Subtilisins modified at position 225 resulting in a shift in catalytic
activity
    2.
    发明授权
    Subtilisins modified at position 225 resulting in a shift in catalytic activity 失效
    在225位修饰的枯草杆菌蛋白酶导致催化活性的变化

    公开(公告)号:US5155033A

    公开(公告)日:1992-10-13

    申请号:US294340

    申请日:1989-01-06

    IPC分类号: C12N9/56

    CPC分类号: C12N9/54

    摘要: There are described certain subtilisins wherein the amino acid sequence of such subtilisins has been modified at a position equivalent to +225 in Bacillus amyloliquefaciens, such that an amino acid selected from the group consisting of alanine, leucine, methionine, glutamine, valine, and serine, has been substituted for the amino acid residue naturally occurring at such position.

    摘要翻译: 描述了某些枯草杆菌蛋白酶,其中这种枯草杆菌蛋白酶的氨基酸序列已经在解淀粉芽孢杆菌中相当于+225的位置被修饰,使得选自丙氨酸,亮氨酸,甲硫氨酸,谷氨酰胺,缬氨酸和丝氨酸的氨基酸 已取代天然存在于该位置的氨基酸残基。

    Subtilisin mutants
    3.
    发明授权

    公开(公告)号:US5204015A

    公开(公告)日:1993-04-20

    申请号:US958885

    申请日:1992-10-09

    摘要: Novel carbonyl hydrolase mutants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases are disclosed. The mutant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to generate the substitution of one or more amino acid residues in the amino acid sequence of a precursor carbonyl hydrolase. Such mutant carbonyl hydrolases have properties which are different from those of the precursor hydrolase and are especially useful in detergent formulations. The substituted amino acid residues correspond to position +123 and/or +274 in Bacillus amyloliquefaciens subtilisin.

    Subtilisin variants
    5.
    发明授权
    Subtilisin variants 失效
    枯草杆菌蛋白酶变体

    公开(公告)号:US07250281B2

    公开(公告)日:2007-07-31

    申请号:US10323324

    申请日:2002-12-18

    CPC分类号: C11D3/38609 C12N9/54

    摘要: Novel carbonyl hydrolase variants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases are disclosed. The variant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor carbonyl hydrolase. Such variant carbonyl hydrolases have properties which are different from those of the precursor hydrolase, such as altered proteolytic activity, altered stability, etc. The substituted amino acid residues correspond to positions +76 in combination with one or more of the following residues +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265 and/or +274 in Bacillus amyloliquefaciens subtilisin.

    摘要翻译: 公开了衍生自天然存在或重组非人羰基水解酶的DNA序列的新型羰基水解酶变体。 变体羰基水解酶通常通过体外修饰编码天然存在或重组羰基水解酶的前体DNA序列获得,以产生前体羰基水解酶的氨基酸序列中的多个氨基酸残基的取代。 这种变体羰基水解酶具有与前体水解酶不同的性质,例如改变的蛋白水解活性,改变的稳定性等。取代的氨基酸残基对应于与一个或多个以下残基组合的位置+76, +101,+103,+104,+107,+123,+27,+105,+ 109,+126,+128,+135,+ 156,+166,+ 195,+ 197,+ 204,+ 206 ,+210,+ 216,+ 217,+ 218,+ 222,+ 260,+ 265和/或+ 274的解淀粉芽孢杆菌枯草杆菌蛋白酶。

    Subtilisin variants multiply-substituted subtilising variants having a substitution at position 76
    6.
    发明授权
    Subtilisin variants multiply-substituted subtilising variants having a substitution at position 76 失效
    枯草杆菌蛋白酶变体在第76位具有取代的多取代的枯草芽孢杆菌变体

    公开(公告)号:US06586221B2

    公开(公告)日:2003-07-01

    申请号:US08322678

    申请日:1994-10-13

    IPC分类号: C12N950

    CPC分类号: C11D3/38609 C12N9/54

    摘要: Novel carbonyl hydrolase variants derived from the DNA sequences of naturally-occurring or recombinant non-human carbonyl hydrolases are disclosed. The variant carbonyl hydrolases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant carbonyl hydrolase to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor carbonyl hydrolase. Such variant carbonyl hydrolases have properties which are different from those of the precursor hydrolase, such as altered proteolytic activity, altered stability, etc. The substituted amino acid residues correspond to positions +76 in combination with one or more of the following residues +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265 and/or +274 in Bacillus amyloliquefaciens subtilisin.

    摘要翻译: 公开了衍生自天然存在或重组非人羰基水解酶的DNA序列的新型羰基水解酶变体。 变体羰基水解酶通常通过体外修饰编码天然存在或重组羰基水解酶的前体DNA序列获得,以产生前体羰基水解酶的氨基酸序列中的多个氨基酸残基的取代。 这种变体羰基水解酶具有与前体水解酶不同的性质,例如改变的蛋白水解活性,改变的稳定性等。取代的氨基酸残基对应于与一个或多个以下残基组合的位置+76, +101,+103,+104,+107,+123,+27,+105,+ 109,+126,+128,+135,+ 156,+166,+ 195,+ 197,+ 204,+ 206 ,+210,+ 216,+ 217,+ 218,+ 222,+ 260,+ 265和/或+ 274的解淀粉芽孢杆菌枯草杆菌蛋白酶。

    Chemically modified enzymes
    7.
    发明授权
    Chemically modified enzymes 失效
    化学修饰的酶

    公开(公告)号:US06277617B1

    公开(公告)日:2001-08-21

    申请号:US08978509

    申请日:1997-11-25

    IPC分类号: A61K3848

    CPC分类号: C11D3/38663 C12N9/00 C12N9/54

    摘要: Modified enzymes are provided in which at least one amino acid, such as asparagine, leucine, methionine or serine, of an enzyme is replaced with a cysteine and the thiol hydrogen is replaced with a substituent group providing a thiol side chain selected from the group consisting of: a) —SR1R2, wherein R1 is an alkyl and R2 is a charged or polar moiety; b) —SR3, wherein R3 is a substituted or unsubstituted phenyl; c) —SR4, wherein R4 is substituted or unsubstituted cyclohexyl; d) —SR5, wherein R5 is C10-C15 alkyl; and e) —SR6 wherein R6 is a C1-6 alkyl. Also, methods of producing the modified enzymes are provided, as well as detergent and feed additives and a composition for the treatment of a textile. A method for using the modified enzymes in organic synthesis is additionally provided. Further, modified enzymes having improved activity, altered pH profile and/or wash performance are provided.

    摘要翻译: 提供了修饰的酶,其中酶的至少一个氨基酸,例如天冬酰胺,亮氨酸,甲硫氨酸或丝氨酸被半胱氨酸替代,硫醇氢被提供选自以下的硫醇侧链的取代基取代: a)-SR1R2,其中R1是烷基,R2是带电荷或极性部分; b)-SR3,其中R3是取代或未取代的苯基; c)-SR4,其中R4是取代或未取代的环己基; d) -SR 5,其中R 5为C 10 -C 15烷基; 安德)-SR6,其中R6是C1-6烷基。此外,提供了制备修饰酶的方法,以及洗涤剂和饲料添加剂以及用于处理织物的组合物。 另外提供了在有机合成中使用修饰的酶的方法。 此外,提供了具有改善的活性,改变的pH曲线和/或洗涤性能的修饰的酶。

    Enzyme treatment to enhance wettability and absorbency of textiles
    8.
    发明授权
    Enzyme treatment to enhance wettability and absorbency of textiles 失效
    酶处理以增强纺织品的润湿性和吸收性

    公开(公告)号:US6066494A

    公开(公告)日:2000-05-23

    申请号:US952617

    申请日:1998-03-16

    摘要: Textile fibers are treated with enzymes in the absence of surfactants, with the effect of increasing the wettability and absorbency of the fibers. The enzymes are pectinases, cellulases, proteases, lipases or combinations thereof. The wetting properties of cotton fibers are found to be most substantially improved by treatment with a mixture of cellulase and pectinase. The effects of five hydrolyzing enzymes on improving the hydrophilicity of several polyester fabrics have been studied. Four out of the five lipases studied improve the water wetting and absorbent properties of the regular polyester fabrics more than alkaline hydrolysis under optimal conditions (3N NaOH at 55.degree. C. for 2 hours). Compared to aqueous hydrolysis, the enzyme reactions have shown to be effective under more moderate conditions, including a relatively low concentration (0.01 g/L), a shorter reaction time (10 minutes), at an ambient temperature (25.degree. C.). Contrary to the results with alkaline hydrolysis, the improved water wettability is accompanied by full strength retention. Lipase has also shown to be effective in improving the wetting and absorbent properties of sulfonated polyester and microdenier polyester fabrics.

    摘要翻译: PCT No.PCT / US97 / 03411 Sec。 371日期:1998年3月16日 102(e)1998年3月16日PCT 1997年3月6日PCT公布。 第WO97 / 33001号公报 日期1997年9月12日在没有表面活性剂的情况下用酶处理纺织纤维,具有增加纤维的润湿性和吸收性的作用。 酶是果胶酶,纤维素酶,蛋白酶,脂肪酶或其组合。 通过用纤维素酶和果胶酶的混合物处理,发现棉纤维的润湿性能最显着地提高。 已经研究了五种水解酶对改善几种聚酯织物亲水性的影响。 所研究的五种脂肪中的四种在最佳条件下(3N NaOH在55℃下2小时)改善了常规聚酯织物的水润湿性和吸水性,而不是碱性水解。 与水解水解相比,酶反应在环境温度(25℃)下在更温和的条件下有效,包括较低的浓度(0.01g / L),较短的反应时间(10分钟)。 与碱性水解的结果相反,改善的水润湿性伴随着完全的强度保持。 脂肪酶也显示出有效地改善了磺化聚酯和微米聚酯织物的润湿和吸收性能。

    Enzyme treatment to enhance wettability and absorbancy of textiles
    10.
    发明授权
    Enzyme treatment to enhance wettability and absorbancy of textiles 有权
    酶处理以增强纺织品的润湿性和吸收性

    公开(公告)号:US06436696B1

    公开(公告)日:2002-08-20

    申请号:US09472660

    申请日:1999-12-27

    IPC分类号: C12S1100

    摘要: Textile fibers are treated with enzymes in the absence of surfactants, with the effect of increasing the wettability and absorbency of the fibers. The enzymes are pectinases, cellulases, proteases, lipases or combinations thereof. The wetting properties of cotton fibers are found to be most substantially improved by treatment with a mixture of cellulase and pectinase. The effects of five hydrolyzing enzymes on improving the hydrophilicity of several polyester fabrics have been studied. Four out of the five lipases studied improve the water wetting and absorbent properties of the regular polyester fabrics more than alkaline hydrolysis under optimal conditions (3N NaOH at 55° C. for 2 hours). Compared to aqueous hydrolysis, the enzyme reactions have shown to be effective under more moderate conditions, including a relatively low concentration (0.01 g/L), a shorter reaction time (10 minutes), at an ambient temperature (25° C.). Contrary to the results with alkaline hydrolysis, the improved water wettability is accompanied by full strength retention. Lipase has also shown to be effective in improving the wetting and absorbent properties of sulfonated polyester and microdenier polyester fabrics.

    摘要翻译: 纺织纤维在没有表面活性剂的情况下用酶处理,具有增加纤维的润湿性和吸收性的作用。 酶是果胶酶,纤维素酶,蛋白酶,脂肪酶或其组合。 通过用纤维素酶和果胶酶的混合物处理,发现棉纤维的润湿性能最显着地提高。 已经研究了五种水解酶对改善几种聚酯织物亲水性的影响。 所研究的五种脂肪中的四种在最佳条件下(3N NaOH在55℃下2小时)改善了常规聚酯织物的水润湿性和吸水性,而不是碱性水解。 与水解水解相比,酶反应已经显示在更温和的条件下有效,包括相对低的浓度(0.01g / L),较短的反应时间(10分钟),在环境温度(25℃)下。 与碱性水解的结果相反,改善的水润湿性伴随着完全的强度保持。 脂肪酶也显示出有效地改善了磺化聚酯和微米聚酯织物的润湿和吸收性能。