Applied Biochemistry and Biotechnology

, Volume 18, Issue 1, pp 159–174

Digestion of pretreated aspen substrates

Hydrolysis rates and adsorptive loss of cellulase enzymes
  • K. Tatsumoto
  • J. O. Baker
  • M. P. Tucker
  • K. K. Oh
  • A. Mohagheghi
  • K. Grohmann
  • M. E. Hlmmel
Session 3-Original Papers
  • 55 Downloads

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.

Index Entries

Cellulase adsorption aspen lignin beta-glucosidase 

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Copyright information

© Humana Press Inc. 1988

Authors and Affiliations

  • K. Tatsumoto
    • 1
  • J. O. Baker
    • 1
  • M. P. Tucker
    • 1
  • K. K. Oh
    • 1
  • A. Mohagheghi
    • 1
  • K. Grohmann
    • 1
  • M. E. Hlmmel
    • 1
  1. 1.Fermentation Section, Biotechnology Research Branch, Solar Fuels Research DivisionSolar Energy Research InstituteGolden

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