with modified amino acid sequences. Such engineered enzymes exhibit improved alpha-glucan product yields and/or lower leucrose yields, for example. Further disclosed are reactions and methods in which engineered glucosyltransferases are used to produce alpha-glucan. 1. A non-native glucosyltransferase comprising at least one amino acid substitution at a position corresponding with amino acid residue Leu-428 , Ala-472 , Leu-513 , Met-529 , Phe-607 , Asn-613 , Gln-616 , Ser-631 , Gly-633 , Phe-634 , Thr-635 , or Phe-951 of SEQ ID NO:62 ,wherein the non-native glucosyltransferase synthesizes alpha-glucan comprising 1,3-linkages, and (i) an alpha-glucan yield that is higher than the alpha-glucan yield of a second glucosyltransferase that only differs from the non-native glucosyltransferase at the substitution position(s), and/or', '(ii) a leucrose yield that is lower than the leucrose yield of the second glucosyltransferase;, 'wherein the non-native glucosyltransferase haswherein the non-native glucosyltransferase comprises a catalytic domain that is at least about 90% identical to residues 55-960 of SEQ ID NO:4, residues 54-957 of SEQ ID NO:65, residues 55-960 of SEQ ID NO:30, residues 55-960 of SEQ ID NO:28, or residues 55-960 of SEQ ID NO:20.2. The non-native glucosyltransferase of claim 1 , wherein:(i) the amino acid substitution at the position corresponding with amino acid residue Leu-428 is with a Val residue;(ii) the amino acid substitution at the position corresponding with amino acid residue Ala-472 is with a Ser or Cys residue;(iii) the amino acid substitution at the position corresponding with amino acid residue Leu-513 is with a Tyr, Phe, or Trp residue;(iv) the amino acid substitution at the position corresponding with amino acid residue Met-529 is with a Leu or Asn residue;(v) the amino acid substitution at the position corresponding with amino acid residue Phe-607 is with a Trp, Tyr, or Asn residue;(vi) the amino ...

VARIANTS OF CELLOBIOHYDROLASES

Disclosed are a number of homologs and variants of Cel7A (formerly cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted. 1. An isolated variant of a parent cellobiohydrolase (CBH) enzyme , wherein said variant has cellulase activity , has at least 80% sequence identity to SEQ ID NO:3 , and has significantly increased melting temperature (Tm) as compared to said parent CBH enzyme.2. The isolated variant of claim 1 , wherein said variant comprises an amino acid substitution selected from the group consisting of: T356L claim 1 , T246P claim 1 , T255D claim 1 , N200R claim 1 , and combinations thereof claim 1 , wherein the position of each amino acid substitution corresponds to SEQ ID NO:3.3. The isolated variant of claim 2 , wherein said variant comprises a T356L substitution.4. The isolated variant of or claim 2 , wherein said variant comprises a T246P substitution.5. The isolated variant of claim 2 , or claim 2 , wherein said variant comprises a T255D substitution.6. The isolated variant of claim 2 , claim 2 , or claim 2 , wherein said variant comprises a N200R substitution.76. The isolated variant of claim 2 , claim 2 , claim 2 , or claim 2 , wherein said variant further comprises an amino acid substitution selected from the group consisting of: T246S and T246V.86. The isolated variant of claim 2 , claim 2 , claim 2 , or wherein said variant further comprises an amino acid substitution selected from the group consisting of: T255I claim 2 , T255K claim 2 , T255P claim 2 , T255R and T255V.95. The isolated variant of claim 2 , claim 2 , claim 2 , or wherein said variant further comprises an N200G amino acid substitution.10. The isolated variant of any one of to claim 2 , wherein said variant further comprises an amino acid substitution selected from the ...

MODIFIED GLUCOSYLTRANSFERASES FOR PRODUCING BRANCHED ALPHA-GLUCAN POLYMERS

Glucosyltransferase enzymes are disclosed herein that produce branched alpha-glucan polymer. Also disclosed, for example, are polynucleotides encoding these enzymes, as well as methods of producing branched alpha-glucan polymer. 2. The glucosyltransferase of claim 1 , wherein the glucosyltransferase comprises an amino acid sequence that is at least 90% identical to SEQ ID NO:85 claim 1 , SEQ ID NO:87 claim 1 , SEQ ID NO:89 claim 1 , SEQ ID NO:91 claim 1 , SEQ ID NO:93 claim 1 , SEQ ID NO:95 claim 1 , or SEQ ID NO:97 claim 1 , and wherein the glucosyltransferase lacks at least one of motifs (i) claim 1 , (ii) claim 1 , or (iii).3. A polynucleotide comprising a nucleotide sequence encoding a glucosyltransferase enzyme according to claim 1 , optionally wherein one or more regulatory sequences are operably linked to the nucleotide sequence claim 1 , and preferably wherein said one or more regulatory sequences include a promoter sequence.4. A method of preparing a polynucleotide sequence encoding a glucosyltransferase enzyme that produces a branched alpha-glucan polymer claim 1 , said method comprising: (1) an amino acid sequence that is at least 90% identical to amino acid positions 54-957 of SEQ ID NO:65, and', (i) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:78,', '(ii) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:79, and', '(iii) a motif comprising an amino acid sequence that is at least 90% identical to SEQ ID NO:80;, '(2) the following three motifs, 'and, '(a) identifying a polynucleotide sequence encoding a parent glucosyltransferase enzyme that comprises a catalytic domain comprising(b) modifying the polynucleotide sequence identified in step (a) to delete and/or mutate at least one of motifs (i), (ii), or (iii) encoded by the polynucleotide sequence, thereby providing a polynucleotide sequence encoding a glucosyltransferase enzyme that produces a branched alpha-glucan polymer.5. ...

PROTEASE VARIANTS AND USES THEREOF

Disclosed herein is one or more subtilisin variants, nucleic acids encoding same, and compositions and methods related to the production and uses thereof, including one or more subtilisin variants that has improved stability and/or soil removal compared to one or more reference subtilisin. 1. A subtilisin variant comprising an amino acid sequence comprising two , three , or four or more amino acid substitutions at positions selected from:(i) 22, 40, 44, 48, 58, 89, 101, 103, 104, 116, 128, 130, 232, 245, and 248;(ii) 40, 101, 128, and 130;(iii) 22 in combination with one or more amino acid substitution at a position selected from 40, 44, 48, 58, 89, 101, 103, 104, 116, 128, 130, 232, 245, and 248;(iv) 40 in combination with one or more amino acid substitution at a position selected from 22, 44, 48, 58, 89, 101, 103, 104, 116, 128, 130, 232, 245 and 248;(v) 44 in combination with one or more amino acid substitution at a position selected from 22, 40, 48, 58, 89, 101, 103, 104, 116, 128, 130, 232, 245 and 248;(vi) 48 in combination with one or more amino acid substitution at a position selected from 22, 40, 44, 58, 89, 101, 103, 104, 116, 128, 130, 232, 245 and 248;(vii) 58 in combination with one or more amino acid substitution at a position selected from 22, 40, 44, 48, 89, 101, 103, 104, 116, 128, 130, 232, 245 and 248;(viii) 89 in combination with one or more amino acid substitution at a position selected from 22, 40, 44, 48, 58, 101, 103, 104, 116, 128, 130, 232, 245 and 248;(ix) 101 in combination with one or more amino acid substitution at a position selected from 22, 40, 44, 48, 58, 89, 103, 104, 116, 128, 130, 232, 245 and 248;(x) 103 in combination with one or more amino acid substitution at a position selected from 22, 40, 44, 48, 58, 89, 101, 104, 116, 128, 130, 232, 245, and 248;(xi) 104 in combination with one or more amino acid substitution at a position selected from 22, 40, 44, 48, 58, 89, 101, 103, 116, 128, 130, 232, 245, and 248;(xii) 116 in ...

PAENIBACILLUS AND BACILLUS SPP. MANNANASES

Disclosed herein are mannanases from or spp, polynucleotides encoding the mannanases, compositions containing the mannanases, and methods of use thereof. Compositions containing mannanases are suitable for use as detergents and for cleaning fabrics and hard surfaces, as well as in a variety of other industrial applications. 1. A mannanase variant , or a recombinant polypeptide or an active fragment thereof comprising an amino acid sequence comprising one or more variation versus SEQ ID NO:2 at one or more position selected from:(i) 10, 19, 38, 59, 60, 62, 63, 66, 67, 68, 70, 71, 74, 75, 78, 79, 80, 97, 129, 131, 135, 136, 143, 167, 168, 184, 213, 214, 225, 228, 235, 242, 244, 258, 259, 261, and 283;(ii) 19, 38, 63, 67, 71, 97, 129, 143, 168, 184, 225, 228, 235, 244, 258, and 261;(iii) 19, 38, 67, 97, 129, 143, 168, 184, 225, 228, 235, 244, 258, and 261;(iv) 19, 38, 67, 129, 168, 184, 225, 244, 258, and 261;(v) 19, 38, 67, 97, 129, 168, 184, 244, 258, and 261;(vi) 85, 19-85, 38-85, 67-85, 85-129, 85-168, 85-184, 85-225, 85-244, 85-258, and 85-261; or(vii) 19-85, 38-85, 67-85, 85-129, 85-168, 85-184, 85-225, 85-244, 85-258, and 85-261;with the proviso that one or more of said variations is non-naturally occurring; andwherein the amino acid positions of said variant or recombinant polypeptide or active fragment thereof are numbered by correspondence with the amino acid sequence of SEQ ID NO:2.2. The mannanase variant claim 1 , or a recombinant polypeptide or an active fragment thereof of claim 1 , wherein said variant or recombinant polypeptide or active fragment thereof comprises one or more variation versus SEQ ID NO:2 selected from:(i) X10Q/T, X19E/V, X38E/I/L/M/Q/R/V, X59D/G/K/N/Q/T, X60F/M/V, X62E/I/Q/V, X63L, X66C/T/V, X67A/D/E/G/P/Q/S/V, X68L/M/R/S/W, X70R/V, X71 D/H, X74E/C/Q/V, X75I, X78A/D/L/M, X79E/F/W, X80Q/T, X97E/L/P/Q, X129M, X131P, X135A/C/Q, X136E, X143Q/R, X167L/S/W/Y, X168A/E/G/L/M/S/T, X184D/F/H/L/M/P, X213E, X214C/Q, X225A/C/P/W, X228A/G/H/I/K/S/V/ ...

PROTEASE VARIANTS AND USES THEREOF

Disclosed herein is one or more subtilisin variant, nucleic acid encoding same, and compositions and methods related to the production and use thereof, including one or more subtilisin variant that has improved stability and/or soil removal compared to one or more reference subtilisin. 1. A subtilisin variant comprising an amino acid sequence comprising two , three , or four or more variations at positions corresponding to SEQ ID NO:2 , wherein said positions are selected from:(i) 1, 3, 9, 10, 15, 22, 24, 26, 27, 28, 29, 30, 31, 35, 37, 40, 43, 45, 48, 52, 68, 71, 76, 77, 78, 86, 87, 95, 96, 98, 99, 100, 101, 102, 103, 105, 108, 111, 114, 115, 117, 119, 123, 125, 126, 127, 128, 129, 130, 136, 143, 146, 147, 151, 155, 158, 160, 161, 165, 184, 187, 193, 202, 203, 204, 210, 211, 216, 217, 234, 238, 239, 242, 243, 250, 255, 258, 259, 260, 264, and 274;(ii) 1, 3, 9, 10, 15, 22, 24, 26, 28, 29, 30, 31, 35, 37, 40, 45, 48, 52, 68, 71, 76, 77, 78, 86, 87, 95, 96, 98, 99, 100, 101, 102, 105, 108, 111, 114, 115, 117, 119, 123, 125, 126, 127, 128, 129, 130, 136, 143, 146, 147, 151, 155, 158, 160, 161, 165, 184, 187, 193, 202, 203, 204, 210, 211, 216, 217, 234, 238, 239, 242, 243, 250, 255, 258, 259, 260, 264, and 274;(iii) 1, 3, 9, 10, 24, 26, 29, 30, 31, 35, 37, 40, 45, 48, 52, 68, 71, 77, 78, 86, 87, 95, 96, 98, 99, 100, 101, 102, 105, 108, 111, 115, 117, 119, 123, 127, 128, 129, 130, 136, 143, 146, 147, 151, 155, 158, 160, 161, 165, 184, 187, 193, 202, 203, 204, 210, 211, 216, 217, 234, 238, 239, 242, 243, 250, 258, 259, 260, 264, and 274;(iv) 3, 9, 10, 35, 68, 77, 78, 86, 87, 99, 101, 115, 123, 127, 128, 165, 184, 187, 202, 203, 210, 217, 242, 250, 258, and 264; or(v) 3, 68, 77, 78, 123, 127, 128, 165, 184, 202, 210, 217, and 258;with the proviso that one or more of said two, three, or four or more variations is a man-made mutation or substitution;wherein said variant has at least 85% but less than 100% amino acid sequence identity to an AprL-Clade subtilisin enzyme ...

POLYPEPTIDES WITH ENDOGLUCANASE ACTIVITY AND USES THEREOF

Disclosed herein are cellulase variants, or active fragments thereof, and polynucleotides encoding same, wherein the cellulase variants, or active fragments thereof, hav endoglucanase activity. Also disclosed herein are compositions comprising said cellulase variants, or active fragments thereof; vectors and/or host cells comprising the polynucleotides encoding said cellulase variants, or active fragments thereof; and methods for making and/or using said cellulase variants, or active fragments thereof and/or compositions containing same; wherein said cellulase variants, or active fragments thereof, have endoglucanase activity. 1. A cellulase variant , or an active fragment thereof , comprising an amino acid sequence comprising a substitution at one or more positions selected from:(i) 4, 20, 23, 29, 32, 36, 44, 51, 77, 80, 87, 90, 97, 98, 99, 102, 112, 116, 135, 136, 142, 153, 154, 157, 161, 163, 192, 194, 204, 208, 210, 212, 216, 217, 221, 222, 225, 227, and 232;(ii) K4X, G/K20X, A/S23X, F29X, S32X, N/Q36X, K44X, S51X, S77X, N80X, G87X, E90X, P97X, V98X, A99X, T102X, G112X, T116X, S135X, P/5136X, A142X, G/H/S153X, Q154X, S157X, A161X, K163X, L192X, A194X, G204X, V208X, T210X, P212X, Q216X, S217X, S221X, S222X, S225X, K227X, and 5232X;(iii) X4V, X20N, X23L, X29W, X32D/Y, X36T, X44V, X51T, X77K/M, X80S, X87A, X90A, X97S, X98G, X99E/Y, X102K, X112S/T/V, X116V, X135T, X136E/K/S, X142D/E/P/Q, X153D, X154E, X157D, X161E/P, X163V, X192V, X194S, X204S, X208H/K, X210V, X212S, X216D/E/G/P/S/T/V, X217G/M, X221L/M, X222A, X225K, X227R, and X232T; or(iv) K4V, G/K20L, A/S23L, F29W, S32D/Y, N/Q36T, K44V, S51T, S77K/M, N80S, G87A, E90A, P97S, V98G, A99E/Y, T102K, G112S/Y/V, T116V, S135T, P/S136E/K/S, A142D/E/P/Q, G/H/S153D, Q154E, S157D, A161E/P, K163V, L192V, A194S, G204S, V208H/K, T210V, P212S, Q216D/E/G/P/S/T/V, S217G/M, S221L/M, S222A, S225K, K227R, and S232T, wherein said variant has endoglucanase activity, and wherein the amino acid positions of the variant, or active ...

POLYPEPTIDES WITH ENDOGLUCANASE ACTIVITY AND USES THEREOF

Disclosed herein are cellulase variants, or active fragments thereof, and polynucleotides encoding same, wherein the cellulase variants, or active fragments thereof, have endoglucanase activity. Also disclosed herein are compositions comprising said cellulase variants, or active fragments thereof; vectors and/or host cells comprising the polynucleotides encoding said cellulase variants, or active fragments thereof; and methods for making and/or using said cellulase variants, or active fragments thereof and/or compositions containing same; wherein said cellulase variants, or active fragments thereof, have endoglucanase activity. 1. A cellulase variant , or an active fragment thereof , comprising an amino acid sequence comprising two or more mutations at two or more positions corresponding to SEQ ID NO:1 positions selected from:(i) 4, 23, 29, 32, 34, 36, 44, 51, 65, 77, 80, 87, 90, 97, 98, 99, 102, 112, 116, 119, 135, 136, 142, 153, 154, 156, 157, 161, 163, 178, 192, 194, 202, 204, 205, 206, 208, 210, 212, 217, 221, 222, 225, 227, 232, 233, 236, 237, 238, 241, 247, 249, and 258;(ii) 4, 29, 32, 36, 51, 77, 80, 87, 90, 102, 112, 116, 135, 136, 142, 153, 154, 161, 163, 192, 204, 210, 217, 221, 225, and 227;(iii) 4V, 23L, 29W, 32D/G/Y, 34D, 36T, 44V, 51T, 65G, 77K/M, 80S, 87A, 90A, 97S, 98G/Y, 99E/H/Y, 102K, 112S/T/V, 116V, 119L, 135T, 136E/K/S, 142E/P, 153D, 154E, 156G, 157D, 161E/P, 163V, 178H, 192V, 194S, 202E, 204S, 205D, 206S, 208H/K, 210V, 212S, 217G/M, 221L/M, 222A, 225K, 227R, 232T, 233A/S, 236A, 237D, 238D, 241A/L/R, 247T, 249G/P, and 258K;(iv) 4V, 29W, 32D, 36T, 51T, 77K/M, 80S, 87A, 90A, 102K, 112S/T, 116V, 135T, 136E, 142P, 153D, 154E, 161P, 163V, 192V, 204S, 210V, 217G, 221L, 225K, and 227R;(v) K4, S23, F29, S32, N34, Q36, K44, S51, D65, S77, N80, G87, E90, P97, V98, A99, T102, G112, T116, F119, S135, P136, A142, S153, Q154, D156, S157, A161, K163, N178, L192, A194, D202, G204, N205, F206, V208, T210, P212, S217, S221, S222, S225, K227, S232, T233, T236, S237 ...

SERINE PROTEASES OF BACILLUS SPECIES

The present disclosure relates to serine proteases cloned from spp., and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications. 1. A recombinant polypeptide or an active fragment thereof in the WHY-clade.2. A recombinant polypeptide or an active fragment thereof , comprising an amino acid sequence having at least 70% identity to the amino acid sequence of SEQ ID NO:3 , SEQ ID NO:4 , SEQ ID NO:7 , SEQ ID NO:10 , SEQ ID NO:11 , SEQ ID NO:14 , SEQ ID NO:15 , SEQ ID NO:22 , SEQ ID NO:25 , SEQ ID NO:28 , SEQ ID NO:31 , SEQ ID NO:34 , SEQ ID NO:37 , SEQ ID NO:40 , SEQ ID NO:43 , or SEQ ID NO:44.3. The recombinant polypeptide or active fragment thereof of or , wherein the recombinant polypeptide or active fragment thereof has proteolytic activity.4. The recombinant polypeptide or active fragment thereof of any of the above claims , wherein the polypeptide or active fragment thereof comprises a DTGIDXXHXXLXNLVXTSLGXS XVGGXXXDVXGH motif , wherein the initial D is the active site Aspartic acid , the terminal H is the active site Histidine , and X is any amino acid.5. The recombinant polypeptide or active fragment thereof of any of the above claims , with the proviso that the polypeptide does not comprise the amino acid sequence of WO2012175708-0002 , WO2012175708-0004 , WO2012175708-0006 , WP010283106 , or WP006679321.6. The recombinant polypeptide or active fragment thereof of any one of - or , wherein the polypeptide or active fragment thereof comprises a DTGIDXXHXXLXNLVXTSLGXSXVGGXXXDVXGH motif , wherein the initial D is the active site Aspartic acid , the terminal H is the active site Histidine , and X , Xa , Xb , and Xc are any amino acid , provided that when Xa is arginine , Xb and Xc are not glycine.7. The recombinant polypeptide or active fragment thereof of any one of - , wherein the VXG sequence of the motif is a VQG.8. The recombinant polypeptide ...

Alpha-amylase combinatorial variants

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

Compositions and methods comprising variant proteases

The present invention provides variant proteases, compositions comprising such variant proteases, and methods of cleaning comprising such variant proteases.

Compositions and methods comprising thermolysin protease variants

The present invention provides serine protease - thermoslysine- variants produced there from. Specifically, the present invention provides serine protease variants having one or more substitutions as compared to a reference serine protease. In addition, the present invention provides compositions comprising these serine protease variants. In some embodiments, the present invention provides cleaning compositions comprising at least one of these serine protease variants.

Alpha-amylase combinatorial variants

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

Novel metalloproteases

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof.

Compositions and methods comprising lg12-clade protease variants

The present invention provides serine protease enzymes produced from LG12-clade enzymes. In addition, the present invention provides compositions comprising these protease enzymes. In some embodiments, the present invention provides cleaning compositions comprising at least one of these protease enzymes.

Serine proteases of bacillus species

The present disclosure relates to serine proteases cloned from Bacillus akibai and Bacillus clarkii , and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications.

Serine proteases of the bacillus gibsonii-clade

The present disclosure relates to serine proteases cloned from Bacillus gibsonii, and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications.

Serine proteases of bacillus species

The present disclosure relates to serine proteases cloned from Bacillus spp ., and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications.

Compositions and methods comprising lg12-clade protease variants

The present disclosure provides LG12-clade enzyme variants, compositions comprising these enzyme variants, and method of using these enzymes and compositions, as well as the polynucleotides encoding these enzymes, the vectors comprising these polynucleotides, and the host cells transformed with such vectors.

Bacillus gibsonii-clade serine proteases

Disclosed herein is one or more subtilisin variant, nucleic acid encoding same, and compositions and methods related to the production and use thereof, including one or more Bacillus gibsonii-clade subtilisin variant that has improved stability and/or soil removal compared to one or more reference subtilisin.

Paenibacillus and bacillus spp. mannanases

Disclosed herein are mannanases from Paenibacillus or Bacillus spp , polynucleotides encoding the mannanases, compositions containing the mannanases, and methods of use thereof. Compositions containing mannanases are suitable for use as detergents and for cleaning fabrics and hard surfaces, as well as in a variety of other industrial applications.

Polypeptides with endoglucanase activity and uses thereof

Disclosed herein are cellulase variants, or active fragments thereof, and polynucleotides encoding same, wherein the cellulase variants, or active fragments thereof, hav endoglucanase activity. Also disclosed herein are compositions comprising said cellulase variants, or active fragments thereof; vectors and/or host cells comprising the polynucleotides encoding said cellulase variants, or active fragments thereof; and methods for making and/or using said cellulase variants, or active fragments thereof and/or compositions containing same; wherein said cellulase variants, or active fragments thereof, have endoglucanase activity.

Protease variants and uses thereof

Disclosed herein is one or more subtilisin variant, nucleic acid encoding same, and compositions and methods related to the production and use thereof, including one or more subtilisin variant that has improved stability and/or soil removal compared to one or more reference subtilisin.

Protease variants and uses thereof

Disclosed herein is one or more subtilisin variants, nucleic acids encoding same, and compositions and methods related to the production and uses thereof, including one or more subtilisin variants that has improved stability and/or soil removal compared to one or more reference subtilisin.

Aprl-clade protease variants and uses thereof

The present disclosure provides AprL-clade protease enzymes, including variant AprL-clade protease enzymes, nucleic acids encoding same, and compositions and methods related to the production and use thereof, including an AprL-clade variant subtilisin enzyme that has improved stability and/or soil removal compared to a parent AprL-clade subtilisin enzyme.

Alpha-amylase combinatorial variants

Disclosed are compositions and methods ralting to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

Alpha-amylase combinatorial variants

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

Alpha-amylase conbinatorial variants

Disclosed are compositions and methods ralting to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

Novel metalloproteases

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof.

Novel metalloproteases

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof.

Compositions and methods comprising lg12-clade protease variants

The present invention provides serine protease enzymes produced from LG12-clade enzymes. In addition, the present invention provides compositions comprising these protease enzymes. In some embodiments, the present invention provides cleaning compositions comprising at least one of these protease enzymes.

Serine proteases of bacillus species

The present disclosure relates to serine proteases cloned from Bacillus Akibai and Bacillus Clarkii , and variants thereof. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications.

Serine proteases of the bacillus gibsonii-clade

The present disclosure relates to serine proteases cloned from Bacillus Gibsonii, and variants therefore. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications.

Serine proteases of the bacillus gibsonii-clade

The present disclosure relates to serine proteases cloned from Bacillus Gibsonii, and variants therefore. Compositions containing the serine proteases are suitable for use in cleaning fabrics and hard surfaces, as well as in a variety of industrial applications.

Compositions and methods comprising lg12-clade protease variants

The present disclosure provides LG12-clade enzyme variants, compositions comprising these enzyme variants, and method of using these enzymes and compositions, as well as the polynucleotides encoding these enzymes, the vectors comprising these polynucleotides, and the host cells transformed with such vectors.

Polypeptides with endoglucanase activity and uses thereof

Disclosed herein are cellulase variants, or active fragments thereof, and polynucleotides encoding same, wherein the cellulase variants, or active fragments thereof, hav endoglucanase activity. Also disclosed herein are compositions comprising said cellulase variants, or active fragments thereof; vectors and/or host cells comprising the polynucleotides encoding said cellulase variants, or active fragments thereof; and methods for making and/or using said cellulase variants, or active fragments thereof and/or compositions containing same; wherein said cellulase variants, or active fragments thereof, have endoglucanase activity.

Preparations for topical skin use and treatment

Topical preparations for release of an active agent and to methods of making and using the topical preparations are provided. The preparations may have an internal phase dispersed within an external phase. The internal phase may be a hydrophilic carrier and an active agent. The external phase may be a silicone matrix.

Beta-glucosidase variants with improved properties

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Cel7A (formerly Trichoderma reesei cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Cel7A (formerly Trichoderma reesei cellobiohydrolase I or CBH1 ), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Variants of cellobiohydrolases.

Se describe un número de homólogos y variantes de CeI7A de Hypocrea jecorina (anteriormente celobiohidrolasa I o CBH1 de Trichoderma reesei), ácidos nucleicos que los codifican, y métodos para producirlos. Los homólogos y variantes de celulasas tienen la secuencia de aminoácidos de una glicosil hidrolasa de la familia 7A, en donde uno o más residuos de aminoácidos se sustituyen y/o se eliminan.

MODIFIED α-AMYLASES HAVING ALTERED CALCIUM BINDING PROPERTIES

Novel α-amylase enzymes are disclosed in which a new calcium binding site is modified by chemically or genetically altering residues associated with that calcium binding site. The novel α-amylases have altered performance characteristics, such as low pH starch hydrolysis performance, stability and activity profiles.

Perhydrolase

The present invention provides methods and compositions comprising at least one perhydrolase enzyme for cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions for generation of peracids. The present invention finds particular use in applications involving cleaning, bleaching and disinfecting.

Perhydrolase

The present invention provides methods and compositions comprising at least one perhydrolase enzyme for cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions for generation of peracids. The present invention finds particular use in applications involving cleaning, bleaching and disinfecting.

Perhydrolase

The present invention provides methods and compositions comprising at least one perhydrolase enzyme for cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions for generation of peracids. The present invention finds particular use in applications involving cleaning, bleaching and disinfecting.

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Cel7A (formerly Trichoderma reesei cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Cel7A (formerly Trichoderma reesei cellobiohydrolase I or CBH1 ), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Cel7A (formerly Trichoderma reesei cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Cel7A (formerly Trichoderma reesei cellobiohydrolase I or CBH1 ), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.

Variants of cellobiohydrolases

Disclosed are a number of homologs and variants of Hypocrea jecorina Cel7A (formerly Trichoderma reesei cellobiohydrolase I or CBH1), nucleic acids encoding the same and methods for producing the same. The homologs and variant cellulases have the amino acid sequence of a glycosyl hydrolase of family 7A wherein one or more amino acid residues are substituted and/or deleted.