The enzymic properties of three electrophoretically distinct β-glucosidases, β-glucosidase-l, -2 and -3, from Aspergillus aculeatus No. F-50 were investigated. β-Glucosidase-3 had a low optimum pH of 3.0, but the other two enzymes had optimum pHs of 4.0~4.5. Both β-glucosidase-l and -2 were potently active not only on soluble cellooligosaccharides, such as cellotriose to cellohexaose, but also on insoluble cellooligosaccharide, of which the average degree of polymerization was 20. On the contrary, β-glucosidase-3 was only slightly active on the insoluble substrate. The combined use of either β-glucosidase-1 or -2 and endo-glucanase remarkably stimulated the hydrolysis of amorphous cellulose, yielding glucose only. But jS-glucosidase-3 did not show such a synergistic effect, and the glucose content of the hydrolyzate was only about 60%. © 1985, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.
CITATION STYLE
Sakamoto, R., Arai, M., & Murao, S. (1985). Enzymic Properties of Three β-Glucosidases from Aspergillus Aculeatus No. F-50. Agricultural and Biological Chemistry, 49(5), 1283–1290. https://doi.org/10.1271/bbb1961.49.1283
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