L-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters

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dc.authoridAteş, Burhan/0000-0001-6080-229X
dc.authoridUlu, Ahmet/0000-0002-4447-6233
dc.authoridODABASI, Mehmet/0000-0002-3288-132X
dc.authoridAcet, Omur/0000-0003-1864-5694
dc.authoridONAL ACET, Burcu/0000-0003-2408-8660
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidAcet, Ömür/IUN-5176-2023
dc.authorwosidNOMA, SAMIR/ABH-1773-2021
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.authorwosidAcet, Ömür/ABI-5085-2020
dc.contributor.authorNoma, Samir Abbas Ali
dc.contributor.authorAcet, Omur
dc.contributor.authorUlu, Ahmet
dc.contributor.authorOnal, Burcu
dc.contributor.authorOdabasi, Mehmet
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:49:07Z
dc.date.available2024-08-04T20:49:07Z
dc.date.issued2021
dc.departmentİnönü Üniversitesien_US
dc.description.abstractCryogels have recently been attracted intense attention as suitable carriers for enzyme immobilization. Herein, L-asparaginase was selected as the model enzyme due to its application such as pharmaceutical and food. Under optimum conditions, L-asparaginase was immobilized on poly (2-hydroxyethyl methacrylate-glycidyl methacrylate) cryogels with 68.8% of immobilization yield and 69.3% of activity recovery. The immobilized enzyme exhibited improved stability with respect to the soluble enzyme at extreme conditions, especially around acidic pH and high temperature. Also, the storage stability and reusability of the immobilized enzyme were found to be approximately 54% and 52% of the original activity after 28 days at room temperature and 10 cycles, respectively. The thermodynamic studies indicated that activation energy (E-a) of the free enzyme decreased from 13.08 to 10.97 kJ/mol, which means an increase in the thermostability of L-asparaginase. The Michaelis-Menten constants (K-m) of 2.04 and 1.67 mM, and the maximum reaction rates (V-max) of 170.0 and 115.0 mu M min(-1) were estimated for soluble and immobilized L-asparaginase, respectively. These findings demonstrated that the designed cryogels turn out to be a good carrier matrix for L-asparaginase immobilization with high catalytic efficiency and enhanced stability.en_US
dc.identifier.doi10.1016/j.polymertesting.2020.106980
dc.identifier.issn0142-9418
dc.identifier.issn1873-2348
dc.identifier.scopus2-s2.0-85097479212en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1016/j.polymertesting.2020.106980
dc.identifier.urihttps://hdl.handle.net/11616/99667
dc.identifier.volume93en_US
dc.identifier.wosWOS:000600290200093en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevier Sci Ltden_US
dc.relation.ispartofPolymer Testingen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectp(HEMA-GMA) cryogelen_US
dc.subjectImmobilizationen_US
dc.subjectL-asparaginaseen_US
dc.subjectEnzyme stabilityen_US
dc.titleL-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parametersen_US
dc.typeArticleen_US

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