Abstract
The aim of this study is to investigate the antimicrobial potential of Lactobacillus plantarum ZJ5, a strain isolated from fermented mustard with a broad range of inhibitory activity against both Gram-positive and Gram-negative bacteria. Here we present the peptide plantaricin ZJ5 (PZJ5), which is an extreme pH and heat-stable. However, it can be digested by pepsin and proteinase K. This peptide has strong activity against Staphylococcus aureus. PZJ5 has been purified using a multi-step process, including ammonium sulfate precipitation, cation-exchange chromatography, hydrophobic interactions and reverse-phase chromatography. The molecular mass of the peptide was found to be 2572.9 Da using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The primary structure of this peptide was determined using amino acid sequencing and DNA sequencing, and these analyses revealed that the DNA sequence translated as a 44-residue precursor containing a 22-amino-acid N-terminal extension that was of the double-glycine type. The bacteriocin sequence exhibited no homology with known bacteriocins when compared with those available in the database, indicating that it was a new class IId bacteriocin. PZJ5 from a food-borne strain may be useful as a promising probiotic candidate.
Highlights
Bacteriocins are ribosomally synthesized peptides that in most cases, exhibit antibacterial activity against bacteria that are closely related to the producing bacteria
Most bacteriocins belong to class II, which are divided into four groups, namely class IIa, IIb, IIc, and IId
The strain was designated L. plantarum ZJ5, and the bacteriocin produced by this strain was named plantaricin ZJ5 (PZJ5)
Summary
Bacteriocins are ribosomally synthesized peptides that in most cases, exhibit antibacterial activity against bacteria that are closely related to the producing bacteria. Bacteriocins from lactic acid bacteria (LAB) are mostly small, heat-stable, hydrophobic, and cationic peptides [1,2] These peptides have attracted significant attention because of their possible applications as non-toxic additives for food preservation and prevention of food spoilage by food-borne pathogenic bacteria [3,4,5]. Depending on their structural characteristics, LAB bacteriocins have been classified by Klaenhammer (1993) into three main groups [6]: class I is small (,5 kDa) peptides called lantibiotics, which contains post-translationally modified amino acid residues, such as lanthionine and 3-methyllanthionine; class II is small, heatstable, nonmodified and membrane-active peptides; and class III is large (.10 kDa) and heat-labile peptides [7].
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