Model cellulose films exposed to H-insolens glucoside hydrolase family 45 endo-cellulase - the effect of the carbohydrate-binding module
(2005) In Journal of Colloid and Interface Science 285(1). p.94-99- Abstract
- The effects of enzyme structure and activity on the degradation of model cellulose substrates were investigated by ellipsometry for the cellulase Humicola insolens GH45. The inactive variant D10N was found to adsorb at the cellulose surface but also to be incorporated into the cellulose films to an extent that depended on pH. For the native protein, the initial adsorption monitored for the inactive variant D10N was followed by enzyme-mediated degradation of the cellulose films. Again, a dependence on pH was found, such that higher pH resulted in slower enzymatic degradation. Removing the carbohydrate-binding module eliminated this pH dependence but also resulted in a decreased adsorption to the cellulose surface, and in a decreased net... (More)
- The effects of enzyme structure and activity on the degradation of model cellulose substrates were investigated by ellipsometry for the cellulase Humicola insolens GH45. The inactive variant D10N was found to adsorb at the cellulose surface but also to be incorporated into the cellulose films to an extent that depended on pH. For the native protein, the initial adsorption monitored for the inactive variant D10N was followed by enzyme-mediated degradation of the cellulose films. Again, a dependence on pH was found, such that higher pH resulted in slower enzymatic degradation. Removing the carbohydrate-binding module eliminated this pH dependence but also resulted in a decreased adsorption to the cellulose surface, and in a decreased net catalytic effect. (c) 2004 Elsevier Inc. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/157372
- author
- Eriksson, Jonny ; Malmsten, M ; Tiberg, Fredrik LU ; Callisen, T H ; Damhus, T and Johansen, K S
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Colloid and Interface Science
- volume
- 285
- issue
- 1
- pages
- 94 - 99
- publisher
- Elsevier
- external identifiers
-
- wos:000228434800014
- pmid:15797401
- scopus:25444435724
- ISSN
- 1095-7103
- DOI
- 10.1016/j.jcis.2004.10.042
- language
- English
- LU publication?
- yes
- id
- 3e1cf092-193e-46d4-8c17-9ba7371b181d (old id 157372)
- date added to LUP
- 2016-04-01 12:34:29
- date last changed
- 2022-03-29 02:41:09
@article{3e1cf092-193e-46d4-8c17-9ba7371b181d,
abstract = {{The effects of enzyme structure and activity on the degradation of model cellulose substrates were investigated by ellipsometry for the cellulase Humicola insolens GH45. The inactive variant D10N was found to adsorb at the cellulose surface but also to be incorporated into the cellulose films to an extent that depended on pH. For the native protein, the initial adsorption monitored for the inactive variant D10N was followed by enzyme-mediated degradation of the cellulose films. Again, a dependence on pH was found, such that higher pH resulted in slower enzymatic degradation. Removing the carbohydrate-binding module eliminated this pH dependence but also resulted in a decreased adsorption to the cellulose surface, and in a decreased net catalytic effect. (c) 2004 Elsevier Inc. All rights reserved.}},
author = {{Eriksson, Jonny and Malmsten, M and Tiberg, Fredrik and Callisen, T H and Damhus, T and Johansen, K S}},
issn = {{1095-7103}},
language = {{eng}},
number = {{1}},
pages = {{94--99}},
publisher = {{Elsevier}},
series = {{Journal of Colloid and Interface Science}},
title = {{Model cellulose films exposed to H-insolens glucoside hydrolase family 45 endo-cellulase - the effect of the carbohydrate-binding module}},
url = {{http://dx.doi.org/10.1016/j.jcis.2004.10.042}},
doi = {{10.1016/j.jcis.2004.10.042}},
volume = {{285}},
year = {{2005}},
}