Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis.
Enzymatic reaction
Enzyme
Enzyme immobilization/entrapment
Super porous cryogel
α-Glucosidase
Journal
Biotechnology reports (Amsterdam, Netherlands)
ISSN: 2215-017X
Titre abrégé: Biotechnol Rep (Amst)
Pays: Netherlands
ID NLM: 101637426
Informations de publication
Date de publication:
Dec 2020
Dec 2020
Historique:
received:
08
07
2020
revised:
08
08
2020
accepted:
25
09
2020
entrez:
7
10
2020
pubmed:
8
10
2020
medline:
8
10
2020
Statut:
epublish
Résumé
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
Identifiants
pubmed: 33024715
doi: 10.1016/j.btre.2020.e00534
pii: S2215-017X(20)30591-9
pmc: PMC7528077
doi:
Types de publication
Journal Article
Langues
eng
Pagination
e00534Informations de copyright
© 2020 Published by Elsevier B.V.
Déclaration de conflit d'intérêts
The authors report no declarations of interest.
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