Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion process

Penicillin G acylase plays an important role in the biocatalytic process of semi-synthetic penicillin. In order to overcome the disadvantages of free enzymes and improve the catalytic performance of enzymes, it is a new method to immobilize enzymes on carrier materials. And magnetic materials have t...

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Autori principali: Mingyi Ma, Xiu Chen, Yao Yue, Jie Wang, Dawei He, Ruijiang Liu
Natura: Articolo
Lingua:English
Pubblicazione: Frontiers Media S.A. 2023-03-01
Serie:Frontiers in Bioengineering and Biotechnology
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Accesso online:https://www.frontiersin.org/articles/10.3389/fbioe.2023.1108820/full
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author Mingyi Ma
Xiu Chen
Yao Yue
Jie Wang
Dawei He
Ruijiang Liu
author_facet Mingyi Ma
Xiu Chen
Yao Yue
Jie Wang
Dawei He
Ruijiang Liu
author_sort Mingyi Ma
collection DOAJ
description Penicillin G acylase plays an important role in the biocatalytic process of semi-synthetic penicillin. In order to overcome the disadvantages of free enzymes and improve the catalytic performance of enzymes, it is a new method to immobilize enzymes on carrier materials. And magnetic materials have the characteristics of easy separation. In the present study, the Magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles were successfully prepared by a rapid-combustion method and calcined at 400°C for 2 h. The surface of the nanoparticles was modified with sodium silicate hydrate, and the PGA was covalently bound to the carrier particles through the cross-linking of glutaraldehyde. The results showed that the activity of immobilized PGA reached 7121.00 U/g. The optimum pH for immobilized PGA was 8 and the optimum temperature was 45°C, the immobilized PGA exhibited higher stability against changes in pH and temperature. The Michaelis–Menten constant (Km) values of the free and immobilized PGA were 0.00387 and 0.0101 mol/L and the maximum rate (Vmax) values were 0.387 and 0.129 μmol/min. Besides, the immobilized PGA revealed excellent cycling performance. The immobilization strategy presented PGA had the advantages of reuse, good stability, cost saving and had considerable practical significance for the commercial application of PGA.
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spelling doaj.art-e76c99edb47c4b51b1f7dee599bb15cd2023-03-13T05:21:16ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852023-03-011110.3389/fbioe.2023.11088201108820Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion processMingyi Ma0Xiu Chen1Yao Yue2Jie Wang3Dawei He4Ruijiang Liu5School of Pharmacy, Jiangsu University, Zhenjiang, ChinaThe People’s Hospital of Danyang, Affiliated Danyang Hospital of Nantong University, Zhenjiang, ChinaSchool of Pharmacy, Jiangsu University, Zhenjiang, ChinaSchool of Pharmacy, Jiangsu University, Zhenjiang, ChinaAffiliated Kunshan Hospital, Jiangsu University, Suzhou, ChinaSchool of Pharmacy, Jiangsu University, Zhenjiang, ChinaPenicillin G acylase plays an important role in the biocatalytic process of semi-synthetic penicillin. In order to overcome the disadvantages of free enzymes and improve the catalytic performance of enzymes, it is a new method to immobilize enzymes on carrier materials. And magnetic materials have the characteristics of easy separation. In the present study, the Magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles were successfully prepared by a rapid-combustion method and calcined at 400°C for 2 h. The surface of the nanoparticles was modified with sodium silicate hydrate, and the PGA was covalently bound to the carrier particles through the cross-linking of glutaraldehyde. The results showed that the activity of immobilized PGA reached 7121.00 U/g. The optimum pH for immobilized PGA was 8 and the optimum temperature was 45°C, the immobilized PGA exhibited higher stability against changes in pH and temperature. The Michaelis–Menten constant (Km) values of the free and immobilized PGA were 0.00387 and 0.0101 mol/L and the maximum rate (Vmax) values were 0.387 and 0.129 μmol/min. Besides, the immobilized PGA revealed excellent cycling performance. The immobilization strategy presented PGA had the advantages of reuse, good stability, cost saving and had considerable practical significance for the commercial application of PGA.https://www.frontiersin.org/articles/10.3389/fbioe.2023.1108820/fullmagnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticlesimmobilizationpenicillin G acylasereusabilitysurface modification
spellingShingle Mingyi Ma
Xiu Chen
Yao Yue
Jie Wang
Dawei He
Ruijiang Liu
Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion process
Frontiers in Bioengineering and Biotechnology
magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles
immobilization
penicillin G acylase
reusability
surface modification
title Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion process
title_full Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion process
title_fullStr Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion process
title_full_unstemmed Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion process
title_short Immobilization and property of penicillin G acylase on amino functionalized magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles prepared via the rapid combustion process
title_sort immobilization and property of penicillin g acylase on amino functionalized magnetic ni0 3mg0 4zn0 3fe2o4 nanoparticles prepared via the rapid combustion process
topic magnetic Ni0.3Mg0.4Zn0.3Fe2O4 nanoparticles
immobilization
penicillin G acylase
reusability
surface modification
url https://www.frontiersin.org/articles/10.3389/fbioe.2023.1108820/full
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