조재현 (경희대학교) | 한빛사논문 > 한빛사

구.농수식품

조회826

경희대학교

Food Chem., Available online 5 November 2020, 128562 | https://doi.org/10.1016/j.foodchem.2020.128562 Development of an endolysin enzyme and its cell wall–binding domain protein and their applications for biocontrol and rapid detection of Clostridium perfringens in food

Abstract

Jae-Hyun Cho^a,1, Joon-Gi Kwon^b,1, Daniel J. O'Sullivan^c, Sangryeol Ryu^b, Ju-Hoon Lee^b,*

^aDepartment of Food Science and Biotechnology, Graduate School of Biotechnology, Kyung Hee University, Yongin, South Korea
^bDepartment of Food and Animal Biotechnology, Department of Agricultural Biotechnology, Center for Food and Bioconvergence, Seoul National University, Seoul, South Korea
^cDepartment of Food Science and Nutrition, University of Minnesota, St. Paul, MN 55108, USA

¹These authors equally contributed to this work.

^*Corresponding author

Abstract
Clostridium perfringens is a well-known pathogen that causes food-borne illnesses. Although bacteriophages can be effective natural food preservatives, phage endolysin and cell wall–binding domain (CBD) provide useful materials for lysis of C. perfringens and rapid detection. The genome of phage CPAS-15 consists of 51.8-kb double-stranded circular DNA with 78 open reading frames, including an endolysin gene. The apparent absence of a virulence factor or toxin gene suggests its safety in food applications. C. perfringens endolysin (LysCPAS15) inhibits host cells by up to a 3-log reduction in 2 h, and enhanced green fluorescent protein (EGFP)-fused CBD protein (EGFP-LysCPAS15_CBD1) detects C. perfringens within 5 min. Both exhibit broader host range spectra and higher stabilities than a bacteriophage. Tests in milk show the same host lysis and specific detection activities, with no hindrance effect from food matrices, indicating that endolysin and its CBD can provide food extended protection from C. perfringens contamination.

논문정보

형식Research article
게재일2020년 11월 (BRIC 등록일 2020-12-24)
연구진국내(교신)+국외 연구진
분야 생명과학 > 미생물학
구분구・농수식품

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