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

Jae Hyun Cho, Joon Gi Kwon, Daniel J. O'Sullivan, Sangryeol Ryu, Ju Hoon Lee

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Article number128562
JournalFood Chemistry
Volume345
DOIs
StatePublished - May 30 2021

Bibliographical note

Funding Information:
This research was supported by a grant (19162MFDS037) from the Ministry of Food and Drug Safety in 2020.

Publisher Copyright:
© 2020

Keywords

  • Bacteriophage
  • Cell wall–binding domain
  • Clostridium perfringens
  • Endolysin
  • Rapid detection

PubMed: MeSH publication types

  • Journal Article

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