Characteristics of Enzymes Produced by Ruminococcus flavefaciens which Degrade Plant Cell Walls
Open Access
- 1 January 1979
- journal article
- research article
- Published by Microbiology Society in Journal of General Microbiology
- Vol. 110 (1), 21-27
- https://doi.org/10.1099/00221287-110-1-21
Abstract
Summary: Enzyme preparations active against crystalline cellulose, marble-milled filter paper, carboxymethyicellulose (CM-cellulose), hemicellulose and xylan were obtained from cultures of Ruminococcus flavefaciens. These preparations also contained swelling factor, pectin methylesterase, pectin lyase and low levels of aryl β-glucosidase and aryl β-xylosidase. CM-cellulase and xylanase activities were present in a high molecular weight complex, but substrate competition studies showed that different active sites were probably responsible for each activity. Analysis of products and viscosity changes during enzymic hydrolysis of CM-cellulose and xylan indicated that the most active enzymes were of the exo-1, 4-β-glycosidase type. A variety of reducing sugars were released from cell walls of Lolium perenne (perennial ryegrass) by enzyme preparations.This publication has 7 references indexed in Scilit:
- The cellulase of Trichoderma koningii. Purification and properties of some endoglucanase components with special reference to their action on cellulose when acting alone and in synergism with the cellobiohydrolaseBiochemical Journal, 1978
- Ruminococcus flavefaciens Cell Coat and Adhesion to Cotton Cellulose and to Cell Walls in Leaves of Perennial Ryegrass (Lolium perenne)Applied and Environmental Microbiology, 1978
- The gel-filtration behaviour of proteins related to their molecular weights over a wide rangeBiochemical Journal, 1965
- Statistical estimations in enzyme kineticsBiochemical Journal, 1961
- The action of cellulolytic enzymes from Myrothecium verrucariaBiochemical Journal, 1961
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- THE BIOLOGICAL DEGRADATION OF SOLUBLE CELLULOSE DERIVATIVES AND ITS RELATIONSHIP TO THE MECHANISM OF CELLULOSE HYDROLYSISJournal of Bacteriology, 1950