Abstract
Bacteriocins have antimicrobial activities against food-spoiling bacteria and food-borne pathogens. Paracin 1.7, a bacteriocin synthesized by Lactobacillus paracasei HD1-7 isolated from Chinese sauerkraut juice, was studied. Following partial purification with ammonium sulfate precipitation, CM Sepharose Fast Flow, and Sephadex G-10 chromatography, the molecular weight of Paracin 1.7 was about 10 kDa based on Tricine-SDS-PAGE results. A 2.87 fold purified bacteriocin was produced, reaching a final yield of 39.93% and the specific activity of 1.56 × 103 AU/mg. The N-terminal amino acid sequence of Paracin 1.7 was VSNTFFA, and the LC/LTQ results revealed that the N-terminal amino acid sequence was similar to that of ABC-type oligopeptide transport system protein and N-acetylmuramoyl-L-alanine amidase. Paracin 1.7 was sensitive to protease K, had antimicrobial activities at a broad pH range (3.0–8.0), and was heat resistant (121 °C for 20 min). Paracin 1.7 from Lactobacillus paracasei HD1-7 is a novel bacteriocin that has potential applications in food preservation.
Highlights
Bacteriocins have antimicrobial activities against food-spoiling bacteria and food-borne pathogens
Paracin 1.7, a bacteriocin synthesized by Lactobacillus paracasei HD1-7 isolated from Chinese sauerkraut juice, was studied
Class-II consists of bacteriocins that lack modified residues[2,3,4,5,6], and include bacteriocins produced by Lactobacillus rhamnosus and bacteriocin Paracin 1.7 produced by L. paracasei HD1-7
Summary
Bacteriocins have antimicrobial activities against food-spoiling bacteria and food-borne pathogens. Paracin 1.7, a bacteriocin synthesized by Lactobacillus paracasei HD1-7 isolated from Chinese sauerkraut juice, was studied. Paracin 1.7 from Lactobacillus paracasei HD1-7 is a novel bacteriocin that has potential applications in food preservation. Bacteriocins are ribosomally synthesized low-molecular weight peptides or proteins with potential use in food preservation due to their bactericidal effects on food spoilage and pathogenic organisms[1]. Based on their primary structure, molecular mass, heat stability, and molecular organization, The LAB peptide bacteriocins are divided into three classes. Class-I consists of bacteriocins (often referred to as lantibiotics) that contain one or more of the modified amino acid residues lanthionine, b-methyllanthionine, dehydroalanine, dehydrobutyrine, and/or D-alanine[2]. The amino acid analysis of this bacteriocin will provide assistance for gene cloning and expression
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