getpdf  NLM PubMed Logo  https://doi.org/10.17113/ftb.57.02.19.5832     


Immobilization of Horseradish Peroxidase on Multi-Armed Magnetic Graphene Oxide Composite: Improvement of Loading Amount and Catalytic Activity   


Junhui Rong1orcid tiny, Zijuan Zhou2orcid tiny, Yun Wang1*orcid tiny, Juan Han3orcid tiny, Chunmei Li1orcid tiny, Wenli Zhang1orcid tiny and Liang Ni1orcid tiny  


1School of Chemistry and Chemical Engineering, Jiangsu University, 212013 Zhenjiang, PR China 
2School of Food Science and Nutrition, University of Leeds, Leeds, LS2 9JT, UK 
3School of Food and Biological Engineering, Jiangsu University, 212013 Zhenjiang, PR China   



Article history
Received: 6 May 2018 
Accepted: 8 May 2019
cc  



Key words
immobilized enzyme, graphene oxide, multi-armed polymer, horseradish peroxidase, synergistic effect    



Summary
In this study, a novel type of multi-armed polymer (poyltehylene glycol, PEG) magnetic graphene oxide (GO) composite (GO@Fe3O4@6arm-PEG-NH2) has been synthesized as a support for immobilization of horseradish peroxidase (HRP) for the first time. The loading amount of HRP was relatively high (186.34 mg/g) due to the surface of carrier material containing a large amount of amino groups from 6arm-PEG-NH2, but degradation rate of phenols was also much higher (95.4 %), which is attributed to the synergistic effect between the free HRP (45.4 %) and the support material of GO@Fe3O4@6arm-PEG-NH2 (13.6 %). Compared with the free enzyme, thermal, storage and operational stability of the immobilized HRP improved. The immobilized HRP still retained over 68.1 % activity after being reused 8 times. These results suggest that the multi-armed magnetic composite has good application prospect for enzyme immobilization.   




*Corresponding author:  tel3  +8615896385156 
                                           email3  yunwang@ujs.edu.cn

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