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Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow

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Abstract

The adsorption and the hydrolytic action of purified cellulases of Trichoderma reesei, namely, cellobiohydrolase I (CBH I), endoglucanase II (EG II), and their core proteins, on steam-pretreated willow were compared. The two enzymes differed clearly in their adsorption and hydrolytic behavior. CBH I required the cellulose-binding domain (CBD) for efficient adsorption and hydrolysis, whereas EG II was able to adsorb to steam pretreated willow without its CBD. Absence of the CBD decreased the hydrolysis of cellulose by EG II, but the decrease was less pronounced than with CBH I. A linear relationship was observed between the amount of enzyme adsorbed and the degree of hydrolysis of cellulose only for CBHI. EG II and EG II core appeared to be able to hydrolyze only 1 to 2% of the substrate regardless of the amount of protein adsorbed.

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Authors and Affiliations

  1. VTT Biotechnology and Food Research, P.O. Box 1501, 02044, VTT, Finland

    Pia Kotiranta, Matti Siika-aho, Liisa Viikari & Maija Tenkanen

  2. Lund University, P.O. Box 124, S-221 00, Lund, Sweden

    Johan Karlsson, József Medve & Folke Tjerneld

Authors
  1. Pia Kotiranta
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  2. Johan Karlsson
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  3. Matti Siika-aho
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  4. József Medve
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  5. Liisa Viikari
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  6. Folke Tjerneld
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  7. Maija Tenkanen
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Correspondence to Maija Tenkanen.

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Kotiranta, P., Karlsson, J., Siika-aho, M. et al. Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow. Appl Biochem Biotechnol 81, 81–90 (1999). https://doi.org/10.1385/ABAB:81:2:81

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  • DOI: https://doi.org/10.1385/ABAB:81:2:81

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