The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model

Eur J Biochem. 1998 Apr 15;253(2):469-75. doi: 10.1046/j.1432-1327.1998.2530469.x.

Abstract

Introduction of a novel method for the quantification of the cellobiose released made it possible to follow the initial stage of hydrolysis of bacterial microcrystalline cellulose (BMCC) by cellobiohydrolases 1,4-beta-D-glucan-cellobiohydrolase I (CBH I) and 1,4-beta-D-glucan-cellobiohydrolase II (CBH II) from Trichoderma reesei. A drastic retardation of the rate of the hydrolysis was observed already at a very low degree of conversion. Earlier-suggested retardation factors, such as product inhibition by cellobiose or enzyme inactivation, could be discounted as primary causes for the pattern. A model including steric hindrance by non-productive binding and erosion of the cellulose surface during the processive action of exoenzymes was proposed to describe the rate retardation observed. Simultaneous action of CBH I and CBH II on cellulose was not a prerequisite for synergy between them.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding, Competitive
  • Cellulase / biosynthesis
  • Cellulase / chemistry*
  • Cellulose / chemistry
  • Cellulose 1,4-beta-Cellobiosidase
  • Computer Simulation
  • Enzyme Repression
  • Fungal Proteins / biosynthesis
  • Fungal Proteins / chemistry*
  • Hydrolysis
  • Kinetics
  • Trichoderma / enzymology*

Substances

  • Fungal Proteins
  • Cellulose
  • Cellulase
  • Cellulose 1,4-beta-Cellobiosidase