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Multienzyme Cellulose Films as Sustainable and Self-Degradable Hydrogen Peroxide-Producing Material

Califano, Davide ; Kadowaki, Marco A.S. ; Calabrese, Vincenzo ; Prade, Rolf Alexander ; Mattia, Davide ; Edler, Karen J. LU orcid ; Polikarpov, Igor and Scott, Janet L. (2020) In Biomacromolecules 21(12). p.5315-5322
Abstract
The use of hydrogen peroxide-releasing enzymes as a component to produce
alternative and sustainable antimicrobial materials has aroused
interest in the scientific community. However, the preparation of such
materials requires an effective enzyme binding method that often
involves the use of expensive and toxic chemicals. Here, we describe the
development of an enzyme-based hydrogen peroxide-producing regenerated
cellulose film (RCF) in which a cellobiohydrolase (TrCBHI) and a cellobiose dehydrogenase (MtCDHA)
were efficiently adsorbed, 90.38 ± 2.2 and 82.40 ± 5.7%, respectively,
without making use of cross-linkers. The enzyme adsorption kinetics and
binding isotherm experiments... (More)
The use of hydrogen peroxide-releasing enzymes as a component to produce
alternative and sustainable antimicrobial materials has aroused
interest in the scientific community. However, the preparation of such
materials requires an effective enzyme binding method that often
involves the use of expensive and toxic chemicals. Here, we describe the
development of an enzyme-based hydrogen peroxide-producing regenerated
cellulose film (RCF) in which a cellobiohydrolase (TrCBHI) and a cellobiose dehydrogenase (MtCDHA)
were efficiently adsorbed, 90.38 ± 2.2 and 82.40 ± 5.7%, respectively,
without making use of cross-linkers. The enzyme adsorption kinetics and
binding isotherm experiments showed high affinity of the proteins
possessing cellulose-binding modules for RCF, suggesting that binding on
regenerated cellulose via specific interactions can be an alternative
method for enzyme immobilization. Resistance to compression and porosity
at a micrometer scale were found to be tunable by changing cellulose
concentration prior to film regeneration. The self-degradation process,
triggered by stacking TrCBHI and MtCDHA (previously immobilized onto separate RCF), produced 0.15 nmol/min·cm2 of H2O2. Moreover, the production of H2O2 was sustained for at least 24 h reaching a concentration of ∼2 mM. The activity of MtCDHA
immobilized on RCF was not affected by reuse for at least 3 days (1
cycle/day), suggesting that no significant enzyme leakage occurred in
that timeframe. In the material herein designed, cellulose (regenerated
from a 1-ethyl-3-methylimidazolium acetate/dimethyl sulfoxide (DMSO)
solution) serves both as support and substrate for the immobilized
enzymes. The sequential reaction led to the production of H2O2 at a micromolar–millimolar level revealing the potential use of the material as a self-degradable antimicrobial agent. (Less)
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author
; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
Biomacromolecules
volume
21
issue
12
pages
8 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85096552483
  • pmid:33202126
ISSN
1525-7797
DOI
10.1021/acs.biomac.0c01393
language
English
LU publication?
no
additional info
Publisher Copyright: © 2020 American Chemical Society.
id
23939729-04bb-4402-a54c-e74fe961c111
date added to LUP
2022-07-12 15:56:11
date last changed
2024-07-23 20:39:59
@article{23939729-04bb-4402-a54c-e74fe961c111,
  abstract     = {{The use of hydrogen peroxide-releasing enzymes as a component to produce<br>
 alternative and sustainable antimicrobial materials has aroused <br>
interest in the scientific community. However, the preparation of such <br>
materials requires an effective enzyme binding method that often <br>
involves the use of expensive and toxic chemicals. Here, we describe the<br>
 development of an enzyme-based hydrogen peroxide-producing regenerated <br>
cellulose film (RCF) in which a cellobiohydrolase (<i>Tr</i>CBHI) and a cellobiose dehydrogenase (<i>Mt</i>CDHA)<br>
 were efficiently adsorbed, 90.38 ± 2.2 and 82.40 ± 5.7%, respectively, <br>
without making use of cross-linkers. The enzyme adsorption kinetics and <br>
binding isotherm experiments showed high affinity of the proteins <br>
possessing cellulose-binding modules for RCF, suggesting that binding on<br>
 regenerated cellulose via specific interactions can be an alternative <br>
method for enzyme immobilization. Resistance to compression and porosity<br>
 at a micrometer scale were found to be tunable by changing cellulose <br>
concentration prior to film regeneration. The self-degradation process, <br>
triggered by stacking <i>Tr</i>CBHI and <i>Mt</i>CDHA (previously immobilized onto separate RCF), produced 0.15 nmol/min·cm<sup>2</sup> of H<sub>2</sub>O<sub>2</sub>. Moreover, the production of H<sub>2</sub>O<sub>2</sub> was sustained for at least 24 h reaching a concentration of ∼2 mM. The activity of <i>Mt</i>CDHA<br>
 immobilized on RCF was not affected by reuse for at least 3 days (1 <br>
cycle/day), suggesting that no significant enzyme leakage occurred in <br>
that timeframe. In the material herein designed, cellulose (regenerated <br>
from a 1-ethyl-3-methylimidazolium acetate/dimethyl sulfoxide (DMSO) <br>
solution) serves both as support and substrate for the immobilized <br>
enzymes. The sequential reaction led to the production of H<sub>2</sub>O<sub>2</sub> at a micromolar–millimolar level revealing the potential use of the material as a self-degradable antimicrobial agent.}},
  author       = {{Califano, Davide and Kadowaki, Marco A.S. and Calabrese, Vincenzo and Prade, Rolf Alexander and Mattia, Davide and Edler, Karen J. and Polikarpov, Igor and Scott, Janet L.}},
  issn         = {{1525-7797}},
  language     = {{eng}},
  month        = {{12}},
  number       = {{12}},
  pages        = {{5315--5322}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biomacromolecules}},
  title        = {{Multienzyme Cellulose Films as Sustainable and Self-Degradable Hydrogen Peroxide-Producing Material}},
  url          = {{http://dx.doi.org/10.1021/acs.biomac.0c01393}},
  doi          = {{10.1021/acs.biomac.0c01393}},
  volume       = {{21}},
  year         = {{2020}},
}