Bacteriocin

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Myeong Su Shin - One of the best experts 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 - One of the best experts 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, R.p. Ross, Colin Hill, 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.

  • Bacteriocins: Biological tools for bio-preservation and shelf-life extension
    International Dairy Journal, 2006
    Co-Authors: Lucy H. Deegan, Paul D. Cotter, Colin Hill, Paul Ross
    Abstract:

    The lactococcal Bacteriocin named nisin (or group N inhibitory substance) was first marketed in England in 1953 and since then has been approved for use in over 48 countries. The successful development of nisin from an initial biological observation through regulatory approval to commercial application is a model that has stimulated significant resurgence in Bacteriocin research in recent years, but similar success is yet to be repeated on the same scale. In spite of this sobering fact, we remain convinced that Bacteriocins can be exploited in foods in a variety of imaginative and commercially significant applications in bio-preservation and shelf-life extension. However, in order to fully realise this potential, it is necessary to understand the biology of Bacteriocins; in particular, to elucidate structure-function relationships, production, immunity, regulation and mode of action. In this paper, we will discuss some of the advances, made mainly with other lactococcal Bacteriocins, in improving food safety, food quality and preventing food spoilage. © 2006 Elsevier Ltd. All rights reserved.

  • potential of Bacteriocin producing lactic acid bacteria for improvements in food safety and quality
    Biochimie, 2002
    Co-Authors: R.p. Ross, Lisa Osullivan, Colin Hill
    Abstract:

    Abstract Lactic acid bacteria (LAB) have been used for centuries in the fermentation of a variety of dairy products. The preservative ability of LAB in foods is attributed to the production of anti-microbial metabolites including organic acids and Bacteriocins. Bacteriocins generally exert their anti-microbial action by interfering with the cell wall or the membrane of target organisms, either by inhibiting cell wall biosynthesis or causing pore formation, subsequently resulting in death. The incorporation of Bacteriocins as a biopreservative ingredient into model food systems has been studied extensively and has been shown to be effective in the control of pathogenic and spoilage microorganisms. However, a more practical and economic option of incorporating Bacteriocins into foods can be the direct addition of Bacteriocin-producing cultures into food. This paper presents an overview of the potential for using Bacteriocin-producing LAB in foods for the improvement of the safety and quality of the final product. It describes the different genera of LAB with potential as biopreservatives, and presents an up-to-date classification system for the Bacteriocins they produce. While the problems associated with the use of some Bacteriocin-producing cultures in certain foods are elucidated, so also are the situations in which incorporation of the Bacteriocin-producer into model food systems have been shown to be very effective.

H Holo - One of the best experts 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).

  • Biosynthesis of Bacteriocins in lactic acid bacteria.
    Antonie van Leeuwenhoek, 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). Based on common features, some of the class II Bacteriocins can be divided into separate groups such as the pediocin-like and strong anti-listeria Bacteriocins, the two-peptide Bacteriocins, and Bacteriocins with a sec-dependent signal sequence. With the exception of the very few Bacteriocins containing a sec-dependent signal sequence, class II Bacteriocins are synthesized in a preform containing an N-terminal double-glycine leader. The double-glycine leader-containing Bacteriocins are processed concomitant with externalization by a dedicated ABC-transporter which has been shown to possess an N-terminal proteolytic domain. The production of some class II Bacteriocins (plantaricins of Lactobacillus plantarum C11 and sakacin P of Lactobacillus sake) have been shown to be transcriptionally regulated through a signal transduction system which consists of three components: an induction factor (IF), histidine protein kinase (HK) and a response regulator (RR). An identical regulatory system is probably regulating the transcription of the sakacin A and carnoBacteriocin B2 operons. The regulation of Bacteriocin production is unique, since the IF is a Bacteriocin-like peptide with a double-glycine leader processed and externalized most probably by the dedicated ABC-transporter associated with the Bacteriocin. However, IF is not constituting the Bacteriocin activity of the bacterium, IF is only activating the transcription of the regulated class II Bacteriocin gene(s). The present review discusses recent findings concerning biosynthesis, genetics, and regulation of class II Bacteriocins.

  • biochemical and genetic characterization of enterocin a from enterococcus faecium a new antilisterial Bacteriocin in the pediocin family of Bacteriocins
    Applied and Environmental Microbiology, 1996
    Co-Authors: Teresa Aymerich, Marta Hugas, L S Håvarstein, H Holo, Margarita Garriga
    Abstract:

    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 structure of enterocin A was determined. It consists of 47 amino acid residues, and the molecular weight was calculated to be 4,829, assuming that the four cysteine residues form intramolecular disulfide bridges. This molecular weight was confirmed by mass spectrometry analysis. The amino acid sequence of enterocin A shared significant homology with a group of Bacteriocins (now termed pediocin-like Bacteriocins) isolated from a variety of lactic acid-producing bacteria, which include members of the genera Lactobacillus, Pediococcus, Leuconostoc, and Carnobacterium. Sequencing of the structural gene of enterocin A, which is located on the bacterial chromosome, revealed an N-terminal leader sequence of 18 amino acid residues, which was removed during the maturation process. The enterocin A leader belongs to the double-glycine leaders which are found among most other small nonlantibiotic Bacteriocins, some lantibiotics, and colicin V. Downstream of the enterocin A gene was located a second open reading frame, encoding a putative protein of 103 amino acid residues. This gene may encode the immunity factor of enterocin A, and it shares 40% identity with a similar open reading frame in the operon of leucocin AUL 187, another pediocin-like Bacteriocin.

Svetoslav Dimitrov Todorov - One of the best experts on this subject based on the ideXlab platform.

  • Bacteriocinogenic LAB Strains for Fermented Meat Preservation: Perspectives, Challenges, and Limitations
    Probiotics and Antimicrobial Proteins, 2017
    Co-Authors: Lorenzo Favaro, Svetoslav Dimitrov Todorov
    Abstract:

    Over the last decades, much research has focused on lactic acid bacteria (LAB) Bacteriocins because of their potential as biopreservatives and their action against the growth of spoilage microbes. Meat and fermented meat products are prone to microbial contamination, causing health risks, as well as economic losses in the meat industry. The use of Bacteriocin-producing LAB starter or protective cultures is suitable for fermented meats. However, although Bacteriocins can be produced during meat processing, their levels are usually much lower than those achieved during in vitro fermentations under optimal environmental conditions. Thus, the direct addition of a Bacteriocin food additive would be desirable. Moreover, safety and technological characteristics of the Bacteriocinogenic LAB must be considered before their widespread applications. This review describes the perspectives and challenges toward the complete disclosure of new Bacteriocins as effective preservatives in the production of safe and “healthy” fermented meat products.

  • novel Bacteriocinogenic enterococcus hirae and pediococcus pentosaceus strains with antilisterial activity isolated from brazilian artisanal cheese
    Journal of Dairy Science, 2017
    Co-Authors: Valeria Quintana Cavicchioli, Svetoslav Dimitrov Todorov, Anderson Carlos Camargo, Luis Augusto Nero
    Abstract:

    ABSTRACT We isolated and characterized Bacteriocin producers Enterococcus hirae ST57ACC and Pediococcus pentosaceus ST65ACC from raw milk artisanal cheeses. Their Bacteriocins were tolerant to temperatures from 4°C to 100°C and under sterilization conditions (121°C for 15 min). Additionally, the tested Bacteriocins remained active after being exposed to pH 2.0 to 10.0 for 2 h. The activity of the Bacteriocins was affected by proteolytic enzymes but remained stable after treatment with EDTA, sodium dodecyl sulfate, NaCl, skim milk, and Tween 80. Cell-free supernatants were capable of inhibiting Listeria innocua and several strains of Listeria monocytogenes obtained from different sources and belonging to different serotypes. When L. monocytogenes 211 and L. monocytogenes 422 were treated with Bacteriocins, growth was completely inhibited over 12 h. Cocultures of Bacteriocinogenic strains and L. monocytogenes 422 in skim milk showed that E. hirae ST57ACC could control the growth of the pathogen in the matrix after 48 h. None of the selected isolates presented positive results on a screening panel for 25 Bacteriocin-related genes, however, indicating that both strains might express novel Bacteriocins.

  • Characterization of a novel Bacteriocin produced by Lactobacillus plantarum ST8SH and some aspects of its mode of action
    Annals of Microbiology, 2016
    Co-Authors: Svetoslav Dimitrov Todorov, Wilhelm Holzapfel, Luis Augusto Nero
    Abstract:

    Bacteriocins produced by lactic acid bacteria (LAB) are ribosomally synthesized antimicrobial peptides, with a diverse mode of bactericidal activity. This study focused on characterization of the bactericidal activity of Bacteriocin ST8SH, with special attention to control of Listeria and Enteroccus species. Lactobacillus plantarum ST8SH produces a Bacteriocin of the pediocin PA-1 family (sharing 96 % similarity on genetic level) with activity against several LAB, Enterococcus spp., Klebsiella pneumoniae , Listeria spp., Streptococcus spp. and some other human and foodborne pathogens. Addition of Bacteriocin ST8SH to exponential or stationary phase cultures of L. monocytogenes ScottA and E. faecalis ATCC 19433 inhibited growth for 12 h. The effects of Bacteriocin ST8SH on L. monocytogenes ScottA and E. faecalis ATCC 19433 were recorded indirectly based on enzyme, protein and nucleotide material leakage. Considering the antimicrobial activity of Bacteriocin ST8SH against the tested microorganisms, and the physiological characteristics of Lb. plantarum ST8SH, either the Bacteriocin or the strain may be used as tools for biopreservation.

Iddo Friedberg - One of the best experts on this subject based on the ideXlab platform.

  • a large scale prediction of Bacteriocin gene blocks suggests a wide functional spectrum for Bacteriocins
    BMC Bioinformatics, 2015
    Co-Authors: James T Morton, Stefan D Freed, Iddo Friedberg
    Abstract:

    Background Bacteriocins are peptide-derived molecules produced by bacteria, whose recently-discovered functions include virulence factors and signaling molecules as well as their better known roles as antibiotics. To date, close to five hundred Bacteriocins have been identified and classified. Recent discoveries have shown that Bacteriocins are highly diverse and widely distributed among bacterial species. Given the heterogeneity of Bacteriocin compounds, many tools struggle with identifying novel Bacteriocins due to their vast sequence and structural diversity. Many Bacteriocins undergo post-translational processing or modifications necessary for the biosynthesis of the final mature form. Enzymatic modification of Bacteriocins as well as their export is achieved by proteins whose genes are often located in a discrete gene cluster proximal to the Bacteriocin precursor gene, referred to as context genes in this study. Although Bacteriocins themselves are structurally diverse, context genes have been shown to be largely conserved across unrelated species.

  • a large scale prediction of Bacteriocin gene blocks suggests a wide functional spectrum for Bacteriocins
    arXiv: Genomics, 2015
    Co-Authors: James T Morton, Stefan D Freed, Iddo Friedberg
    Abstract:

    Bacteriocins are peptide-derived molecules produced by bacteria, whose recently-discovered functions include virulence factors and signalling molecules as well as their better known roles as antibiotics. To date, close to five hundred Bacteriocins have been identified and classified. Recent discoveries have shown that Bacteriocins are highly diverse and widely distributed among bacterial species. Given the heterogeneity of Bacteriocin compounds, many tools struggle with identifying novel Bacteriocins due to their vast sequence and structural diversity. Many Bacteriocins undergo post-translational processing or modifications necessary for the biosynthesis of the final mature form. Enzymatic modification of Bacteriocins as well as their export is achieved by proteins whose genes are often located in a discrete gene cluster proximal to the Bacteriocin precursor gene, referred to as \textit{context genes} in this study. Although Bacteriocins themselves are structurally diverse, context genes have been shown to be largely conserved across unrelated species. Using this knowledge, we set out to identify new candidates for context genes which may clarify how Bacteriocins are synthesized, and identify new candidates for Bacteriocins that bear no sequence similarity to known toxins. To achieve these goals, we have developed a software tool, Bacteriocin Operon and gene block Associator (BOA) that can identify homologous Bacteriocin associated gene clusters and predict novel ones. We discover that several phyla have a strong preference for bactericon genes, suggesting distinct functions for this group of molecules. Availability: this https URL