Purification and characterization of a novel bacteriocin CAMT2 produced by Bacillus amyloliquefaciens isolated from marine fish Epinephelus areolatus

- The molecular mass of purified bacteriocin CAMT2 is about 20.0 kDa.
- N-terminal sequencing reveal low similarity with existing antimicrobial peptide.
- The purified bacteriocin CAMT2 show wider antimicrobial activity spectrum.
- CAMT2 resistant 100 °C and pH 2-10, but lost activity treated with proteases K.
- Significant reduction of L. monocytogenes counts for CAMT2 than control in meat.

A novel bacteriocin named CAMT2 was produced by strain ZJHD3-06 which was isolated from the marine fish Epinephelus areolatus and identified as Bacillus amyloliquefaciens, Bacteriocin CAMT2 inhibits important food spoilage and food-borne pathogens such as Listeria monocytogenes, Staphylococcus aureus, Escherichia coli and Vibrio parahaemolyticus. Bacteriocin CAMT2 was purified by ammonium sulfate precipitation, gel filtration chromatography on Sephadex G-50 and reversed phase chromatography on a C18 column. The molecular mass of the purified bacteriocin CAMT2 was about 20.0 kDa and N-terminal sequencing of the peptides revealed low similarity with existing antimicrobial peptides, as determined by an LC-MS/MS system. Bacteriocin CAMT2 was resistant for up to 100 °C and pH ranging 2-10, but lost its activity when treated with protease K. The bacteriocin also showed significant antimicrobial activity against L. monocytogenes in a meat model system. These obtained results suggest that bacteriocin CAMT2 has potential for use as a food biopreservative.