Characterization of bacteriocin N15 produced by enterococcus faecium N15 and cloning of the related genes

Losteinkit, Chanvadee; Uchiyama, Kimio; Ochi, Shuichiro; Takaoka, Tomoyo; Nagahisa, Keisuke; Shioya, Suteaki

doi:10.1016/s1389-1723(01)80157-2

Cited by 23 publications

(3 citation statements)

References 24 publications

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“…In contrast, Losteinkit et al (2001) working with a bacteriocin N 15 produced by E. faecium isolated from nuka (Japanese rice-bran paste) reported that bacteriocin activity was stable under heat treatment at 100 1C for 2 h. Campos et al (2006) reported a high thermal resistance of bacteriocins produced by L. lactis and E. faecium, which did not elicit any loss of antimicrobial activity against L. monocytogenes and Staphylococcus aureus after treated at 100 1C for 60 min. In our experimental design metabolites produced by E. faecium demonstrated low thermal resistance.…”

Section: Effect Of Temperature Treatmentsmentioning

confidence: 99%

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Preliminary characterization of bacteriocin-like substances from lactic acid bacteria isolated from organic leafy vegetables

Ponce

Moreira

Valle

et al. 2008

LWT - Food Science and Technology

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Section: Effect Of Temperature Treatmentsmentioning

confidence: 99%

“…Trypsin only inactivates supernatant culture produced by E. faecium, except when E. coli was used as indicator. Losteinkit et al (2001) working with a Bacteriocin N15 produced by E. faecium N15 found that this activity was inhibited by proteinase K, a-chymotrypsin, pepsin, trypsin and lysozyme.…”

Section: Sensitivity To Proteolytic Enzymesmentioning

confidence: 99%

Preliminary characterization of bacteriocin-like substances from lactic acid bacteria isolated from organic leafy vegetables

Ponce

Moreira

Valle

et al. 2008

LWT - Food Science and Technology

View full text Add to dashboard Cite

“…Our preliminary examination indicated that the sonorensin produced by MT93 could belong to class II, because it was shown to be active against Listeria. Class IIa bacteriocins have a conserved amino acid sequence, YGNGV, in the amino-terminal region and LDNAIE in histidine kinases (30). Based on these amino acid sequences, two primers, oligo 48 and oligo 105 (Table 1), were syn- thesized, and amplification PCR was carried out with total genomic DNA of MT93 as the template.…”

Section: Isolation and Identification Of Microorganisms Producing Antmentioning

confidence: 99%

Sonorensin: an Antimicrobial Peptide, Belonging to the Heterocycloanthracin Subfamily of Bacteriocins, from a New Marine Isolate, Bacillus sonorensis MT93

Chopra

Singh

Choudhary

et al. 2014

Appl Environ Microbiol

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Marine environments are the greatest fronts of biodiversity, representing a resource of unexploited or unknown microorganisms and new substances having potential applications. Among microbial products, antimicrobial peptides (AMPs) have received great attention recently due to their applications as food preservatives and therapeutic agents. A new marine soil isolate producing an AMP was identified as Bacillus sonorensis based on 16S rRNA gene sequence analysis. It produced an AMP that showed a broad spectrum of activity against both Gram-positive and Gram-negative bacteria. The peptide, named sonorensin, was purified to homogeneity using a combination of chromatographic techniques. The intact molecular mass of the purified peptide, 6,274 Da, as revealed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF), was in agreement with Tricine-SDS-PAGE analysis. A PCR array of primers was used to identify AMP structural genes, which allowed the successful amplification of the related genes from strain MT93. The putative open reading frame of sonorensin was amplified, cloned into the pET-32a(؉) vector, expressed as a thioredoxin (Trx) fusion protein in Escherichia coli, and then purified. Sequence alignment analysis revealed that the bacteriocin being reported could belong to new subfamily of bacteriocins, heterocycloanthracin. The peptide indicated its potential as a biocontrol agent or food antimicrobial agent, due to its antimicrobial activity against bacteria such as Listeria monocytogenes and Staphylococcus aureus. This is the first report of the production, purification, and characterization of wild-type and recombinant bacteriocin by B. sonorensis and the first bacteriocin of the heterocycloanthracin subfamily to be characterized.

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Construction of Plasmid Vector for Expression of Bacteriocin N15-Encoding Gene and Effect of Engineered Bacteria on Enterococcus faecalis

Lertcanawanichakul

2007

Curr Microbiol

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A 6.09-kb plasmids vector pOri253 was constructed from the plasmid pIL253 (5.2 kb) and a 0.89-kb fragment of oriColE1 from pBluescript II KS. The bifunctional plasmid pOri253 conferred erythromycin resistance in both Escherichia coli and Enterococcus faecalis. It has unique sites for EcoRI, BamHI, SalI, and PstI derived from pIL253 and was lost at a low rate in E. faecalis JCM8726 when cultured in Man, Rogosa, & Sharpe broth without antibiotic. The lactococcal promoter P23 was inserted at one end of the pOri253 multicloning site. Gene expression was assessed by an entAI gene, which produced bacteriocin N15. The E. faecalis harboring constructed plasmid carrying P23 (pOrient23) had more antibacterial activity than parental E. faecalis JCM8726 and its clone harboring non-P23-containing plasmid (pOrient), as determined by means of an overlay method.

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Characterization of bacteriocin N15 produced by enterococcus faecium N15 and cloning of the related genes

Cited by 23 publications

References 24 publications

Preliminary characterization of bacteriocin-like substances from lactic acid bacteria isolated from organic leafy vegetables

Preliminary characterization of bacteriocin-like substances from lactic acid bacteria isolated from organic leafy vegetables

Sonorensin: an Antimicrobial Peptide, Belonging to the Heterocycloanthracin Subfamily of Bacteriocins, from a New Marine Isolate, Bacillus sonorensis MT93

Construction of Plasmid Vector for Expression of Bacteriocin N15-Encoding Gene and Effect of Engineered Bacteria on Enterococcus faecalis

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