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Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin

Palonen, H; Tjerneld, Folke LU ; Zacchi, Guido LU and Tenkanen, M (2004) In Journal of Biotechnology 107(1). p.65-72
Abstract
The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG Il or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG 11 also bound to... (More)
The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG Il or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG 11 also bound to isolated lignin. Surprisingly, the catalytic domains of the two enzymes of T reesei differed essentially in the adsorption to isolated lignin. The catalytic domain of EG II was able to adsorb to alkaline isolated lignin with a high affinity, whereas the catalytic domain of CBH I did not adsorb to any of the lignins, tested. The results indicate that the cellulose binding domain has a significant role in the unspecific binding of cellulases to lignin. (C) 2003 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
lignocellulose, lignin, adsorption, Trichoderma reesei, cellulase
in
Journal of Biotechnology
volume
107
issue
1
pages
65 - 72
publisher
Elsevier
external identifiers
  • pmid:14687972
  • wos:000187912200006
  • scopus:0346363683
ISSN
1873-4863
DOI
10.1016/j.jbiotec.2003.09.011
language
English
LU publication?
yes
id
2806caad-d9af-4a0d-990f-e17bc20d4079 (old id 120892)
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http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T3C-4B429PY-1-G&_cdi=4943&_orig=search&_coverDate=01%2F08%2F2004&_qd=1&_sk=998929998&view=c&wchp=dGLbVzb-zSkWW&_acct=C000041498&_version=1&_userid=745831&md5=9f49d9e73a1c5156b5dbaf012687231c&ie=f.p
date added to LUP
2007-06-25 14:39:31
date last changed
2017-12-10 03:55:37
@article{2806caad-d9af-4a0d-990f-e17bc20d4079,
  abstract     = {The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG Il or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG 11 also bound to isolated lignin. Surprisingly, the catalytic domains of the two enzymes of T reesei differed essentially in the adsorption to isolated lignin. The catalytic domain of EG II was able to adsorb to alkaline isolated lignin with a high affinity, whereas the catalytic domain of CBH I did not adsorb to any of the lignins, tested. The results indicate that the cellulose binding domain has a significant role in the unspecific binding of cellulases to lignin. (C) 2003 Elsevier B.V. All rights reserved.},
  author       = {Palonen, H and Tjerneld, Folke and Zacchi, Guido and Tenkanen, M},
  issn         = {1873-4863},
  keyword      = {lignocellulose,lignin,adsorption,Trichoderma reesei,cellulase},
  language     = {eng},
  number       = {1},
  pages        = {65--72},
  publisher    = {Elsevier},
  series       = {Journal of Biotechnology},
  title        = {Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin},
  url          = {http://dx.doi.org/10.1016/j.jbiotec.2003.09.011},
  volume       = {107},
  year         = {2004},
}