Abstract
Bacteriocins are ribosomally synthesized peptides or proteins possessing antibacterial activity against foodborne pathogens and spoilage bacteria. A novel bacteriocin, plantaricin LPL-1 was determined as a class IIa bacteriocin according to the YGNGV motif, and producer strain Lactobacillus plantarum LPL-1 was identified based on physio-biochemical characteristics and 16S rDNA sequence. The novel bacteriocin, plantaricin LPL-1 was purified by salt precipitation, cation exchange, gel filtration, and reverse phase high-performance liquid chromatography (RP-HPLC). The molecular mass of plantaricin LPL-1 was 4347.8467 Da by Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis and entire amino acid sequence of plantaricin LPL-1 was VIADKYYGNGVSCGKHTCTVDWGEAFSCSVSHLANFGHGKC. Plantaricin LPL-1 possessed the merits of easy degradation by proteases, wide pH stability (2–10), high thermal stability (121°C, 20 min), surfactants stability and bactericidal activity against foodborne spoilage and pathogens bacteria. The mode action and membrane permeabilization of plantaricin was identified. The information of plantaricin LPL-1 indicated that it is not only a novel class IIa bacteriocin, but also a promising natural and safe biologic preservative for the food preservation industry.
Highlights
Bacteriocins are ribosomally synthesized peptides or protein with antibacterial activity toward strains either within the same species or across different genera (De Vuyst and Leroy, 2007), an increasing number of novel bacteriocins against foodborne pathogens have been reported (Liu et al, 2015; Yi et al, 2016; Zhao et al, 2016)
A novel class IIa bacteriocin, plantaricin LPL-1 produced by L. plantarum LPL-1 isolated from fermented fish in Beijing, China, was purified and characterized
The plantaricin LPL-1 was just purified by absorption and desorption of pH, and cation exchange column, but it did not prove that plantaricin LPL-1 was a novel class IIa bacteriocin
Summary
Bacteriocins are ribosomally synthesized peptides or protein with antibacterial activity toward strains either within the same species or across different genera (De Vuyst and Leroy, 2007), an increasing number of novel bacteriocins against foodborne pathogens have been reported (Liu et al, 2015; Yi et al, 2016; Zhao et al, 2016). The bacteriocin nisin, which was found in 1933 in New Zealand, has been allowed to be used in 48 countries since its first marketed in England in 1953 (Tagg et al, 1995) Based on their primary structure, molecular mass, thermal stability, mode of action, and genetic properties, the bacteriocins produced by LAB have been divided into four classes (Klaenhammer, 1993): class I (
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