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

Basit Öğe Kaydı
dc.authoridODABASI, Mehmet/0000-0002-3288-132X
dc.authoridONAL ACET, Burcu/0000-0003-2408-8660
dc.authoridAtes, Burhan/0000-0001-6080-229X
dc.authoridAcet, Omur/0000-0003-1864-5694
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.accessioned2025-03-17T12:25:57Z
dc.date.available2025-03-17T12:25:57Z
dc.date.issued2021
dc.departmentTarsus Üniversitesi
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.
dc.identifier.doi10.1016/j.polymertesting.2020.106980
dc.identifier.issn0142-9418
dc.identifier.issn1873-2348
dc.identifier.scopus2-s2.0-85097479212
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.polymertesting.2020.106980
dc.identifier.urihttps://hdl.handle.net/20.500.13099/1965
dc.identifier.volume93
dc.identifier.wosWOS:000600290200093
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier Sci Ltd
dc.relation.ispartofPolymer Testing
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WOS_20250316
dc.subjectp(HEMA-GMA) cryogel
dc.subjectImmobilization
dc.subjectL-asparaginase
dc.subjectEnzyme stability
dc.titleL-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters
dc.typeArticle

Dosyalar

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu