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A New Model For Enzymatic Hydrolysis of Cellulose Based on the Two-Domain Structure of Cellobiohydrolase I

Bio/Technology volume 9, pages 286–290 (1991)Cite this article

Abstract

We have studied the kinetics of adsorption to macrocrystalline cellulose (Avicel) and its hydrolysis by intact and isolated domains of Trichoderma reesei cellobiohydrolase I (CBH I). The catalytic domain (the core) shows lower adsorption and activity than the complete enzyme, the effect being more pronounced the lower the enzyme concentration and the higher the extent of degradation. Apparent dissociation constants were derived from adsorption isotherms through non-linear regression analysis using a two-site model. Total binding capacities were estimated to be 1.1, 0.17 and 6.0 μmol protein/g Avicel (69, 9.3 and 53 mg/g) for intact enzyme, core and binding domain, respectively. The structural characteristics of cellulose that influence enzyme adsorption are discussed and a model is developed for the action of two-domain cellulases. This model may be applicable to other enzymes such as cutinases and amylases, which also have separate catalytic and binding domains and act on insoluble polymeric substrates.

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Author notes

  1. Göran Pettersson: Corresponding author.

Authors and Affiliations

  1. Department of Biochemistry, Biomedical Centre, University of Uppsala, P.O. Box 576, S-751 23, Uppsala, Sweden

    Jerry Ståhlberg, Gunnar Johansson & Göran Pettersson

Authors
  1. Jerry Ståhlberg
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  2. Gunnar Johansson
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  3. Göran Pettersson
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Ståhlberg, J., Johansson, G. & Pettersson, G. A New Model For Enzymatic Hydrolysis of Cellulose Based on the Two-Domain Structure of Cellobiohydrolase I. Nat Biotechnol 9, 286–290 (1991). https://doi.org/10.1038/nbt0391-286

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