Engineering the thermotolerance and pH optimum of family 11 xylanases by site-directed mutagenesis

Methods in Enzymology

Volumn 388, Issue , 2004, Pages 156-167

  Turunen, Ossi ^a   Jänis, Janne ^a   Fenel, Fred ^a   Leisola, Matti ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; XYLAN ENDO 1,3 BETA XYLOSIDASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CATALYST; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INACTIVATION; ENZYME PURIFICATION; ENZYME SUBSTRATE; EXPRESSION VECTOR; GENE SEQUENCE; HYDROGEN BOND; ION EXCHANGE; MASS SPECTROMETRY; MOLECULAR MODEL; NONHUMAN; PH MEASUREMENT; PKA; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN FAMILY; SITE DIRECTED MUTAGENESIS; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; BACILLUS; BINDING SITES; DISULFIDES; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; TRICHODERMA; XYLOSIDASES;

VECTORS;

EID: 4043183430     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(04)88014-5     Document Type: Article

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