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Digestion of pretreated aspen substrates.

Authors :
Tatsumoto, K.
Baker, J.
Tucker, M.
Oh, K.
Mohagheghi, A.
Grohmann, K.
Hlmmel, M.
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