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Sökning: WFRF:(Callisen T H)

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1.
  • Eriksson, Jonny, et al. (författare)
  • Enzymatic degradation of model cellulose films
  • 2005
  • Ingår i: Journal of Colloid and Interface Science. - : Elsevier BV. - 1095-7103 .- 0021-9797. ; 284:1, s. 99-106
  • Tidskriftsartikel (refereegranskat)abstract
    • Enzymatic degradation of model cellulose films prepared by a spin-coating technique was investigated by ellipsometry. The cellulose films were prior to degradation characterized by ellipsometry, contact angle measurements, ESCA (electron spectroscopy for chemical analysis) and AFM (atomic force microscopy). At enzyme addition to preformed cellulose films an initial adsorption was observed, which was followed by a total interfacial mass decrease due to enzymatic degradation of the cellulose films. The degradation rate was found to be constant during an extended time of hours, whereafter the degradation leveled off. In parallel to the decreased interfacial mass, the cellulose degradation resulted in a thinner and more dilute interfacial film. At long degradation times, however, there was an expansion of the cellulose film. The enzyme concentration affected the degradation rate significantly, with a faster degradation at a higher enzyme concentration. The effects of pH, temperature, ionic strength and stirring rate in the cuvette were also investigated. (c) 2004 Elsevier Inc. All rights reserved.
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2.
  • Eriksson, Jonny, et al. (författare)
  • Model cellulose films exposed to H-insolens glucoside hydrolase family 45 endo-cellulase - the effect of the carbohydrate-binding module
  • 2005
  • Ingår i: Journal of Colloid and Interface Science. - : Elsevier BV. - 1095-7103 .- 0021-9797. ; 285:1, s. 94-99
  • Tidskriftsartikel (refereegranskat)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.
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  • Resultat 1-3 av 3

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