Novel bacteriocin produced by Lactobacillus alimentarius FM-MM4 from a traditional Chinese fermented meat Nanx Wudl: Purification, identification and antimicrobial characteristics. (July 2017)

• Record Type: Journal Article
• Authors: Hu, Yanxin; Liu, Xiaoli; Shan, Chengjun; Xia, Xiudong; Wang, Ying; Dong, Mingsheng; Zhou, Jianzhong
• Is Part Of: Food control. Volume 77(2017:Jul.)
• Page Start: 290
• Page End: 297
• Publication Date: 2017-07
• Subjects: Bacteriocin -- Lactobacillus alimentarius -- Purification -- Identification -- Antimicrobial properties; Food -- Quality -- Periodicals; Food -- Analysis -- Periodicals; Food handling -- Periodicals; Food industry and trade -- Quality control -- Periodicals; Aliments -- Industrie et commerce -- Qualité -- Contrôle -- Périodiques; Aliments -- Qualité -- Périodiques; Aliments -- Analyse -- Périodiques; Hygiène alimentaire -- Périodiques; Food -- Analysis; Food handling; Food -- Quality; Periodicals; Electronic journals; 664.07
• DOI: 10.1016/j.foodcont.2017.02.007
• Languages: English
• ISSNs: 0956-7135

Abstract

Abstract: The present study aims to purify and characterize a novel bacteriocin (designated as lactocin MM4 ) produced by Lactobacillus alimentarius FM-MM4, which was isolated from Nanx Wudl, a traditional Chinese fermented meat. Lactocin MM4 was extracted by ethyl acetate and purified through cation exchange chromatography and semi-preparative high-performance liquid chromatography (RP-HPLC). As revealed by LC-MS/MS, lactocin MM4 has a molecular mass of 1104.58 Da with the N-terminal sequence QGVGPLGQGHR, demonstrating low homology with previously reported class II bacteriocins. Lactocin MM4 exhibited broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative food-borne pathogens, as well as several yeasts. It was considerably thermo-stable with 84.7% residual antimicrobial activity after exposure to121 °C for 15 min, and it was highly stable at acidic pH (2–5). Proteases, such as trypsin, protease K, papain and pepsin, could completely inactivate the bacteriocin, while other enzymes, such as lipase and amylase, had no effect on its antimicrobial activity. These results indicate the potential of lactocin MM4 for application in food preservation. Highlights: A novel bacteriocin named Lactocin MM4 was produced by L. alimentarius FM-MM4 . Lactocin MM4 owns a molecular mass of 1104.58 Da. The N-terminal sequence is QGVGPLGQGHR. Broad-spectrum antimicrobial activity and thermal stabilities of Lactocin MM4 . Potential research and application value in the food preservation.