Enhanced enzymatic activity and stability by in situ entrapment of α Glucosidase within super porous p(HEMA) cryogels during synthesis
dc.authorid | Demirci, Şahin / 0000-0001-7083-1481 | |
dc.authorid | Şahiner, Mehtap / 0000-0001-8666-7954 | |
dc.authorid | Yılmaz, Selehattin / 0000-0003-4607-3523 | |
dc.authorid | Şahiner, Nurettin / 0000-0003-0120-530X | |
dc.contributor.author | Demirci, Şahin | |
dc.contributor.author | Şahiner, Mehtap | |
dc.contributor.author | Yılmaz, Selehattin | |
dc.contributor.author | Karadağ, Erdener | |
dc.contributor.author | Şahiner, Nurettin | |
dc.date.accessioned | 2025-01-27T18:53:24Z | |
dc.date.available | 2025-01-27T18:53:24Z | |
dc.date.issued | 2020 | |
dc.department | Çanakkale Onsekiz Mart Üniversitesi | |
dc.description.abstract | 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 Km and Vmax 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. | |
dc.description.sponsorship | Council of Higher Education System, (YOK-100/2000) | |
dc.identifier.doi | 10.1016/j.btre.2020.e00534 | |
dc.identifier.issn | 2215-017X | |
dc.identifier.scopus | 2-s2.0-85091638865 | |
dc.identifier.scopusquality | Q1 | |
dc.identifier.uri | https://doi.org/10.1016/j.btre.2020.e00534 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12428/12706 | |
dc.identifier.volume | 28 | |
dc.indekslendigikaynak | Scopus | |
dc.language.iso | en | |
dc.publisher | Elsevier B.V. | |
dc.relation.ispartof | Biotechnology Reports | |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.snmz | KA_Scopus_20250125 | |
dc.subject | Enzymatic reaction; Enzyme; Enzyme immobilization/entrapment; Super porous cryogel; ?-Glucosidase | |
dc.title | Enhanced enzymatic activity and stability by in situ entrapment of α Glucosidase within super porous p(HEMA) cryogels during synthesis | |
dc.type | Article |
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