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|Title:||Isolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183||Authors:||Hoh, Y.K.
|Issue Date:||Sep-1993||Citation:||Hoh, Y.K., Yeoh, H.-H., Tan, T.K. (1993-09). Isolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183. World Journal of Microbiology & Biotechnology 9 (5) : 555-558. ScholarBank@NUS Repository. https://doi.org/10.1007/BF00386292||Abstract:||Two extracellular β-glucosidases (cellobiase, EC 188.8.131.52), I and II, from Aspergillus nidulans USDB 1183 were purified to homogeneity with molecular weights of 240,000 and 78,000, respectively. Both hydrolysed laminaribiose, β-gentiobiose, cellobiose, p-nitrophenyl-β-L-glucoside, phenyl-β-L-glucoside, o-nitrophenyl-β-L-glucoside, salicin and methyl-β-L-glucoside but not α-linked disaccharides. Both were competitively inhibited by glucose and non-competitively (mixed) inhibited by glucono-1,5-lactone. β-Glucosidase I was more susceptible to inhibition by Ag+ and less inhibited by Fe2+ and Fe3+ than β-glucosidase II. © 1993 Rapid Communications of Oxford Ltd.||Source Title:||World Journal of Microbiology & Biotechnology||URI:||http://scholarbank.nus.edu.sg/handle/10635/99697||ISSN:||09593993||DOI:||10.1007/BF00386292|
|Appears in Collections:||Staff Publications|
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