Enterocin
Mostrando 1-12 de 32 artigos, teses e dissertações.
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1. Antimicrobial activity of enterocin obtained from Enterococcus durans on Shiga-like toxin-producing Escherichia coli
RESUMO: Escherichia coli, produtora de toxina Shiga-like (STEC), apresenta riscos à saúde humana, constituindo uma importante fonte de contaminação na indústria de alimentos. Diversos processos industriais eliminam esse microrganismo, contudo podem alterar as características do produto. Métodos alternativos de conservação tem sido uma opção para
Cienc. Rural. Publicado em: 02/09/2019
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2. Antibacterial efficacy of Nisin, Pediocin 34 and Enterocin FH99 against Listeria monocytogenes and cross resistance of its bacteriocin resistant variants to common food preservatives
Antilisterial efficiency of three bacteriocins, viz, Nisin, Pediocin 34 and Enterocin FH99 was tested individually and in combination against Listeria mononcytogenes ATCC 53135. A greater antibacterial effect was observed when the bacteriocins were combined in pairs, indicating that the use of more than one LAB bacteriocin in combination have a higher antiba
Braz. J. Microbiol.. Publicado em: 14/05/2013
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3. Identificação molecular de bactérias ácido láticas isoladas de leite cru e queijo, e pesquisa de genes de bacteriocinas / Molecular identification of lactic acid bacteria isolated from raw milk and cheese, and detection of bacteriocin genes
Considering the importance of the lactic acid bacteria (LAB) as biopreservatives, and their inhibitory potencial against pathogens and spoilage microrganisms, the aim of this study was identify using molecular methodologies LAB isolates obtained from raw milk and soft cheese, and to conduct a detailed study about the presence of bacteriocin codifying genes.
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 16/02/2011
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4. Estudo da produção e purificação parcial de enterocina utilizando Enterococcus spp. / Study of enterocin production and partial purification by Enterococcus spp.
Bacteriocins are protein substances produced by bacteria that are bactericidal or bacteriostatic against sensitive bacterial species. Both gram-negative and gram-positive organisms, including the lactic acid bacteria, produce these compounds. These bacteria are extensively used in food processing, for their contribution to shelf life, texture and organolepti
Publicado em: 2004
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5. Enterocin P Causes Potassium Ion Efflux from Enterococcus faecium T136 Cells
Enterocin P is a bacteriocin produced by Enterococcus faecium P13. We studied the mechanism of its bactericidal action using enterocin-P-sensitive E. faecium T136 cells. The bacteriocin is incapable of dissipating the transmembrane pH gradient. On the other hand, depending on the buffer used, enterocin P dissipates the transmembrane potential. Enterocin P ef
American Society for Microbiology.
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6. Purification and characterization of enterocin 4, a bacteriocin produced by Enterococcus faecalis INIA 4.
A simple two-step procedure was developed to obtain pure enterocin 4, a bacteriocin produced by Enterococcus faecalis INIA 4. Chemical and genetic characterization revealed that the primary structure of enterocin 4 is identical to that of peptide antibiotic AS-48 from Enterococcus faecalis S-48. In contrast to the reported inhibitory spectrum of AS-48, enter
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7. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins.
A new bacteriocin has been isolated from an Enterococcus faecium strain. The bacteriocin, termed enterocin A, was purified to homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and mass spectrometry analysis. By combining the data obtained from amino acid and DNA sequencing, the primary struc
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8. Heterologous Coproduction of Enterocin A and Pediocin PA-1 by Lactococcus lactis: Detection by Specific Peptide-Directed Antibodies
Antibodies against enterocin A were obtained by immunization of rabbits with synthetic peptides PH4 and PH5 designed, respectively, on the N- and C-terminal amino acid sequences of enterocin A and conjugated to the carrier protein KLH. Anti-PH4-KLH antibodies not only recognized enterocin A but also pediocin PA-1, enterocin P, and sakacin A, three bacterioci
American Society for Microbiology.
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9. Characterization and Heterologous Expression of the Genes Encoding Enterocin A Production, Immunity, and Regulation in Enterococcus faecium DPC1146
Enterocin A is a small, heat-stable, antilisterial bacteriocin produced by Enterococcus faecium DPC1146. The sequence of a 10,879-bp chromosomal region containing at least 12 open reading frames (ORFs), 7 of which are predicted to play a role in enterocin biosynthesis, is presented. The genes entA, entI, and entF encode the enterocin A prepeptide, the putati
American Society for Microbiology.
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10. Enterocin P Selectively Dissipates the Membrane Potential of Enterococcus faecium T136
Enterocin P is a pediocin-like, broad-spectrum bacteriocin which displays a strong inhibitory activity against Listeria monocytogenes. The bacteriocin was purified from the culture supernatant of Enterococcus faecium P13, and its molecular mechanism of action against the sensitive strain E. faecium T136 was evaluated. Although enterocin P caused significant
American Society for Microbiology.
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11. Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum.
Enterocin P is a new bacteriocin produced by Enterococcus faecium P13 isolated from a Spanish dry-fermented sausage. Enterocin P inhibited most of tested spoilage and food-borne gram-positive pathogenic bacteria, such as Listeria monocytogenes, Staphylococcus aureus, Clostridium perfringens, and Clostridium botulinum. Enterocin P is produced during growth in
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12. Enhancement of the Enterocin CRL35 Activity by a Synthetic Peptide Derived from the NH2-Terminal Sequence
The enterocin CRL35 biosynthetic gene cluster was cloned and sequenced. The sequence was revealed to be highly identical to that of the mundticin KS gene cluster (S. Kawamoto, J. Shima, R. Sato, T. Eguchi, S. Ohmomo, J. Shibato, N. Horikoshi, K. Takeshita, and T. Sameshima, Appl. Environ. Microbiol. 68:3830-3840, 2002). Short synthetic peptides were designed
American Society for Microbiology.