Evidence map›Paper›PMID 41667955›Full record

ArticleBMC microbiology2026

Purification and characterization of novel class IId bacteriocins, petauricin A and petauricin B produced by Lactococcus petauri NC2.

Tanziba Alam, Thien Hoang Phan, Ghoson Mosbah Daba, Jiro Nakayama, Takeshi Zendo

Abstract read
In one paragraph

Article in BMC microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Tanziba AlamDepartment of Biosciences and Bioengineering, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan.
Thien Hoang PhanDepartment of Biosciences and Bioengineering, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan.
Ghoson Mosbah DabaDepartment of Biosciences and Bioengineering, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan.
Jiro NakayamaDepartment of Biosciences and Bioengineering, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan.
Takeshi ZendoDepartment of Biosciences and Bioengineering, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan. zendo@agr.kyushu-u.ac.jp.

Funding

Japan Society for the Promotion of Science 21H02107
6 · The paper itself

Abstract

Bacteriocins produced by lactic acid bacteria (LAB) possess a well-established safety profile and are therefore widely studied as safe antimicrobial substances. The development of diverse novel bacteriocins is essential for managing harmful bacteria that are continually evolving. This study describes the purification, characterization, and mode of action of the bacteriocins produced by Lactococcus petauri strain NC2 isolated from fermented sausage. Three-step chromatographic purification, including hydrophobic interaction, cation exchange, and reverse-phase high-performance liquid chromatography of the active culture supernatants, was followed by mass spectrometry analysis, which detected the two purified bacteriocins with molecular weights of 4711.8 Da and 5432.7 Da, designated petauricin A and petauricin B, respectively. The whole genome analysis detected the presence of the gene cluster consisting of putative bacteriocin precursor genes (petA, petB) and biosynthesis-related genes (petIa, petIb, petC, petD). Sequence alignment revealed the amino acid sequences of putative translated bacteriocin core peptides, petauricin A and petauricin B, have sequence similarity to garvicin AG1 (97%) and garvicin AG2 (72%), respectively. While petauricin A showed inhibitory activity only toward the species of L. garvieae, the inhibitory spectrum of petauricin B included several genera such as Lactococcus, Latilactobacillus, Enterococcus, Listeria, Heyndrickxia, and Pediococcus. Composition and organization of the gene cluster, peptide sequences, and antibacterial behaviours indicate that petauricin A and petauricin B are classified as class IId bacteriocins. Both bacteriocins demonstrated strong bactericidal activity. This study reports that the L. petauri strain NC2 produces bacteriocins with promising antibacterial activity, representing the first novel bacteriocins characterized in the L. petauri species.

Indexed as

BacteriocinsLactococcusAmino Acid SequenceAnti-Bacterial AgentsChromatography, High Pressure LiquidMass SpectrometryMeat ProductsMolecular WeightMultigene FamilyAnti-Bacterial AgentsBacteriocinsBacteriocin purificationBiosynthetic gene clusterLactococcus petauriMode of actionPetauricin

Identifiers

PMID41667955
PMCPMC12998123

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.