US2009155413A1PendingUtilityA1
Enzyme
Est. expiryMar 8, 2020(expired)· nominal 20-yr term from priority
C12N 9/2482C12Y 302/01008
60
PatentIndex Score
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Claims
Abstract
The present invention relates to a variant xylanase polypeptide, or fragment thereof having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with parent enzyme.
Claims
exact text as granted — not AI-modified1 - 22 . (canceled)
23 . A method of degrading or modifying a plant cell wall which method comprises contacting said plant cell wall with a polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
24 . A method according to claim 23 wherein said polypeptide is derived from a family 11 xylanase.
25 . A method according to claim 23 wherein said amino acid modification is of one or more surface amino acid residues.
26 . A method according to claim 23 wherein said amino acid modification is of one or more solvent accessible residues.
27 . A method according to claim 23 wherein there are at least two of said amino acid modifications.
28 . A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,
of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or its/their equivalent positions in other homologous xylanase polypeptides.
29 . A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
30 . A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
31 . A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
32 . A method according to claim 23 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
33 . A method according to claim 23 wherein the inhibitor is an inhibitor found naturally in plant tissues.
34 . A method according to claim 23 wherein the sensitivity to the inhibitor is reduced.
35 . A method of processing a plant material which method comprises contacting said plant material with a polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
36 . A method according to claim 35 wherein said polypeptide is derived from a family 11 xylanase.
37 . A method according to claim 35 wherein said amino acid modification is of one or more surface amino acid residues.
38 . A method according to claim 35 wherein said amino acid modification is of one or more solvent accessible residues.
39 . A method according to claim 35 wherein there are at least two of said amino acid modifications.
40 . A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,
of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or its/their equivalent positions in other homologous xylanase polypeptides.
41 . A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
42 . A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
43 . A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
44 . A method according to claim 35 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
45 . A method according to claim 35 wherein the inhibitor is an inhibitor found naturally in plant tissues.
46 . A method according to claim 35 wherein the sensitivity to the inhibitor is reduced.
47 . A method of baking or processing cereals or starch production or processing wood or enhancing the bleaching of wood pulp which method comprises the use of a polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
48 . A method according to claim 47 wherein said polypeptide is derived from a family 11 xylanase.
49 . A method according to claim 47 wherein said amino acid modification is of one or more surface amino acid residues.
50 . A method according to claim 47 wherein said amino acid modification is of one or more solvent accessible residues.
51 . A method according to claim 47 wherein there are at least two of said amino acid modifications.
52 . A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,
of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or its/their equivalent positions in other homologous xylanase polypeptides.
53 . A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
54 . A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
55 . A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
56 . A method according to claim 47 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
57 . A method according to claim 47 wherein the inhibitor is an inhibitor found naturally in plant tissues.
58 . A method according to claim 47 wherein the sensitivity to the inhibitor is reduced.
59 . A nucleotide sequence encoding a variant polypeptide, wherein said polypeptide is a variant xylanase polypeptide, or fragment thereof having xylanase activity; wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, comprises one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme.
60 . A nucleotide sequence according to claim 59 wherein said polypeptide is derived from a family 11 xylanase.
61 . A nucleotide sequence according to claim 59 wherein said amino acid modification is of one or more surface amino acid residues.
62 . A nucleotide sequence according to claim 59 wherein said amino acid modification is of one or more solvent accessible residues.
63 . A nucleotide sequence according to claim 59 wherein there are at least two of said amino acid modifications.
64 . A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues:
Ala1-Trp6, Asn8, Thr10-Gly23, Asn25, Ser27, Asn29, Ser31-Asn32, Gly34, Thr43-Thr44, Ser46-Thr50, Asn52, Asn54, Gly56-Asn61, Asn63, Arg73-Leu76, Thr87-Arg89, Thr91-Lys95, Thr97, Lys99, Asp101-Gly102, Thr104, Thr109-Thr111, Tyr113-Asn114, Asp119-Thr124, Thr126, Gln133-Asn141, Thr143, Thr145, Thr147-Asn148, Asn151, Lys154-Gly157, Asn159-Leu160, Ser162-Trp164, Gln175, Ser177, Ser179, Asn181, Thr183,
of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or its/their equivalent positions in other homologous xylanase polypeptides.
65 . A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
66 . A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues.
67 . A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other amino acid residues are any one or more of amino acid residues numbers: 3, 4, 5, 6, 7, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 38, 39, 40, 41, 42, 43, 44, 45, 55, 56, 57, 58, 59, 60, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 108, 109, 110, 126, 127, 128, 129, 130, 131, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168, 169, 170, 171, 172, 179, 180, 181, 182, 183 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
68 . A nucleotide sequence according to claim 59 wherein said amino acid modification is at any one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides; and wherein said variant xylanase polypeptide, or fragment thereof having xylanase activity, in addition comprises one or more amino acid modifications at any one of the other amino acid residues; and wherein said other surface amino acid residues are any one or more of amino acid residues numbers: 1, 2, 46, 47, 48, 49, 50, 51, 52, 53, 54, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149, 150, 151, 152, 153, 154, 155, 156, 157, 184, 185 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1 or their equivalent positions in other homologous xylanase polypeptides.
69 . A nucleotide sequence according to claim 59 wherein the inhibitor is an inhibitor found naturally in plant tissues.
70 . A nucleotide sequence according to claim 59 wherein the sensitivity to the inhibitor is reduced.
71 . A method according to claim 23 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
72 . A method according to claim 23 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
73 . A method according to claim 23 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
74 . A method according to claim 23 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
75 . A method according to claim 35 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
76 . A method according to claim 35 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
77 . A method according to claim 35 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
78 . A method according to claim 35 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
79 . A method according to claim 47 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
80 . A method according to claim 47 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
81 . A method according to claim 47 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
82 . A method according to claim 47 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
83 . A nucleotide sequence according to claim 59 wherein said polypeptide has at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
84 . A nucleotide sequence according to claim 59 wherein said polypeptide has at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
85 . A nucleotide sequence according to claim 59 wherein said polypeptide has at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
86 . A nucleotide sequence according to claim 59 wherein said polypeptide has at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package.
87 . A method according to claim 23 wherein said polypeptide is derivable from SEQ ID NO: 9.
88 . A method according to claim 35 wherein said polypeptide is derivable from SEQ ID NO: 9.
89 . A method according to claim 47 wherein said polypeptide is derivable from SEQ ID NO: 9.
90 . A nucleotide sequence according to claim 59 wherein said polypeptide is derivable from SEQ ID NO: 9.
91 . An isolated variant polypeptide or fragment thereof having at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package, and having xylanase activity, comprising two or more amino acid modifications, wherein said amino acid modifications are at two or more of positions 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ ID NO: 1, or their equivalent positions in other family 11 xylanases, such that the polypeptide or fragment thereof has altered sensitivity to a xylanase inhibitor as compared with the parent xylanase, wherein one of said modifications is at position 11, wherein the variant polypeptide is a family 11 xylanase.
92 . An isolated variant polypeptide or fragment thereof having at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package, and having xylanase activity, comprising two or more amino acid modifications, wherein said amino acid modifications are at two or more of positions 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ ID NO: 1, or their equivalent positions in other family 11 xylanases, such that the polypeptide or fragment thereof has altered sensitivity to a xylanase inhibitor as compared with the parent xylanase, wherein one of said modifications is at position 11, wherein the variant polypeptide is a family 11 xylanase.
93 . An isolated variant polypeptide or fragment thereof having at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package, and having xylanase activity, comprising two or more amino acid modifications, wherein said amino acid modifications are at two or more of positions 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ ID NO: 1, or their equivalent positions in other family 11 xylanases, such that the polypeptide or fragment thereof has altered sensitivity to a xylanase inhibitor as compared with the parent xylanase, wherein one of said modifications is at position 11, wherein the variant polypeptide is a family 11 xylanase.
94 . A variant xylanase polypeptide, or fragment thereof having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
95 . A variant xylanase polypeptide, or fragment thereof having at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
96 . A variant xylanase polypeptide, or fragment thereof having at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues;
wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
97 . A variant xylanase polypeptide, or fragment thereof having at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues;
wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
98 . A variant xylanase polypeptide, or fragment thereof having at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from SEQ ID No. 9.
99 . A method according to claim 23 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
100 . A method according to claim 35 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
101 . A method according to claim 47 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
102 . A nucleotide sequence according to claim 59 wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
103 . A variant xylanase polypeptide, or fragment thereof having at least 40% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues;
wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
104 . A variant xylanase polypeptide, or fragment thereof having at least 50% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
105 . A variant xylanase polypeptide, or fragment thereof having at least 60% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
106 . A variant xylanase polypeptide, or fragment thereof having at least 80% homology to SEQ ID NO: 1 as determined by using the GCG Wisconsin Bestfit package and having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride Xyn
107 . A variant xylanase polypeptide, or fragment thereof having xylanase activity, comprising one or more amino acid modifications such that the polypeptide or fragment thereof has an altered sensitivity to a xylanase inhibitor as compared with the parent xylanase enzyme; wherein the variant polypeptide is derived from a family 11 xylanase; wherein said amino acid modification is of two or more surface amino acid residues; wherein said amino acid modification is at an equivalent position to one or more of amino acid residues numbers: 11, 12, 13, 15, 17, 29, 31, 32, 34, 113, 114, 119, 120, 121, 122, 123, 124 and 175 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; wherein one of said modifications is at an equivalent position to amino acid residue number 11 of the B. subtilis amino acid sequence shown as SEQ I.D. No. 1; and wherein said polypeptide is derivable from any of the xylanase sequences presented in FIG. 2 or referred to in the following Table:
Aspergillus niger Xyn A
Aspergillus kawachii Xyn C
Aspergillus tubigensis Xyn A
Bacillus circulans Xyn A
Bacillus pumilus Xyn A
Bacillus subtilis Xyn A
Cellulomonas fimi Xyn D
Chainia spp. Xyn
Clostridium acetobutylicum Xyn B
Clostridium stercorarium Xyn A
Fibrobacter succinogenes Xyn C
Neocallimastix patriciarum Xyn A
Nocardiopsis dassonvillei Xyn II
Ruminococcus flavefaciens Xyn A
Schizophyllum commune Xyn
Streptomyces lividans Xyn B
Streptomyces lividans Xyn C
Streptomyces sp. No. 36a Xyn
Streptomyces thermoviolaceus Xyn II
Thermomonospora fusca Xyn A
Trichoderma harzianum Xyn
Trichoderma reesei Xyn I
Trichoderma reesei Xyn II
Trichoderma viride XynJoin the waitlist — get patent alerts
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