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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 LU and Tenkanen, Maija (1999) In Applied Biochemistry and Biotechnology 81(2). p.81-90
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... (More)
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. (Less)
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Contribution to journal
publication status
published
subject
keywords
Adsorption, cellulose hydrolysis, cellobiohydrolase, endoglucanase, Trichoderma reesei
in
Applied Biochemistry and Biotechnology
volume
81
issue
2
pages
81 - 90
publisher
Humana Press
external identifiers
  • scopus:0001958030
ISSN
1559-0291
language
English
LU publication?
yes
id
b8b7b656-7632-4ddf-89bf-449de58192e6 (old id 125350)
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http://humanapress.com/index.php?option=com_journalshome&task=articledetails&category=journals&article_code=ABAB:81:2:81
date added to LUP
2007-07-06 09:27:46
date last changed
2017-07-02 03:38:22
@article{b8b7b656-7632-4ddf-89bf-449de58192e6,
  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.},
  author       = {Kotiranta, Pia and Karlsson, Johan and Siika-Aho, Matti and Medve, József and Viikari, Liisa and Tjerneld, Folke and Tenkanen, Maija},
  issn         = {1559-0291},
  keyword      = {Adsorption,cellulose hydrolysis,cellobiohydrolase,endoglucanase,Trichoderma reesei},
  language     = {eng},
  number       = {2},
  pages        = {81--90},
  publisher    = {Humana Press},
  series       = {Applied Biochemistry and Biotechnology},
  title        = {Adsorption and Activity of Trichoderma reesei Cellobiohydrolase I, Endoglucanase II, and the Corresponding Core Proteins on Steam Pretreated Willow},
  volume       = {81},
  year         = {1999},
}