Function of the family-9 and family-22 carbohydrate-binding modules in a modular β-1,3-1,4-glucanase/xylanase derived from Clostridium stercorarium Xyn10B

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 8, 2005, Pages 1562-1567

  Zhao, Guangshan ^a   Ali, Ehsan ^a   Araki, Rie ^a   Sakka, Makiko ^a   Kimura, Tetsuya ^a   Sakka, Kazuo ^a  

^a MIE UNIVERSITY   (Japan)

Author keywords

1,3 1,4 glucanase; Carbohydrate binding module (CBM); Clostridium stercorarium; Xylanase

Indexed keywords

CARBOHYDRATES; CATALYSIS; CATALYST ACTIVITY; HYDROLYSIS; PLANTS (BOTANY); POLYPEPTIDES; POLYSACCHARIDES;

Β-1,3-1,4-GLUCANASE; CARBOHYDRATE-BINDING MODULE (CBM); CLOSTRIDIUM STERCORARIUM; XYLANASE;

ENZYMES;

ENDO 1,4 BETA XYLANASE; GLYCOSIDASE; PRIMER DNA;

ARTICLE; CARBOHYDRATE METABOLISM; CHEMISTRY; CLOSTRIDIUM; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; NUCLEOTIDE SEQUENCE; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS;

BASE SEQUENCE; CARBOHYDRATE METABOLISM; CLOSTRIDIUM; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDO-1,4-BETA XYLANASES; GLYCOSIDE HYDROLASES; PLASMIDS; SUBSTRATE SPECIFICITY;

CLOSTRIDIUM; CLOSTRIDIUM STERCORARIUM;

EID: 23944472099     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.69.1562     Document Type: Article

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