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Digestion of pretreated aspen substrates.
- Source :
- Applied Biochemistry & Biotechnology; 1988, Vol. 18 Issue 1, p159-174, 16p
- Publication Year :
- 1988
-
Abstract
- Considerable controversy exists concerning the role lignin plays in the adsorption of cellulase enzymes on biomass. Recent studies using extracted, purified hardwood lignin have shown these materials have a propensity for cellulase adsorption; however, native lignin is carbohydrate-linked and far less condensed. In this study, we report the results of adsorption-kinetics analyses of cellulase-complex activities using five pretreated aspen substrates, including an exhaustively enzyme-hydrolyzed one. These data indicate that the polymer-binding cellulase activities are removed from solution at higher rates and extents in the presence of low lignin-content versus high lignin-content substrates. This order of adsorption was found to be essentially the inverse for beta-glucosidase adsorption. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 02732289
- Volume :
- 18
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Applied Biochemistry & Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 73024942
- Full Text :
- https://doi.org/10.1007/BF02930823