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Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis

Here, poly(2-hydroxyethyl methacrylate) (p(HEMA)) cryogel were prepared in the presence 0.48, 0.96, and 1.92 mL of α-Glucosidase enzyme (0.06 Units/mL) solutions to obtain enzyme entrapped superporous p(HEMA) cryogels, donated as α-Glucosidase@p(HEMA)-1, α-Glucosidase@p(HEMA)-2, and α-Glucosidase@p(...

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Autores principales: Demirci, Sahin, Sahiner, Mehtap, Yilmaz, Selehattin, Karadag, Erdener, Sahiner, Nurettin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7528077/
https://www.ncbi.nlm.nih.gov/pubmed/33024715
http://dx.doi.org/10.1016/j.btre.2020.e00534
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author Demirci, Sahin
Sahiner, Mehtap
Yilmaz, Selehattin
Karadag, Erdener
Sahiner, Nurettin
author_facet Demirci, Sahin
Sahiner, Mehtap
Yilmaz, Selehattin
Karadag, Erdener
Sahiner, Nurettin
author_sort Demirci, Sahin
collection PubMed
description Here, poly(2-hydroxyethyl methacrylate) (p(HEMA)) cryogel were prepared in the presence 0.48, 0.96, and 1.92 mL of α-Glucosidase enzyme (0.06 Units/mL) solutions to obtain enzyme entrapped superporous p(HEMA) cryogels, donated as α-Glucosidase@p(HEMA)-1, α-Glucosidase@p(HEMA)-2, and α-Glucosidase@p(HEMA)-3, respectively. The enzyme entrapped p(HEMA) cryogels revealed no interruption for hemolysis and coagulation of blood rendering viable biomedical application in blood contacting applications. The α-Glucosidase@p(HEMA)-1 was found to preserve its’ activity% 92.3 ± 1.4 % and higher activity% against free α-Glucosidase enzymes in 15–60℃ temperature, and 4–9 pH range. The K(m) and V(max) values of α-Glucosidase@p(HEMA)-1 cryogel was calculated as 3.22 mM, and 0.0048 mM/min, respectively versus 1.97 mM, and 0.0032 mM/min, for free enzymes. The α-Glucosidase@p(HEMA)-1 cryogel was found to maintained enzymatic activity more than 50 % after 10 consecutive uses, and also preserved their activity more than 50 % after 10 days of storage at 25 ℃, whereas free α-Glucosidase enzyme maintained only 1.9 ± 0.9 % activity under the same conditions.
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spelling pubmed-75280772020-10-05 Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis Demirci, Sahin Sahiner, Mehtap Yilmaz, Selehattin Karadag, Erdener Sahiner, Nurettin Biotechnol Rep (Amst) Research Article Here, poly(2-hydroxyethyl methacrylate) (p(HEMA)) cryogel were prepared in the presence 0.48, 0.96, and 1.92 mL of α-Glucosidase enzyme (0.06 Units/mL) solutions to obtain enzyme entrapped superporous p(HEMA) cryogels, donated as α-Glucosidase@p(HEMA)-1, α-Glucosidase@p(HEMA)-2, and α-Glucosidase@p(HEMA)-3, respectively. The enzyme entrapped p(HEMA) cryogels revealed no interruption for hemolysis and coagulation of blood rendering viable biomedical application in blood contacting applications. The α-Glucosidase@p(HEMA)-1 was found to preserve its’ activity% 92.3 ± 1.4 % and higher activity% against free α-Glucosidase enzymes in 15–60℃ temperature, and 4–9 pH range. The K(m) and V(max) values of α-Glucosidase@p(HEMA)-1 cryogel was calculated as 3.22 mM, and 0.0048 mM/min, respectively versus 1.97 mM, and 0.0032 mM/min, for free enzymes. The α-Glucosidase@p(HEMA)-1 cryogel was found to maintained enzymatic activity more than 50 % after 10 consecutive uses, and also preserved their activity more than 50 % after 10 days of storage at 25 ℃, whereas free α-Glucosidase enzyme maintained only 1.9 ± 0.9 % activity under the same conditions. Elsevier 2020-09-28 /pmc/articles/PMC7528077/ /pubmed/33024715 http://dx.doi.org/10.1016/j.btre.2020.e00534 Text en © 2020 Published by Elsevier B.V. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Demirci, Sahin
Sahiner, Mehtap
Yilmaz, Selehattin
Karadag, Erdener
Sahiner, Nurettin
Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis
title Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis
title_full Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis
title_fullStr Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis
title_full_unstemmed Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis
title_short Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis
title_sort enhanced enzymatic activity and stability by in situ entrapment of α-glucosidase within super porous p(hema) cryogels during synthesis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7528077/
https://www.ncbi.nlm.nih.gov/pubmed/33024715
http://dx.doi.org/10.1016/j.btre.2020.e00534
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