The antimicrobial reagent role on the degradation of model cellulose film

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The antimicrobial reagent role on the degradation of model cellulose film. / Jausovec, D.; Angelescu, Daniel; Voncina, B.; Nylander, Tommy; Lindman, Björn.

I: Journal of Colloid and Interface Science, Vol. 327, Nr. 1, 2008, s. 75-83.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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T1 - The antimicrobial reagent role on the degradation of model cellulose film

AU - Jausovec, D.

AU - Angelescu, Daniel

AU - Voncina, B.

AU - Nylander, Tommy

AU - Lindman, Björn

PY - 2008

Y1 - 2008

N2 - The effect of the antimicrobial agent TMPAC (3-(trimethoxysilyl)-propyldimethyloctadecyl ammonium chloride) on the cellulase activity oil model cellulose substrate was investigated by in situ-null ellipsometry. The cellulases used were extracted from Trichoderma virlde and Aspergillus niger, and the model cellulose film was prepared by spin-coating silicon oxide wafers with cellulose solubilized in N-methylmorpholine-N-oxide/dimethyl sulfoxide solution. Upon enzyme addition to the previously equilibrated cellulose film, the initial enzyme adsorption oil the substrate was followed by an overall decrease in film mass owing to enzymatic digestion of the cellulose. The loss of cellulose film mass was associated with a non-monotonously behavior of the cellulose film thickness. The activities of the two enzymes were different, a much higher degradation rate being observed for the Trichoderma viride cellulase. The degradation rate with this cellulase decreased significantly when the cellulose film was treated with the antimicrobial agent. The antimicrobial agent did not affect the cellulose degradation catalyzed by the Aspergillus niger cellulase. It was, hence, demonstrated for the first time that, depending on the cellulase type, the antimicrobial agent can inhibit enzymatic activity at the solid-liquid interface. (C) 2008 Published by Elsevier Inc.

AB - The effect of the antimicrobial agent TMPAC (3-(trimethoxysilyl)-propyldimethyloctadecyl ammonium chloride) on the cellulase activity oil model cellulose substrate was investigated by in situ-null ellipsometry. The cellulases used were extracted from Trichoderma virlde and Aspergillus niger, and the model cellulose film was prepared by spin-coating silicon oxide wafers with cellulose solubilized in N-methylmorpholine-N-oxide/dimethyl sulfoxide solution. Upon enzyme addition to the previously equilibrated cellulose film, the initial enzyme adsorption oil the substrate was followed by an overall decrease in film mass owing to enzymatic digestion of the cellulose. The loss of cellulose film mass was associated with a non-monotonously behavior of the cellulose film thickness. The activities of the two enzymes were different, a much higher degradation rate being observed for the Trichoderma viride cellulase. The degradation rate with this cellulase decreased significantly when the cellulose film was treated with the antimicrobial agent. The antimicrobial agent did not affect the cellulose degradation catalyzed by the Aspergillus niger cellulase. It was, hence, demonstrated for the first time that, depending on the cellulase type, the antimicrobial agent can inhibit enzymatic activity at the solid-liquid interface. (C) 2008 Published by Elsevier Inc.

KW - ellipsometry

KW - enzymatic degradation

KW - antimicrobial agent

KW - model cellulose him

U2 - 10.1016/j.jcis.2008.08.002

DO - 10.1016/j.jcis.2008.08.002

M3 - Article

VL - 327

SP - 75

EP - 83

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

SN - 0021-9797

IS - 1

ER -