The use of forced protein evolution to investigate and improve stability of family 10 xylanases: The production of Ca2--independent stable xylanases

Journal of Biological Chemistry

Volumn 279, Issue 52, 2004, Pages 54369-54379

  Andrews, Simon R ^b   Taylor, Edward J ^a,b   Pell, Gavin ^b   Vincent, Florence ^a   Ducros, Valérie M A ^a   Davies, Gideon J ^a   Lakey, Jeremy H ^b   Gilbert, Harry J ^b  

^a UNIVERSITY OF YORK   (United Kingdom)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOTECHNOLOGY; CALCIUM; ENZYMES; FREE ENERGY; VAN DER WAALS FORCES;

METAL IONS; THERMOSTABILITY; XYLANASE;

PROTEINS;

CALCIUM; PROTEIN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

AMINO ACID SUBSTITUTION; ARTICLE; CELLULOMONAS; CELLVIBRIO; DISULFIDE BOND; ENZYME STABILITY; ENZYME SYNTHESIS; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; THERMOSTABILITY;

BINDING SITES; CALCIUM; CELLVIBRIO; CHEMISTRY, PHYSICAL; CRYSTALLIZATION; DIRECTED MOLECULAR EVOLUTION; DISULFIDES; DRUG RESISTANCE; EDETIC ACID; ENDO-1,4-BETA XYLANASES; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; HYDROGEN BONDING; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; PEPTIDE HYDROLASES; POLYMERASE CHAIN REACTION; PROTEIN FOLDING; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SULFHYDRYL COMPOUNDS; THERMODYNAMICS; XYLOSIDASES;

CELLULOMONAS; CELLULOMONAS FIMI; CELLVIBRIO; CELLVIBRIO JAPONICUS;

EID: 11144224089     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M409044200     Document Type: Article

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