Use of bacteriophages as biocontrol agents is promising tool to control pathogenic bacteria including antibiotics-resistant bacteria. Not only bacteriophages but also endolysins, which are the peptidoglycan hydrolyzing enzymes encoded by bacteriophage...
Use of bacteriophages as biocontrol agents is promising tool to control pathogenic bacteria including antibiotics-resistant bacteria. Not only bacteriophages but also endolysins, which are the peptidoglycan hydrolyzing enzymes encoded by bacteriophages, have high potential for applications as biocontrol agents for foodborne pathogens. In this study, a putative endolysin gene was identified from the genome of the bacteriophage BPS13, which infects Bacillus cereus. In silico analysis of this endolysin, designated LysBPS13 showed that LysBPS13 consists with N-terminal catalytic domain (PRGP domain) and C-terminal cell wall binding domain (SH3_5 domain). Further characterization with the purified LysBPS13 revealed that this endolysin is an N-acetylmuramyl-L-alanine amidase, whose activity was not dependent on metal ions. Especially LysBPS13 has remarkable thermostability in the presence of glycerol as LysBPS13 showed lytic activity even after boiling for 30 min. Taken together, LysBPS13 can be considered as a favorable candidate as a new antimicrobial agent to control B. cereus in food products.