Academic Journal

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

Bibliographic Details
Title: Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow
Authors: Kotiranta, Pia, Karlsson, Johan, Siika-aho, Matti, Medve, J., Viikari, Liisa, Tjerneld, Folke, Tenkanen, Maija
Superior Title: Kotiranta , P , Karlsson , J , Siika-aho , M , Medve , J , Viikari , L , Tjerneld , F & Tenkanen , M 1999 , ' Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow ' , Applied Biochemistry and Biotechnology , vol. 81 , no. 2 , pp. 81-90 . https://doi.org/10.1385/ABAB:81:2:81
Publication Year: 1999
Description: 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.
Document Type: article in journal/newspaper
Language: English
DOI: 10.1385/ABAB:81:2:81
Availability: https://doi.org/10.1385/ABAB:81:2:81
https://cris.vtt.fi/en/publications/59100370-f3e6-44fd-8b77-33c8a4804a01
Rights: info:eu-repo/semantics/closedAccess
Accession Number: edsbas.6F191B1E
Database: BASE
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