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Characterization of Endolysin LysECP26 Derived from rV5-like Phage vB_EcoM-ECP26 for Inactivation of Escherichia coli O157:H7

Journal of Microbiology and Biotechnology 2020년 30권 10호 p.1552 ~ 1558
박도원, 박종현,
소속 상세정보
박도원 ( Park Do-Won ) - Gachon University Department of Food Science and Biotechnology
박종현 ( Park Jong-Hyun ) - Gachon University Department of Food Science and Biotechnology

Abstract


With an increase in the consumption of non-heated fresh food, foodborne shiga toxin-producing Escherichia coli (STEC) has emerged as one of the most problematic pathogens worldwide. Endolysin, a bacteriophage-derived lysis protein, is able to lyse the target bacteria without any special resistance, and thus has been garnering interest as a powerful antimicrobial agent. In this study, rV5-like phage endolysin targeting E. coli O157:H7, named as LysECP26, was identified and purified. This endolysin had a lysozyme-like catalytic domain, but differed markedly from the sequence of lambda phage endolysin. LysECP26 exhibited strong activity with a broad lytic spectrum against various gram-negative strains (29/29) and was relatively stable at a broad temperature range (4°C? 55°C). The optimum temperature and pH ranges of LysECP26 were identified at 37°C?42°C and pH 7? 8, respectively. NaCl supplementation did not affect the lytic activity. Although LysECP26 was limited in that it could not pass the outer membrane, E. coli O157: H7 could be effectively controlled by adding ethylenediaminetetraacetic acid (EDTA) and citric acid (1.44 and 1.14 log CFU/ml) within 30 min. Therefore, LysECP26 may serv as an effective biocontrol agent for gram-negative pathogens, including E. coli O157:H7.

키워드

E. coli O157:H7; rV5-like phage; endolysin; outer membrane permeabilizers (OMPs)

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