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

Pia Kotiranta; Johan Karlsson; Matti Siika-aho; J. Medve; Liisa Viikari; Folke Tjerneld; Maija Tenkanen

doi:10.1385/ABAB:81:2:81

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

Pia Kotiranta, Johan Karlsson, Matti Siika-aho, J. Medve, Liisa Viikari, Folke Tjerneld, Maija Tenkanen (Corresponding Author)

Lund University

Research output: Contribution to journal › Article › Scientific › peer-review

32 Citations (Scopus)

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.

Original language	English
Pages (from-to)	81-90
Number of pages	10
Journal	Applied Biochemistry and Biotechnology
Volume	81
Issue number	2
DOIs	https://doi.org/10.1385/ABAB:81:2:81
Publication status	Published - 1999
MoE publication type	A1 Journal article-refereed

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

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.",

author = "Pia Kotiranta and Johan Karlsson and Matti Siika-aho and J. Medve and Liisa Viikari and Folke Tjerneld and Maija Tenkanen",

year = "1999",

doi = "10.1385/ABAB:81:2:81",

language = "English",

volume = "81",

pages = "81--90",

journal = "Applied Biochemistry and Biotechnology",

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TY - JOUR

T1 - Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow

AU - Kotiranta, Pia

AU - Karlsson, Johan

AU - Siika-aho, Matti

AU - Medve, J.

AU - Viikari, Liisa

AU - Tjerneld, Folke

AU - Tenkanen, Maija

PY - 1999

Y1 - 1999

N2 - 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.

AB - 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.

U2 - 10.1385/ABAB:81:2:81

DO - 10.1385/ABAB:81:2:81

M3 - Article

SN - 0273-2289

VL - 81

SP - 81

EP - 90

JO - Applied Biochemistry and Biotechnology

JF - Applied Biochemistry and Biotechnology

IS - 2

ER -

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

Abstract

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