The role of carboxyl groups on the chitosanase and CMCase activity of a bifunctional enzyme purified from a commercial cellulase with EDC modification

Biochemical Engineering Journal

Volumn 41, Issue 2, 2008, Pages 142-148

  Liu, Ping ^a   Xia, Wenshui ^a,b   Liu, Jing ^c  

^a JIANGNAN UNIVERSITY   (China)

^b WUHAN POLYTECHNIC UNIVERSITY   (China)

^c Jiangsu Animal Husbandry and Veterinary College   (China)

Author keywords

Active site; Cellulase; Chemical modification; Chitosanase; EDC; Lysozyme

Indexed keywords

AMINES; BINDING ENERGY; CARBOXYLATION; DYNAMIC ANALYSIS; FOOD ADDITIVES; PROTONS; PURIFICATION; QUALITY ASSURANCE; RELIABILITY;

AMINOPROPYL; BI FUNCTIONAL ENZYMES; BIFUNCTIONAL; CARBODI IMIDE; CARBOXYL GROUPS; CHITOSANASE (CHOA); ELSEVIER (CO); STRUCTURE INTEGRITY; SUBSTRATE BINDING (SBD); SUBSTRATE RECOGNITION; TRICHODERMA VIRIDE; WATER SOLUBLE CARBODIIMIDE (WSC);

ENZYME ACTIVITY;

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; CARBOXYL GROUP; CELLULASE; CHITOSAN; CHITOSANASE; LYSOZYME;

ARTICLE; CHEMICAL BINDING; CHEMICAL MODIFICATION; CIRCULAR DICHROISM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME PURIFICATION; ENZYME SUBSTRATE; MOLECULAR RECOGNITION; PRIORITY JOURNAL;

TRICHODERMA VIRIDE;

EID: 48049116647     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2008.04.011     Document Type: Article

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