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Isolation and partial characterization of a bacteriocin produced by Lactobacillus plantarum BM‐1 isolated from a traditionally fermented Chinese meat product
Lactobacillus plantarum BM‐1 isolated from a traditionally fermented Chinese meat product was found
to produce a novel bacteriocin that is active against a wide range of gram‐positive and gram‐negative
bacteria. Production of the bacteriocin BM‐1 started early in the exponential phase and its maximum
activity (5120 AU/mL) was recorded early during the stationary phase (16 hr). Bacteriocin BM‐1 is
sensitive to proteolytic enzymes but stable in the pH range of 2.0–10.0 and heat‐resistant (15 min at 121°
C). This bacteriocin was purified through pH‐mediated cell adsorption–desorption and cationexchange
chromatography on an SP Sepharose Fast Flow column. The molecular weight of the purified
bacteriocinBM‐1 was determined to be 4638.142 Da by electrospray ionization Fourier transformmass
spectrometry. Furthermore, the N‐terminal amino acid sequence was obtained through automated
Edman degradation and found to comprise the following 15 amino acid residues: H2N‐Lys‐Tyr‐Tyr‐
Gly‐Asn‐Gly‐Val‐Tyr‐Val‐Gly‐Lys‐His‐Ser‐Cys‐Ser. Comparison of this sequence with that of other
bacteriocins revealed that bacteriocin BM‐1 contains the consensus YGNGVamino acid motif near the
N‐terminus. Based on its physicochemical characteristics, molecular weight, and N‐terminal amino
acid sequence, plantaricin BM‐1 is a novel class IIa bacteriocin.
Key words Bacteriocin, Lactobacillus plantarum, N‐terminal amino acid sequence
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