Affiliation:
1. College of Food Science, Shihezi University, Shihezi 832000, China
Abstract
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 DH5α, and L. delbruckii), and (iv) examine the biochemical properties
of recombinant multicopper oxidase, (v) apply the recombinant enzyme into smoked horsemeat
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.
Funder
National Natural Science Foundation of China
Publisher
Bentham Science Publishers Ltd.
Subject
Biochemistry,General Medicine,Structural Biology
Cited by
7 articles.
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