Isolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183

Y K Hoh; H H Yeoh; T K Tan

doi:10.1007/BF00386292

Isolation and characterization of β-glucosidases from Aspergillus nidulans mutant USDB 1183

World J Microbiol Biotechnol. 1993 Sep;9(5):555-8. doi: 10.1007/BF00386292.

Authors

Y K Hoh¹, H H Yeoh, T K Tan

Affiliation

¹ Department of Botany, Faculty of Science, National University of Singapore, 10 Kent Ridge Crescent, 0511, Singapore, Singapore.

PMID: 24420198
DOI: 10.1007/BF00386292

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 Fe(2+) and Fe(3+) than β-glucosidase II.