Adsorption and Activity of Trichoderma reesei Cellobiohydrolase I, Endoglucanase II, and the Corresponding Core Proteins on Steam Pretreated Willow

Research output: Contribution to journalArticle

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 CBH I. 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.

Details

Authors
  • Pia Kotiranta
  • Johan Karlsson
  • Matti Siika-Aho
  • József Medve
  • Liisa Viikari
  • Folke Tjerneld
  • Maija Tenkanen
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biochemistry and Molecular Biology

Keywords

  • Adsorption, cellulose hydrolysis, cellobiohydrolase, endoglucanase, Trichoderma reesei
Original languageEnglish
Pages (from-to)81-90
JournalApplied Biochemistry and Biotechnology
Volume81
Issue number2
Publication statusPublished - 1999
Publication categoryResearch
Peer-reviewedYes