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The antimicrobial reagent role on the degradation of model cellulose film

Jausovec, D.; Angelescu, Daniel LU ; Voncina, B.; Nylander, Tommy LU and Lindman, Björn LU (2008) In Journal of Colloid and Interface Science 327(1). p.75-83
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
ellipsometry, enzymatic degradation, antimicrobial agent, model cellulose him
in
Journal of Colloid and Interface Science
volume
327
issue
1
pages
75 - 83
publisher
Elsevier
external identifiers
  • wos:000259789300011
  • scopus:52049127238
ISSN
1095-7103
DOI
10.1016/j.jcis.2008.08.002
language
English
LU publication?
yes
id
6249c517-c4b6-44f7-8e78-1a77c27753a0 (old id 1285749)
date added to LUP
2009-02-06 09:16:56
date last changed
2017-09-24 03:44:05
@article{6249c517-c4b6-44f7-8e78-1a77c27753a0,
  abstract     = {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.},
  author       = {Jausovec, D. and Angelescu, Daniel and Voncina, B. and Nylander, Tommy and Lindman, Björn},
  issn         = {1095-7103},
  keyword      = {ellipsometry,enzymatic degradation,antimicrobial agent,model cellulose him},
  language     = {eng},
  number       = {1},
  pages        = {75--83},
  publisher    = {Elsevier},
  series       = {Journal of Colloid and Interface Science},
  title        = {The antimicrobial reagent role on the degradation of model cellulose film},
  url          = {http://dx.doi.org/10.1016/j.jcis.2008.08.002},
  volume       = {327},
  year         = {2008},
}