Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/99700
Title: Kinetic properties of β-glucosidase from cassava
Authors: Yeoh, H.-H. 
Keywords: β-glucosidase
cassava
inhibition kinetics.
Km values
linamarase
Manihot esculenta
Issue Date: 1989
Source: Yeoh, H.-H. (1989). Kinetic properties of β-glucosidase from cassava. Phytochemistry 28 (3) : 721-724. ScholarBank@NUS Repository.
Abstract: β-Glucosidases from the leaf, peel and tuber cortex of cassava cv. Merah Jambu exhibited linamarase activity and had in common many kinetic properties. They were also capable of hydrolysing p-nitrophenyl-β-d-monoglycosides and cyanogenic β-monoglucosides but lacked activity towards the p-nitrophenyl-β-d-diglycosides, a cyanogenic diglucoside, and other β- or α-linked disaccharides. The Km values for p-nitrophenyl-β-d-monoglycosides were generally lower than those for linamarin, prunasin and salicin. Ag2+ inhibited both β-glucosidase and linamarase activities. Glucono-1,5-lactone inhibited the enzyme competitively, irrespective of the substrates used, while imidazole showed competitive inhibition with linamarin but non-competitive (mixed) inhibition with p-nitrophenyl-β-d-glucoside. The enzyme was unaffected by glucose. © 1989.
Source Title: Phytochemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/99700
ISSN: 00319422
Appears in Collections:Staff Publications

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