文献类型：期刊文献

英文题名：Purification, characterization and structural identification of a novel bacteriocin produced by marine original Enterococcus durans YQ-6, and its inhibition of Listeria monocytogenes

作者：Li, Qibin[1];Chen, Quanyi[1];Wu, Yueying[1];Chen, Zhibao[2];Liu, Ying[1,3];Fang, Zhijia[1];Deng, Qi[1]

机构：[1]Guangdong Ocean Univ, Key Lab Adv Proc Aquat Prod, Coll Food Sci & Technol, Guangdong Prov Engn Technol Res Ctr Marine Food,Gu, Zhanjiang 524088, Peoples R China;[2]Guangdong Ocean Univ, Coll Coastal Agr Sci, Zhanjiang 524088, Peoples R China;[3]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China

年份：2023

卷号：173

外文期刊名：LWT-FOOD SCIENCE AND TECHNOLOGY

收录：SCI-EXPANDED(收录号：WOS:000992251400001)、、EI(收录号：20232614298759)、Scopus(收录号：2-s2.0-85163163298)、WOS

基金：This work was supported by the Guangdong Province Science and Technology Project (grant numbers: 2016A020222014) and Guangdong Innovation Team of Seafood Green Processing Technology (grant numbers: 2019KCXTD011) .

语种：英文

外文关键词：Enterococcus durans; Bacteriocin CAMT6; Purification; Antibacterial activity; Characteristics

外文摘要：The bacteriocin CAMT6 is a novel bacteriocin produced by Enterococcus durans YQ-6 isolated from Larimichthys polyactis in the South China Sea. In this study, the bacteriocin CAMT6 was purified by extraction using ethyl acetate, Sephadex LH-20 column chromatography, cation exchange chromatography and reversed-phase highperformance liquid chromatography, in sequence. The Liquid Chromatograph Triple Quadrupole Mass Spectrometer (LC-MS/MS) analysis revealed that the relative molecular mass and amino acid sequence of the bacteriocin CAMT6 were 1254.63 Da and N-GAVHDVKDVLDS, respectively. Combined with the circular dichroism (CD) spectroscopy results, CAMT6 was determined to be a novel Class IId bacteriocin. CAMT6 exhibited broad-spectrum antibacterial activity, inhibiting both gram-negative and gram-positive bacteria, even fungi. CAMT6 exhibited strong temperature stability, was stable over pH 2-7, and was inactivated by proteases. CAMT6 also significantly removed L. monocytogenes biofilms and inhibited L. monocytogenes by disrupting the permeability of the cell membrane. Furthermore, CAMT6 can effectively inhibit the growth of L. monocytogenes in chicken breast. These results suggest that the bacteriocin CAMT6 could serve as a potential biological preservative for food.