The adaptability, purification and properties of exo-β 1,3-glucanase from the fungus Trichoderma reesei
- 1 December 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 191 (3), 863-866
- https://doi.org/10.1042/bj1910863
Abstract
The fungus T. reesei grows on barley (Hordeum vulgare L.) .beta.-glucan and pachyman, secreting increased quantities of exo-.beta.1,3-glucanase. This enzyme is found in commercial cellulase preparations, from which it has been partially purified. It has a MW of 70,000, an isoelectric point of 4.2, is cold-stable and hydrolyzes both .beta.1 .fwdarw. 3- and .beta.1 .fwdarw. 6-linkages.This publication has 14 references indexed in Scilit:
- A new staining technique for proteins in polyacrylamide gels using Coomassie brilliant blue G250Analytical Biochemistry, 1977
- A new spectrophotometric assay for protein in cell extractsAnalytical Biochemistry, 1977
- The Role of Protein in the Structure of Barley Endosperm Cell WallsBiochemical Society Transactions, 1977
- Purification of an exo-β-D-glucanase from cell-free extracts of Candida utilisBiochemical Journal, 1976
- Exo-β-glucanases in yeastBiochemical Journal, 1968
- PURIFICATION OF AN EXO-BETA-D-(1-]3)-GLUCANASE FROM BASIDIOMYCETE SPECIES QM 8061968
- The Biochemistry of Laminarin and the Nature of LaminarinasePublished by Wiley ,1966
- The enzymic degradation of laminarin. 1. The distribution of laminarinase among micro-organismsBiochemical Journal, 1963
- β-D-1, 3 GLUCANASES IN FUNGICanadian Journal of Microbiology, 1959
- Notes on sugar determination.1952