A single amino acid substitution enhances the catalytic activity of family 11 xylanase at alkaline pH

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 8, 2005, Pages 1492-1497

  Shibuya, Hajime ^a   Kaneko, Satoshi ^b   Hayashi, Kiyoshi ^b  

^a FORESTRY AND FOREST PRODUCTS RESEARCH INSTITUTE   (Japan)

^b NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

Author keywords

Alkalophilic; Family 11; pH dependent activity; Random mutagenesis; Xylanase

Indexed keywords

DYES; ENZYMES; MUTAGENESIS; PARAMETER ESTIMATION; PH; SOLUBILITY;

ALKALOPHILIC; FAMILY 11; PH-DEPENDENT ACTIVITY; RANDOM MUTAGENESIS; XYLANASE;

GENES;

ENDO 1,4 BETA XYLANASE; PRIMER DNA;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PH;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; CATALYSIS; DNA PRIMERS; ENDO-1,4-BETA XYLANASES; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA;

STREPTOMYCES LIVIDANS; THERMOBIFIDA FUSCA;

EID: 23944468483     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.69.1492     Document Type: Article

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