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

Cryogels 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 met...

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Autores principales:	Samir Abbas Ali Noma, Ömür Acet, Ahmet Ulu, Burcu Önal, Mehmet Odabaşı, Burhan Ateş
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	p(HEMA-GMA) cryogel Immobilization l-asparaginase Enzyme stability Polymers and polymer manufacture TP1080-1185
Acceso en línea:	https://doaj.org/article/b910b17c102440cfb3aaec4570119a7f
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spelling	oai:doaj.org-article:b910b17c102440cfb3aaec4570119a7f2021-11-24T04:25:38Zl-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters0142-941810.1016/j.polymertesting.2020.106980https://doaj.org/article/b910b17c102440cfb3aaec4570119a7f2021-01-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S0142941820322091https://doaj.org/toc/0142-9418Cryogels 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 (Ea) 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 (Km) of 2.04 and 1.67 mM, and the maximum reaction rates (Vmax) of 170.0 and 115.0 μM 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.Samir Abbas Ali NomaÖmür AcetAhmet UluBurcu ÖnalMehmet OdabaşıBurhan AteşElsevierarticlep(HEMA-GMA) cryogelImmobilizationl-asparaginaseEnzyme stabilityPolymers and polymer manufactureTP1080-1185ENPolymer Testing, Vol 93, Iss , Pp 106980- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	p(HEMA-GMA) cryogel Immobilization l-asparaginase Enzyme stability Polymers and polymer manufacture TP1080-1185
spellingShingle	p(HEMA-GMA) cryogel Immobilization l-asparaginase Enzyme stability Polymers and polymer manufacture TP1080-1185 Samir Abbas Ali Noma Ömür Acet Ahmet Ulu Burcu Önal Mehmet Odabaşı Burhan Ateş l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters
description	Cryogels 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 (Ea) 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 (Km) of 2.04 and 1.67 mM, and the maximum reaction rates (Vmax) of 170.0 and 115.0 μM 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.
format	article
author	Samir Abbas Ali Noma Ömür Acet Ahmet Ulu Burcu Önal Mehmet Odabaşı Burhan Ateş
author_facet	Samir Abbas Ali Noma Ömür Acet Ahmet Ulu Burcu Önal Mehmet Odabaşı Burhan Ateş
author_sort	Samir Abbas Ali Noma
title	l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters
title_short	l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters
title_full	l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters
title_fullStr	l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters
title_full_unstemmed	l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters
title_sort	l-asparaginase immobilized p(hema-gma) cryogels: a recent study for biochemical, thermodynamic and kinetic parameters
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/b910b17c102440cfb3aaec4570119a7f
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l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters

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