Abstract
Two extracellular β-glucosidases (cellobiase, EC 3.2.1.21), 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.
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Hoh, Y.K., Yeoh, H.H. & Tan, T.K. Isolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183. World J Microbiol Biotechnol 9, 555–558 (1993). https://doi.org/10.1007/BF00386292
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DOI: https://doi.org/10.1007/BF00386292