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)

Research output: Contribution to journalArticleScientificpeer-review

29 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 languageEnglish
Pages (from-to)81-90
Number of pages10
JournalApplied Biochemistry and Biotechnology
Volume81
Issue number2
DOIs
Publication statusPublished - 1999
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Salix
Trichoderma
Steam
Cellulose
Adsorption
Proteins
Hydrolysis
Enzymes
Cellulases
endoglucanase 2
Substrates

Cite this

Kotiranta, Pia ; Karlsson, Johan ; Siika-aho, Matti ; Medve, J. ; Viikari, Liisa ; Tjerneld, Folke ; Tenkanen, Maija. / Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow. In: Applied Biochemistry and Biotechnology. 1999 ; Vol. 81, No. 2. pp. 81-90.
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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.",
author = "Pia Kotiranta and Johan Karlsson and Matti Siika-aho and J. Medve and Liisa Viikari and Folke Tjerneld and Maija Tenkanen",
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Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II, and the corresponding core proteins on steam pretreated willow. / Kotiranta, Pia; Karlsson, Johan; Siika-aho, Matti; Medve, J.; Viikari, Liisa; Tjerneld, Folke; Tenkanen, Maija (Corresponding Author).

In: Applied Biochemistry and Biotechnology, Vol. 81, No. 2, 1999, p. 81-90.

Research output: Contribution to journalArticleScientificpeer-review

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

VL - 81

SP - 81

EP - 90

JO - Applied Biochemistry and Biotechnology

JF - Applied Biochemistry and Biotechnology

SN - 0273-2289

IS - 2

ER -