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@ARTICLE{Kappauf:901843,
author = {Kappauf, Katrin and Majstorovic, Nikola and Agarwal, Seema
and Rother, Dörte and Claaßen, Christiane},
title = {{M}odulation of transaminase activity by encapsulation in
temperature‐sensitive poly({N}‐acryloyl glycinamide)
hydrogels},
journal = {ChemBioChem},
volume = {22},
number = {24},
issn = {1439-7633},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {FZJ-2021-03862},
pages = {3452-3461},
year = {2021},
abstract = {Smart hydrogels hold much potential for biocatalysis, not
only for the immobilization of enzymes, but also for the
control of enzyme activity. We investigated upper critical
solution temperature-type poly N-acryloyl glycinamide
(pNAGA) hydrogels as a smart matrix for the amine
transaminase from Bacillus megaterium (BmTA). Physical
entrapment of BmTA in pNAGA hydrogels results in high
immobilization efficiency $(>89 \%)$ and high activity
$(97 \%).$ The temperature-sensitiveness of pNAGA is
preserved upon immobilization of BmTA and shows a gradual
deswelling upon temperature reduction. While enzyme activity
is mainly controlled by temperature, deactivation tended to
be higher for immobilized BmTA $(≈62–68 \%)$ than for
free BmTA $(≈44 \%),$ suggesting a deactivating effect
due to deswelling of the pNAGA gel. Although the
deactivation in response to hydrogel deswelling is not yet
suitable for controlling enzyme activity sufficiently, it is
nevertheless a good starting point for further
optimization.},
cin = {IBG-1},
ddc = {540},
cid = {I:(DE-Juel1)IBG-1-20101118},
pnm = {2172 - Utilization of renewable carbon and energy sources
and engineering of ecosystem functions (POF4-217)},
pid = {G:(DE-HGF)POF4-2172},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:34596326},
UT = {WOS:000706751900001},
doi = {10.1002/cbic.202100427},
url = {https://juser.fz-juelich.de/record/901843},
}