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

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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, József; Viikari, Liisa; Tjerneld, Folke; Tenkanen, Maija.

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

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Kotiranta, Pia ; Karlsson, Johan ; Siika-Aho, Matti ; Medve, József ; 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.

RIS

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, József

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 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.

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 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.

KW - Adsorption

KW - cellulose hydrolysis

KW - cellobiohydrolase

KW - endoglucanase

KW - Trichoderma reesei

M3 - Article

VL - 81

SP - 81

EP - 90

JO - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

T2 - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

JF - Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

SN - 1559-0291

IS - 2

ER -