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Model cellulose films exposed to H. insolens glucoside hydrolase family 45 endo-cellulase—the effect of the carbohydrate-binding module
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, YKI – Ytkemiska institutet.
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2005 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 285, p. 94-99Article in journal (Refereed)
Abstract [en]

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

Place, publisher, year, edition, pages
2005. Vol. 285, p. 94-99
Keywords [en]
Ellipsometry, cellulose model surface, spin coating, adsorption, cellulase, enzymatic degradation
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-26679OAI: oai:DiVA.org:ri-26679DiVA, id: diva2:1053682
Note
A1752Available from: 2016-12-08 Created: 2016-12-08 Last updated: 2020-12-01Bibliographically approved

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