Purification and characterization of plantaricin LR14: a novel bacteriocin produced by Lactobacillus plantarum LR/14

• Published in: Applied microbiology and biotechnology Vol. 79; no. 5; pp. 759 - 767
• Main Authors: Tiwari, Santosh Kumar, Srivastava, Sheela
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Berlin/Heidelberg : Springer-Verlag 01.07.2008; Springer Berlin Heidelberg; Springer; Springer Nature B.V
• Subjects: Amino Acid Sequence; Amino acids; Ammonium; Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Bacterial Proteins - pharmacology; Bacteriocin; Bacteriocins - chemistry; Bacteriocins - isolation & purification; Bacteriocins - metabolism; Bacteriocins - pharmacology; Biological and medical sciences; Biotechnologically Relevant Enzymes and Proteins; Biotechnology; Cation-exchange chromatography; Characterization; Chromatography; Enzymes; Fundamental and applied biological sciences. Psychology; Indicator organisms; Isoelectric Point; Lactobacillus plantarum; Lactobacillus plantarum - chemistry; Lactobacillus plantarum - metabolism; Life Sciences; Mass spectrometry; mechanism of action; Microbial Genetics and Genomics; Microbiology; Micrococcus luteus; Micrococcus luteus - drug effects; Mode of action; Molecular Sequence Data; Molecular Weight; Peptides; Proteins; purification; RP-FPLC; Scientific imaging; Studies; Characterization; Purification; Cation-exchange chromatography; RP-FPLC; Bacteriocin; Mode of action; Cation exchange; Lactic acid bacteria; Lactobacillus plantarum; Bactericidal effect; Ion exchange chromatography; Bacteria; Lactobacillaceae; Mechanism of action
• ISSN: 0175-7598; 1432-0614
• DOI: 10.1007/s00253-008-1482-6

Bacteriocin produced by Lactobacillus plantarum strain LR/14 was purified to homogeneity by a multi-step protocol consisting of ammonium sulfate precipitation, cation-exchange chromatography, gel-filtration, and reverse-phase FPLC. L. plantarum LR/14 secreted a low-molecular-weight bacteriocin consisting of two peptides designated as plantaricin LR14α and -β with molecular mass of 3,012.46 and 5,605.74 Da, respectively. The purified peptides were characterized to be highly thermostable and active in acidic pH range, with a pI of >10.0. Both α and β peptides showed bactericidal mode of action against indicator strain, Micrococcus luteus and together showed a synergistic action. These peptides were differentially sensitive to a range of proteolytic enzymes, indicating differences in their composition. Amino acid sequencing revealed that the N-terminus in both the cases is blocked; thus, only a partial sequence could be obtained after CNBr digestion. These sequences, when compared with those available in the database, showed no homology with known bacteriocins, indicating it to be a novel compound.