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Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels

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 Baci...

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Autores principales: Kappauf, Katrin, Majstorovic, Nikola, Agarwal, Seema, Rother, Dörte, Claaßen, Christiane
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9293319/
https://www.ncbi.nlm.nih.gov/pubmed/34596326
http://dx.doi.org/10.1002/cbic.202100427
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author Kappauf, Katrin
Majstorovic, Nikola
Agarwal, Seema
Rother, Dörte
Claaßen, Christiane
author_facet Kappauf, Katrin
Majstorovic, Nikola
Agarwal, Seema
Rother, Dörte
Claaßen, Christiane
author_sort Kappauf, Katrin
collection PubMed
description 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.
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spelling pubmed-92933192022-07-20 Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels Kappauf, Katrin Majstorovic, Nikola Agarwal, Seema Rother, Dörte Claaßen, Christiane Chembiochem Full Papers 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. John Wiley and Sons Inc. 2021-10-13 2021-12-10 /pmc/articles/PMC9293319/ /pubmed/34596326 http://dx.doi.org/10.1002/cbic.202100427 Text en © 2021 The Authors. ChemBioChem published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Full Papers
Kappauf, Katrin
Majstorovic, Nikola
Agarwal, Seema
Rother, Dörte
Claaßen, Christiane
Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels
title Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels
title_full Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels
title_fullStr Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels
title_full_unstemmed Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels
title_short Modulation of Transaminase Activity by Encapsulation in Temperature‐Sensitive Poly(N‐acryloyl glycinamide) Hydrogels
title_sort modulation of transaminase activity by encapsulation in temperature‐sensitive poly(n‐acryloyl glycinamide) hydrogels
topic Full Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9293319/
https://www.ncbi.nlm.nih.gov/pubmed/34596326
http://dx.doi.org/10.1002/cbic.202100427
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