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. 1980 Feb 1;185(2):515–519. doi: 10.1042/bj1850515

Partial purification and characterization of a new intracellular beta-glucosidase of Trichoderma reesei.

M Inglin, B A Feinberg, J R Loewenberg
PMCID: PMC1161380  PMID: 6772150

Abstract

A new intracellular beta-glucosidase was isolated from Trichoderma reesei. It was sequentially purified by (NH4)2SO4 precipitation and chromatography and rechromatography on Sephadex G-150. The enzyme has a mol.wt. of 98 000, optimal activity at pH 6.5, pI 4.4 and Km values of 6.7 mM and 3.3 mM for sophorose and cellobiose respectively. Possible functions of the enzyme may be regulation of cellulase induction and/or to serve as a proenzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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