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Model cellulose fil...
Model cellulose films exposed to H-insolens glucoside hydrolase family 45 endo-cellulase - the effect of the carbohydrate-binding module
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- Eriksson, Jonny (författare)
- Uppsala universitet,Institutionen för farmaci
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- Malmsten, Martin (författare)
- Uppsala universitet,Institutionen för farmaci
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- Tiberg, Fredrik (författare)
- Lund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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Callisen, T H (författare)
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Damhus, T (författare)
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Johansen, K S (författare)
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(creator_code:org_t)
- Elsevier BV, 2005
- 2005
- Engelska.
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Ingår i: Journal of Colloid and Interface Science. - : Elsevier BV. - 1095-7103 .- 0021-9797. ; 285:1, s. 94-99
- Relaterad länk:
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
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