The breakdown of cellulose and its derivatives by enzymes from Myrothecium verrucaria
- 1 October 1962
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 85 (1) , 67-72
- https://doi.org/10.1042/bj0850067
Abstract
The action of cell-free filtrates from M. verrucaria and from rumen bacteria was examined on soluble carboxymethylcellulose, in soluble swollen-cellulose powder, and cotton fibers. Maximum activity of carboxymethylcellulase and cellulase was evident at 50[degree]. CarboxymethylceUulase and cellulase exhibited maximum stability between pH 5 and 7. Neither enzymic system was inactivated by digestion with pepsin or trypsin.Keywords
This publication has 10 references indexed in Scilit:
- The action of cellulolytic enzymes from Myrothecium verrucariaBiochemical Journal, 1961
- Measurement of carboxymethylcellulase activityAnalytical Biochemistry, 1960
- The N-acetylation and estimation of hexosaminesBiochemical Journal, 1959
- Substrate specificity of rumen cellulolytic enzymesBiochemical Journal, 1959
- A microdetermination of cellulose in studies with cellulaseBiochemical Journal, 1958
- Cellulolytic preparations from Micro-organisms of the Rumen and from Myrothecium verrucariaJournal of General Microbiology, 1957
- Cellulolysis by Rumen Micro-organismsJournal of General Microbiology, 1957
- Fungal Cellulases I. General Properties of Unpurified Enzyme Preparations From Aspergillus Oryz.A'eAustralian Journal of Biological Sciences, 1952
- THE BIOLOGICAL DEGRADATION OF SOLUBLE CELLULOSE DERIVATIVES AND ITS RELATIONSHIP TO THE MECHANISM OF CELLULOSE HYDROLYSISJournal of Bacteriology, 1950