Dataset Information

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

ABSTRACT: 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.

SUBMITTER: Rong J

PROVIDER: S-EPMC6718962 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

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Publications

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

Rong Junhui J Zhou Zijuan Z Wang Yun Y Han Juan J Li Chunmei C Zhang Wenli W Ni Liang L

Food technology and biotechnology 20190601 2

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 high ...[more]

PMID: 31537975

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Project description:BACKGROUND: Horseradish peroxidases (HRPs) from Armoracia rusticana have long been utilized as reporters in various diagnostic assays and histochemical stainings. Regardless of their increasing importance in the field of life sciences and suggested uses in medical applications, chemical synthesis and other industrial applications, the HRP isoenzymes, their substrate specificities and enzymatic properties are poorly characterized. Due to lacking sequence information of natural isoenzymes and the low levels of HRP expression in heterologous hosts, commercially available HRP is still extracted as a mixture of isoenzymes from the roots of A. rusticana. RESULTS: In this study, a normalized, size-selected A. rusticana transcriptome library was sequenced using 454 Titanium technology. The resulting reads were assembled into 14871 isotigs with an average length of 1133 bp. Sequence databases, ORF finding and ORF characterization were utilized to identify peroxidase genes from the 14871 isotigs generated by de novo assembly. The sequences were manually reviewed and verified with Sanger sequencing of PCR amplified genomic fragments, resulting in the discovery of 28 secretory peroxidases, 23 of them previously unknown. A total of 22 isoenzymes including allelic variants were successfully expressed in Pichia pastoris and showed peroxidase activity with at least one of the substrates tested, thus enabling their development into commercial pure isoenzymes. CONCLUSIONS: This study demonstrates that transcriptome sequencing combined with sequence motif search is a powerful concept for the discovery and quick supply of new enzymes and isoenzymes from any plant or other eukaryotic organisms. Identification and manual verification of the sequences of 28 HRP isoenzymes do not only contribute a set of peroxidases for industrial, biological and biomedical applications, but also provide valuable information on the reliability of the approach in identifying and characterizing a large group of isoenzymes.

Dataset Information

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

Publications

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

Similar Datasets

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