Superporous neutral, anionic, and cationic cryogel reactors to improved enzymatic activity and stability of ?-Glucosidase enzyme via entrapment method

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dc.authorid0000-0001-7083-1481en_US
dc.authorid0000-0003-0120-530Xen_US
dc.authorscopusid56026625600en_US
dc.authorscopusid6602001525en_US
dc.authorwosidHQZ-4087-2023en_US
dc.authorwosidKVP-4764-2024en_US
dc.contributor.authorDemirci, Şahin
dc.contributor.authorŞahiner, Nurettin
dc.date.accessioned2024-12-23T11:37:43Z
dc.date.available2024-12-23T11:37:43Z
dc.date.issued2021en_US
dc.departmentFakülteler, Fen Fakültesi, Kimya Bölümü
dc.departmentRektörlük, Rektörlüğe Bağlı Bölümler, Nanobilim ve Teknoloji Araştırma ve Uygulama Merkezi
dc.description.abstractAlthough enzymes are unique catalysts with highest selectivity for desired products, their cost, poor stability, and delicate reaction condition are the main drawbacks. To circumvent these obstacles and render viable enzymatic reactions with increased durability and stability, enzymes are generally immobilized in very different substrates. Therefore, herein, α-Glucosidase from Saccharomyces cerevisiae (α-Glu) as a model enzyme was entrapped within neutral, anionic and cationic synthetic cryogels such as poly(Acrylamide) (α-Glu@p(AAm)), poly(2‐acrylamido‐2‐methyl‐1‐propane sulfonic acid) (α-Glu@p(AMPS)), and poly(3‐acrylamidopropyltrimethyl ammonium chloride) (α-Glu@p(APTMACl)) during the synthesis process. The prepared α-Glu@p(AAm), α-Glu@p(AMPS), and α-Glu@p(APTMACl) cryogels were used as reactor and found to main their enzymatic activity of 80.9 ± 3.5, 61.5 ± 2.2, and 50.9 ± 3.1% with respect to free enzyme at its’ optimum conditions, pH 6.8 and 37 °C, respectively. Interestingly, at harsher pH conditions, it was fond that α-Glu@p(AMPS) cryogels showed 100% activity at pH 8.0, and α-Glu@p(APTMACl) cryogels showed 100% activity at pH 5.0, whereas free α-Glu almost lost its catalytic activity completely at the same pHs. The operational and storage stability studies revealed that the entrapment of α-Glu within cryogels led to much better operational and storage stability than free α-Glu enzyme e.g., more than 50% activity after 10th usage and 10-day storage time at room temperature while almost no activity is attained for free enzyme. The kinetic parameters such as Km and Vmax of α-Glu@cryogel were also calculated by using Lineweaver-Burk plotting method and compared each other and free α-Glu enzyme.en_US
dc.identifier.citationDemirci, S., & Şahiner, N. (2021). Superporous neutral, anionic, and cationic cryogel reactors to improved enzymatic activity and stability of α-Glucosidase enzyme via entrapment method. Chemical Engineering Journal, 409, 128233. https://doi.org/10.1016/j.cej.2020.128233en_US
dc.identifier.doi10.1016/j.cej.2020.128233
dc.identifier.issn1385-8947
dc.identifier.issn1873-3212
dc.identifier.scopus2-s2.0-85098523046
dc.identifier.urihttps://doi.org/10.1016/j.cej.2020.128233
dc.identifier.urihttps://hdl.handle.net/20.500.12428/6777
dc.identifier.volume409en_US
dc.identifier.wosWOS:000618081200002
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.institutionauthorDemirci, Şahin
dc.institutionauthorŞahiner, Nurettin
dc.language.isoen
dc.publisherElsevier B.V.en_US
dc.relation.ispartofChemical Engineering Journalen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBiotechnologyen_US
dc.subjectCryogel reactoren_US
dc.subjectEntrapmenten_US
dc.subjectEnzymeen_US
dc.subjectSuperporous enzyme reactoren_US
dc.subjectα-Glucosidaseen_US
dc.titleSuperporous neutral, anionic, and cationic cryogel reactors to improved enzymatic activity and stability of ?-Glucosidase enzyme via entrapment method
dc.typeArticle

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