Two-peptide bacteriocin from Lactobacillus plantarum PMU 33 strainisolated from som-fak, a Thai low salt fermented fish product
W. Noonpakdee1*, P. Jumriangrit1, K. Wittayakom1, J. Zendo,J. Nakayama2, K. Sonomoto2 , S. Panyim1
1Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok 10400, Thailand
2Laboratory of Microbial Science and Technology, Division of Bioscience and Biotechnology,Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 6-10-1 Hakozaki,Higashi-ku, Fukuoka 812-8581, Japan
*Author for Correspondence.
Department of Biochemistry,
Faculty of Science,
Mahidol University,
Bangkok 10400, Thailand.
Tel: +66-2-2015600 ; Fax: +66-2-3547174;
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Abstract.
A total of 12,520 lactic acid bacteria (LAB) isolated from fermented fish products “som-fak” were screened for bacteriocin. One Lactobacillus plantarum PMU33 strain produced bacteriocin that inhibited a large number of Gram-positive bacteria including food borne pathogens, Listeria monocytogenes, Bacillus cereus and Staphylococcus aureus. Biochemical studies revealed that the bacteriocin was heat stable even at autoclaving temperature (121°C for 15 min) and was active over a wide pH range (2-10). The bacteriocin purified and characterized from the culture supernatant consists of two peptides with the molecular masses of 3222 and 3099 by mass spectrometry analysis. The molecular mass of this two-peptide bacteriocin were nearly identical to that of two-peptide plantaricin W (Plw) which consists of two peptides Plwα and Plwβ. The genes encoding these two peptides amplified by PCR with Plw gene specific primer showed identical sequences to Plwα and Plwβ. The bacteriocins and their producing strains isolated from som-fak may find application as bio-preservatives in fermented food products.
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