Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/120892
- author
- Palonen, H ; Tjerneld, Folke LU ; Zacchi, Guido LU and Tenkanen, M
- organization
- publishing date
- 2004
- 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)
- alternative location
- 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
- 2016-04-01 12:34:49
- date last changed
- 2023-11-26 18:39:56
@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}}, keywords = {{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}}, doi = {{10.1016/j.jbiotec.2003.09.011}}, volume = {{107}}, year = {{2004}}, }