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Heterologous Expression and Application of Multicopper Oxidases from Enterococcus spp. for Degradation of Biogenic Amines

文献类型： 外文期刊

作者： Li, Binbin 1 ; Wang, Yuan 1 ; Xue, Linlin 1 ; Lu, Shiling 1 ;

作者机构： 1.Shihezi Univ, Coll Food Sci, Shihezi 832000, Peoples R China

2.Xinjiang Acad Agr & Reclamat Sci, Shihezi 832000, Peoples R China

关键词： Biogenic amine; recombinant enzyme; Enterococcus spp.; multicopper oxidase; amine degradation; recombinant strains

期刊名称：PROTEIN AND PEPTIDE LETTERS （ 影响因子：1.156； 五年影响因子：1.054 ）

ISSN： 0929-8665

年卷期： 2021 年 28 卷 2 期

页码：

收录情况： SCI

摘要： Background: Biogenic amines are harmful to human health at a certain extent. As a kind of biogenic amine oxidase, multicopper oxidase can be used to degrade them. Currently, the literature about enzyme from Enterococcus spp. are limited, and recombinant multicopper oxidase might be an effective way to degrade biogenic amines. Objective: (i) Select and identify strains that can degrade biogenic amines, (ii) overexpress enzyme from Enterococcus spp., (iii) measure gene expression and probe amine-degradation differences among strains (native, E. coli DH5 alpha, and L. delbruckii), and (iv) examine the biochemical properties of recombinant multicopper oxidase, (v) apply the recombinant enzyme into smoked horse-meat sausage. Methods: Reverse transcription PCR and high-performance liquid chromatography were performed to examine gene expression and amine degradation rate. Results: The results demonstrated that target enzymes were successfully overexpressed, accompanied by increased amine-degrading activity (P<0.05). Gene from E. faecalis M5B was expressed in L. delbrueckii resulted in degradation rates for phenylethylamine, putrescine, histamine and tyramine of 54%, 52%, 70% and 40%, respectively, significantly higher than achieved by other recombinant strains. Conclusion: In this work, gene expression levels were higher in recombinant M5B than recombinant M2B, regardless of host. E. coli is more stable to express multicopper oxidase. Besides, the amine-degrading ability was markedly increased in the two recombinant strains. After prolonged incubation, the recombinant enzyme could degrade three amines, and it displayed high alkali resistance and thermostability.

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