The antimicrobial reagent role on the degradation of model cellulose film
(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:
https://lup.lub.lu.se/record/1285749
- author
- Jausovec, D. ; Angelescu, Daniel LU ; Voncina, B. ; Nylander, Tommy LU and Lindman, Björn LU
- organization
- publishing date
- 2008
- 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
- 2016-04-01 12:23:31
- date last changed
- 2022-01-27 03:05:25
@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}},
keywords = {{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}},
doi = {{10.1016/j.jcis.2008.08.002}},
volume = {{327}},
year = {{2008}},
}