Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/99651
Title: Cassava leaf β-glucosidase specificity and inhibition
Authors: Hock-Hin, Y. 
Hin-Cheow, W.
Keywords: β-glucosidase
cassava
Euphorbiaceac
inhibitors.
Manihot esculenta
substrate specificity
Issue Date: Jul-1992
Citation: Hock-Hin, Y.,Hin-Cheow, W. (1992-07). Cassava leaf β-glucosidase specificity and inhibition. Phytochemistry 31 (7) : 2263-2265. ScholarBank@NUS Repository.
Abstract: The specificity of cassava leaf β-glucosidase towards 33 glycosides was examined. Only 11 glycosides were hydrolysed. Among these, there was greater preference for p-nitrophenyl-p-d-glucoside, p-nitrophenyl-β-d-fucoside and linamarin than for o-nitrophenyl-β-d-glucoside, o-nitrophenyl-β-d-fucoside, p-nitrophenyl-β-d-galactoside, p-nitrophenyl-β-d-mannoside, p-nitrophenyl-β-d-xyloside, phenyl-β-glucoside, prunasin and salicin. Glycosides having disaccharide residues as well as α- and β-linked diglucosides were not hydrolysed. The type of glycone and aglycone for the glycoside appeared to be important for enzyme activity. Results of pH dependence studies using p-nitrophenyl-β-d-glucoside, p-nitrophenyl-β-d-fucoside and linamarin as substrates suggested involvement of an acidic amino acid side chain in the enzyme active site. Glucono-1,5-Iactone inhibited the enzyme competitively. The other monosaccharides and their derivatives tested did not show any inhibition of enzyme activity. © 1992.
Source Title: Phytochemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/99651
ISSN: 00319422
Appears in Collections:Staff Publications

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