Partial purification and characterization of a new intracellular β-glucosidase of Trichoderma reesei
- 1 February 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 185 (2), 515-519
- https://doi.org/10.1042/bj1850515
Abstract
A new intracellular .beta.-glucosidase was isolated from T. reesei. It was sequentially purified by (NH4)2SO4 precipitation and chromatography and rechromatography on Sephadex G-150. The enzyme has a MW of 98,000, optimal activity at pH 6.5, an isoelectric point of 4.4 and Km values of 6.7 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.This publication has 10 references indexed in Scilit:
- Induction of cellulolytic enzymes in Trichoderma reesei by sophoroseJournal of Bacteriology, 1979
- Cellobiase from Trichoderma viride: Purification, properties, kinetics, and mechanismBiotechnology & Bioengineering, 1977
- Sophorose metabolism and cellulase induction in TrichodermaArchiv für Mikrobiologie, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- The Mechanism of Enzymatic Cellulose DegradationEuropean Journal of Biochemistry, 1974
- Catabolite Repression of Cellulase Formation in Trichoderma viride*The Journal of Biochemistry, 1972
- INDUCTION OF CELLULASE IN FUNGI BY CELLOBIOSEJournal of Bacteriology, 1960