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Bacteriocin

The Experts below are selected from a list of 312 Experts worldwide ranked by ideXlab platform

Myeong Su Shin – 1st expert on this subject based on the ideXlab platform

  • isolation and partial characterization of a Bacteriocin produced by pediococcus pentosaceus k23 2 isolated from kimchi
    Journal of Applied Microbiology, 2008
    Co-Authors: Myeong Su Shin

    Abstract:

    Aims:  Screening and partial characterization of a Bacteriocin produced by Pediococcus pentosaceus K23-2 isolated from Kimchi, a traditional Korean fermented vegetable.

    Methods and Results:  A total of 1000 lactic acid bacteria were isolated from various Kimchi samples and screened for the production of Bacteriocin. Pediocin K23-2, a Bacteriocin produced by the Pediococcus pentosaceus K23-2 strain, showed strong inhibitory activity against Listeria monocytogenes. The Bacteriocin activity remained unchanged after 15 min of heat treatment at 121°C or exposure to organic solvents; however, it diminished after treatment with proteolytic enzymes. The Bacteriocin was maximally produced at 37°C, when the pH of the culture broth was maintained at 5·0 during the fermentation, although the optimum pH for growth was 7·0. The molecular weight of the Bacteriocin was about 5 kDa according to a tricine SDS-PAGE analysis.

    Conclusions: Pediococcus pentosaceus K23-2 isolated from Kimchi produces a Bacteriocin, which shares similar characteristics to the Class IIa Bacteriocins. The Bacteriocin is heat stable and shows wide antimicrobial activity against Gram-positive bacteria, especially L. monocytogenes.

    Significance and Impact of the Study:  Pediocin K23-2 and pediocin K23-2-producing P. pentosaceus K23-2 could potentially be used in the food and feed industries as natural biopreservatives, and for probiotic application to humans or livestock.

  • Isolation and partial characterization of a Bacteriocin produced by Pediococcus pentosaceus K23‐2 isolated from Kimchi
    Journal of Applied Microbiology, 2008
    Co-Authors: Myeong Su Shin

    Abstract:

    Aims:  Screening and partial characterization of a Bacteriocin produced by Pediococcus pentosaceus K23-2 isolated from Kimchi, a traditional Korean fermented vegetable.

    Methods and Results:  A total of 1000 lactic acid bacteria were isolated from various Kimchi samples and screened for the production of Bacteriocin. Pediocin K23-2, a Bacteriocin produced by the Pediococcus pentosaceus K23-2 strain, showed strong inhibitory activity against Listeria monocytogenes. The Bacteriocin activity remained unchanged after 15 min of heat treatment at 121°C or exposure to organic solvents; however, it diminished after treatment with proteolytic enzymes. The Bacteriocin was maximally produced at 37°C, when the pH of the culture broth was maintained at 5·0 during the fermentation, although the optimum pH for growth was 7·0. The molecular weight of the Bacteriocin was about 5 kDa according to a tricine SDS-PAGE analysis.

    Conclusions: Pediococcus pentosaceus K23-2 isolated from Kimchi produces a Bacteriocin, which shares similar characteristics to the Class IIa Bacteriocins. The Bacteriocin is heat stable and shows wide antimicrobial activity against Gram-positive bacteria, especially L. monocytogenes.

    Significance and Impact of the Study:  Pediocin K23-2 and pediocin K23-2-producing P. pentosaceus K23-2 could potentially be used in the food and feed industries as natural biopreservatives, and for probiotic application to humans or livestock.

Colin Hill – 2nd expert on this subject based on the ideXlab platform

  • Microbial production of Bacteriocins for use in foods
    Microbial Production of Food Ingredients Enzymes and Nutraceuticals, 2020
    Co-Authors: D.g. Burke, Paul D. Cotter, R.p. Ross, Colin Hill

    Abstract:

    Abstract: Bacteriocins are ribosomally synthesised, antimicrobial peptides produced by bacteria. Many Bacteriocins produced by food grade lactic acid bacteria exhibit the potential to control spoilage and pathogenic bacteria in food. Here we review the means by which these Bacteriocins are employed by the food industry, that is through the production of Bacteriocins by Bacteriocinogenic bacteria from within the food or by the addition of a Bacteriocin to the food in the form of an ingredient or preservative.

  • Antimicrobials for food and feed; a Bacteriocin perspective.
    Current Opinion in Biotechnology, 2020
    Co-Authors: Paula M. O'connor, Colin Hill, R.p. Ross, Taís Mayumi Kuniyoshi, R.p.s. Oliveira, Paul D. Cotter

    Abstract:

    Bacteriocins are natural antimicrobials that have been consumed via fermented foods for millennia and have been the focus of renewed efforts to identify novel Bacteriocins, and their producing microorganisms, for use as food biopreservatives and other applications. Bioengineering Bacteriocins or combining Bacteriocins with multiple modes of action (hurdle approach) can enhance their preservative effect and reduces the incidence of antimicrobial resistance. In addition to their role as food biopreservatives, Bacteriocins are gaining credibility as health modulators, due to their ability to regulate the gut microbiota, which is strongly associated with human wellbeing. Indeed the strengthening link between the gut microbiota and obesity make Bacteriocins ideal alternatives to Animal Growth Promoters (AGP) in animal feed also. Here we review recent advances in Bacteriocin research that will contribute to the development of functional foods and feeds as a consequence of roles in food biopreservation and human/animal health.

  • Bacteriocin production a probiotic trait
    Applied and Environmental Microbiology, 2012
    Co-Authors: Alleson Dobson, Paul D. Cotter, Paul R Ross, Colin Hill

    Abstract:

    Bacteriocins are an abundant and diverse group of ribosomally synthesized antimicrobial peptides produced by bacteria and archaea. Traditionally, Bacteriocin production has been considered an important trait in the selection of probiotic strains, but until recently, few studies have definitively demonstrated the impact of Bacteriocin production on the ability of a strain to compete within complex microbial communities and/or positively influence the health of the host. Although research in this area is still in its infancy, there is intriguing evidence to suggest that Bacteriocins may function in a number of ways within the gastrointestinal tract. Bacteriocins may facilitate the introduction of a producer into an established niche, directly inhibit the invasion of competing strains or pathogens, or modulate the composition of the microbiota and influence the host immune system. Here we review the role of Bacteriocin production in complex microbial communities and their potential to enhance human health.

H Holo – 3rd expert on this subject based on the ideXlab platform

  • Bacteriocin diversity in streptococcus and enterococcus
    Journal of Bacteriology, 2007
    Co-Authors: D B Diep, H Holo

    Abstract:

    Most Bacteriocins in gram-positive bacteria are small and heat stable (peptide Bacteriocins), and their antimicrobial activities are directed against a broader spectrum of bacteria than is seen for Bacteriocins of gram-negative bacteria. Many excellent Bacteriocin reviews have been published in recent years (10, 15, 16, 19, 27, 29, 77, 83). The heat-stable peptide Bacteriocins from lactic acid bacteria have so far been grouped into two major classes: class I, the lantibiotics, and class II, the heat-stable nonlantibiotics. In addition, a third class of Bacteriocins has been suggested which includes secreted heat-labile cell wall-degrading enzymes (71, 88), but classification of such enzymes as Bacteriocins has recently been disputed (19, 49). Lantibiotics contain a number of posttranslational modifications that include dehydration of serine and threonine to form 2,3dehydroalanine (Dha) and 2,3-dehydrobutyrine (Dhb), respectively. Some of the dehydrated residues are covalently bound to the sulfur in neighboring cysteines, creating the characteristic lantionine and methyllantionine residues. It has also been shown that in a few cases the dehydroalanine can be converted to D-alanine (109, 118) and that additional modifications, such as lysinoalanine, 2-oxobutyrate, S-aminovinyl-D-cysteine, and S-aminovinyl-D-methylcysteine, are formed in some lantibiotics (59). Both class I and class II Bacteriocins display great diversity with regard to their modes of action, structures, genetics, modes of secretion, choices of target organisms, etc. There is still lack of consensus on how to subdivide class I and II peptide Bacteriocins further into subclasses. The lantibiotics have been divided into two subgroups, type A and type B, according to structural features (64). Type A lantibiotics (e.g., nisin, subtilin, and Pep5) are elongated molecules with a flexible structure in solution, while type B lantibiotics adapt a more rigid and globular structure (64). However, this picture is changing, since structural studies of the lantibiotic plantaricin C has been shown to hold structural elements of both type A and B lantibiotics (123). Also, nuclear magnetic resonance spectroscopy has shown that the peptides of the two-peptide lantibiotic lacticin 3247 are structurally different. While the peptide designated lacticin 3147 A1 has a specific lanthionine bridging pattern resembling the globular type B lantibiotic mersacidin, the A2 peptide is a member of the elongated type A lantibiotic subclass (80). In the present review, we refer to the A and B types of lantibiotics as one-peptide lantibiotics and mention specifically when a Bacteriocin is a two-peptide lantibiotic. Lack of consensus also exists in the differentiation between subgroups of the nonlantibiotic class II peptide Bacteriocins. In this review, we retain the pediocin-like Bacteriocin in class IIa, the two-peptide Bacteriocins in class IIb, and the leaderless peptide Bacteriocins in class IIc, and finally, we define the circular Bacteriocins as class IId. This overview will discuss the dissemination of the class I and II peptide Bacteriocins in enterococci and streptococci and the possibility of identifying such Bacteriocins in genome sequences. The lactic acid bacteria in fermented food have been the focus of Bacteriocin research during the last 15 to 20 years. Numerous peptide Bacteriocins have been characterized, and many have been used intentionally or unintentionally in food

  • enterocin b a new Bacteriocin from enterococcus faecium t136 which can act synergistically with enterocin a
    Microbiology, 1997
    Co-Authors: P Casaus, Pablo E. Hernández, Luis M. Cintas, Trine Nilsen, H Holo

    Abstract:

    Summary: The strain Enterococcus faecium T136 produces two Bacteriocins, enterocin A, a member of the pediocin family of Bacteriocins, and a new Bacteriocin termed enterocin B. The N-terminal amino acid sequences of enterocins A and B were determined, and the gene encoding enterocin B was sequenced. The primary translation product was a 71 aa peptide containing a leader peptide of the double-glycine type which is cleaved off to give mature enterocin B of 53 aa. Enterocin B does not belong to the pediocin family of Bacteriocins and shows strong homology to carnoBacteriocin A. However, sequence similarities in their leader peptides and C-termini suggest that enterocin B and carnoBacteriocin A are related to Bacteriocins of the pediocin family. Enterocins A and B had only slightly different inhibitory spectra, and both were active against a wide range of Gram-positive bacteria, including listeriae, staphylococci and most lactic acid bacteria tested. Both had bactericidal activities, but survival at a frequency of 10-44-10-2 was observed when sensitive cultures were exposed to either Bacteriocin. The number of survivors was drastically reduced when a mixture of the two Bacteriocins was added to the cells.

  • Biosynthesis of Bacteriocins in lactic acid bacteria
    Antonie Van Leeuwenhoek International Journal of General and Molecular Microbiology, 1996
    Co-Authors: D B Diep, L S Håvarstein, M B Brurberg, V Eijsink, H Holo

    Abstract:

    A large number of new Bacteriocins in lactic acid bacteria (LAB) has been characterized in recent years. Most of the new Bacteriocins belong to the class II Bacteriocins which are small (30–100 amino acids) heat-stable and commonly not post-translationally modified. While most Bacteriocin producers synthesize only one Bacteriocin, it has been shown that several LAB produce multiple Bacteriocins (2–3 Bacteriocins).