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PubMed2026

Genomic Insights Into the Probiotic and Safety Attributes of Pediococcus acidilactici BC-7 for its Potential Application in Livestock Health.

Pediococcus acidilactici is widely recognized for its health-beneficial aspects and has gained increasing interest for use in livestock industry. It shows strong probiotic efficacy, antimicrobial activity, cholesterol-lowering potential, immune modulation, and other therapeutic attributes. The novel strain from indigenous habitats mainly depicted potent probiotic efficacy and high adaptability. In this study, we evaluated the probiotic characteristics and genomic features of strain BC-7 obtained from a Nili - Ravi buffalo calf raised under domestic conditions using phenotypic assessment, genomic analysis and in vivo studies. The strain BC-7 exhibited key probiotic traits i.e., gut tolerance (70.43% - 97.5%), auto-aggregation (85.24%), co-aggregation (14.33% - 25.88%), hydrophobicity (78.33% - 88%), antioxidant potential (54%), and antibacterial activity (16.47-18 mm). The safety analysis revealed that BC-7 exhibited susceptibility and resistance to various antimicrobial agents and showed no β hemolytic activity. BC-7 was taxonomically classified as Pediococcus acidilactici by 16 S rRNA gene sequencing. Whole genome sequence (WGS) analysis showed that P. acidilactici BC-7 contains a 1.9 Mb genome with 42% GC content. Pediococccus acidilactici BC-7 harbored 1900 genes, which were mainly associated with metabolism and genetic processes. Based on genomic comparison, BC-7 shared 99% average nucleotide identity and strong genomic collinearity with P. acidilactici NARCC1 which is a TYPE strain having potent probiotic potential. Probiotic strain BC-7 shared 1,664 core genes with reference strains and 69 unique genes specific for metabolism and genetic processes. The BC-7 strain contained unique bacteriocins-associated genes and defense-related CAzymes, it harbors only vancomycin resistance genes and lacked true virulence determinants. In vivo trial showed that BC-7 treated mice showed increased growth rate, improved immune modulation, and membrane integrity. These significant findings revealed that BC-7 emerging as a potential probiotic strain with strong functionality and efficacy. Thus, our strain BC-7 could be used as a promising candidate for applications in the animal health industry.

Gastrointestinal tract↗
PubMed1999

Induction and characterization of Pediococcus acidilactici temperate bacteriophage

Mitomycin C was used to induce temperate bacteriophage from three strains of Pediococcus acidilactici. The new bacteriophage, designated pa97, pa40, and pa42, were characterized based on morphology, DNA homology, and major protein profiles. Morphological attributes (small isometric heads with non-contractile tails) place these bacteriophages within the B1 group of the family Siphovirdae. Restriction endonuclease digests suggested that the bacteriophage genomes were linear molecules without cohesive ends, and between 33 and 37 kilobases in length. All three bacteriophages possessed one major protein with an estimated mass of 30 to 35 kilodaltons. Bacteriophage pa42 also contained a second major protein of approximately 47 kilodaltons. DNA-DNA hybridization showed bacteriophages pa40 and pa42 were homologous to each other, but not to pa97, suggesting that Pediococcus acidilactici bacteriophage fall into at least two different species.

Journal Article↗
PubMed1985

Association of a 13.6-Megadalton Plasmid in Pediococcus pentosaceus with Bacteriocin Activity.

Pediococcus pentosaceus FBB61 and L7230, isolated from cucumber fermentations, produced a bacteriocin, designated pediocin A, which had identical activity spectra against species of Pediococcus, Clostridium, Staphylococcus, and Streptococcus. Both strains possessed a 13.6-megadalton plasmid (pMD136). Plasmid curing experiments suggested that both bacteriocin immunity and production determinants were encoded by pMD136. Use of pediocin-producing strains in food fermentations is discussed.

Journal Article↗
PubMed1992

Assessment of Pediococcus acidilactici as a Potential Silage Inoculant.

Eighteen Pediococcus strains were screened for their potential as silage inoculants. Pediococcus acidilactici G24 was found to be the most suitable, exhibiting a short lag phase on both glucose and fructose, a rapid rate of acid production, a high sugar-to-lactate conversion efficiency, no detectable breakdown of proteins or lactic acid, and the ability to grow within a broad range of pH and temperature. When tested in laboratory silos using grass with a water-soluble carbohydrate content of 24 g/kg of aqueous extract, P. acidilactici G24 stimulated the natural Lactobacillus plantarum population and accelerated the rates of lactic acid production and pH decrease. After 6 days of fermentation, the inoculated silage exhibited a 12% decrease in ammonia nitrogen and an 11% increase in crude protein levels compared with uninoculated controls. The use of an L. plantarum inoculant at a rate of 10 bacteria per g of grass in conjunction with P. acidilactici G24 produced no additional beneficial effect. Inoculation of grass with a water-soluble carbohydrate level of 8 g/kg of aqueous extract with P. acidilactici G24 led to no acceleration in the rate of L. plantarum growth or pH decrease. However, after 7 days of fermentation the inoculated silage had a 14% lower ammonia nitrogen protein content than did uninoculated controls. The results suggest that P. acidilactici G24 may be useful as a silage inoculant for crops with a sufficiently high water-soluble carbohydrate level.

Journal Article↗
PubMed1999

The development of bactericidal yeast strains by expressing the Pediococcus acidilactici pediocin gene (pedA) in Saccharomyces cerevisiae.

The excessive use of sulphur dioxide and other chemical preservatives in wine, beer and other fermented food and beverage products to prevent the growth of unwanted microbes holds various disadvantages for the quality of the end-products and is confronted by mounting consumer resistance. The objective of this study was to investigate the feasibility of controlling spoilage bacteria during yeast-based fermentations by engineering bactericidal strains of Saccharomyces cerevisiae. To test this novel concept, we have successfully expressed a bacteriocin gene in yeast. The pediocin operon of Pediococcus acidilactici PAC1.0 consists of four clustered genes, namely pedA (encoding a 62 amino acid precursor of the PA-1 pediocin), pedB (encoding an immunity factor), pedC (encoding a PA-1 transport protein) and pedD (encoding a protein involved in the transport and processing of PA-1). The pedA gene was inserted into a yeast expression/secretion cassette and introduced as a multicopy episomal plasmid into a laboratory strain (Y294) of S. cerevisiae. Northern blot analysis confirmed that the pedA structural gene in this construct (ADH1P-MFa1S-pedA-ADH1T, designated PED1), was efficiently expressed under the control of the yeast alcohol dehydrogenase I gene promoter (ADH1P) and terminator (ADH1T). Secretion of the PED1-encoded pediocin PA-1 was directed by the yeast mating pheromone alpha-factor's secretion signal (MFa1S). The presence of biologically active antimicrobial peptides produced by the yeast transformants was indicated by agar diffusion assays against sensitive indicator bacteria (e.g. Listeria monocytogenes B73). Protein analysis indicated the secreted heterologous peptide to be approximately 4.6 kDa, which conforms to the expected size. The heterologous peptide was present at relatively low levels in the yeast supernatant but pediocin activity was readily detected when intact yeast colonies were used in sensitive strain overlays. This study could lead to the development of bactericidal yeast strains where S. cerevisiae starter cultures not only conduct the fermentations in the wine, brewing and baking industries but also act as biological control agents to inhibit the growth of spoilage bacteria.

Bacteriocins↗
PubMed2001

Optimum production, stability, partial purification and inhibitory spectrum of antimicrobial compounds produced by Pediococcus pentosaceus DI.

The optimum conditions for production of antimicrobial compounds by Pediococcus pentosaceus DI were studied. The antimicrobial compounds in cell free fermented medium were extracted (methanol-acetone), then tested for inhibitory activity against fourteen bacterial strains and its stability to heating, various pH and proteolytic enzymes. In addition, methanol-acetone extract was partial purified through Sephadex G-100 column and thin-layer chromatography. Production of antimicrobial compounds were maximized when P. pentosaceus DI was grown in lactobacilli MRS containing 0.05% L-cysteine-HCl medium at 30 degrees C for 48 h. The methanol-acetone extract showed relatively broad antimicrobial spectrum including lactic acid bacteria and some spoilage and pathogenic bacteria. Antimicrobial activity of methanol-acetone extract was retained after heating (100 degrees C for 30 min) at pH 2.5 to 6.0 but was lost after treating with several proteolytic enzymes at pH 6.5 and 7.0. Sephadex G-100 column revealed three peaks in methanol-acetone extract. The major peak was eluted at 40 ml and including three fractions, which exhibited inhibitory activity, while the other peaks were principally free from any antimicrobial compounds. Thin-layer chromatography of crude methanol-acetone extract and the three fractions, which exhibited inhibitory activity, showed that there was one main spot with Rf at 0.8.

Bacteria↗
PubMed2000

Analysis of the genetic determinant for production of the pediocin P of Pediococcus pentosaceus Pep1.

Pediococcus pentosaceus Pep1 is a vacuum-packaged Turkish sausage isolate which produces a potentially novel bacteriocin of the pediocin (anti-Listeria) family of peptides designated as pediocin P. Curing experiments and plasmid profile analysis indicated that both bacteriocin immunity and production determinants were linked and encoded by 9.0 MDa plasmid, pHD1.0. Attempts to transform purified plasmid pHD1.0 into recipient Escherichia coli JM109 cells by electroporation were successful but none of the E. coli JM109 cells were able to express and/or release pediocin P. However, P. pentosaceus PC, a plasmid-cured variant of P. pentosaceus Pep1 was successfully transformed with pHD1.0 by electroporation and Bac-Bacs P. pentosaceus PC cells restarted to express and/or release pediocin P again as indicated by the presence of zone of growth inhibition of L. plantarum NCDO 955 around colonies.

Bacteriocins↗
PubMed2004

Pediocin production by Pediococcus acidilactici in solid state culture on a waste medium: process simulation and experimental results.

The production of pediocin by Pediococcus acidilactici was comparatively studied in submerged and solid-state culture, using polyurethane foam particles soaked in commercial (MRS) and waste media with various supplements, where product concentrations were 15 times higher in MRS medium. For the solid state analysis, cultures were treated by successive compression and refilling of tubular minireactors equipped with a piston, without the need for reinoculation. This method was found to be simple, reproducible, and easily controllable, allowing culture productivity to be maintained for long periods of time without alterations in the basic properties of the system. In addition, yields were found to be superior compared to those from submerged culture. The system kinetics were modeled on the basis of widely accepted assumptions with a good fit to the experimental results and observed biomass fluctuations less evident than those predicted by the kinetic model.

Bacteriocins↗
PubMed2000

Nucleotide sequence and analysis of plasmid pMD136 from Pediococcus pentosaceus FBB61 (ATCC43200) involved in pediocin A production.

The complete sequence of the 19515-bp plasmid pMD136 from Pediococcus pentosaceus FBB61 (ATCC43200) has been determined. This plasmid is involved in Pediocin A production, a bacteriocin active against a wide range of gram-positive bacteria. It appears to replicate via a theta mechanism, with structures closely related to those of many lactococcal plasmids. Genes homologous to mobilization functions are also present, which are similar in sequence and arrangement to mobA, mobB, and mobC of some staphylococcal plasmids, although the last one contains a deletion in its central part. The region involved in bacteriocin activity has been limited to a 9.4-kb fragment, containing 10 open reading frames organized in a single operon. Since Pediocin A has a molecular weight of about 80 kDa (Piva and Headon, Microbiology, 140, 697-702, 1994), and a gene long enough to encode it is not present in pMD136, it is proposed that genes residing on the plasmid are responsible for the regulation of bacteriocinogenic activity. Gene arrangement and sequence homologies suggest the presence of a two-component-like regulatory mechanism.

Amino Acid Sequence↗
PubMed1990

Non-PTS uptake and subsequent metabolism of glucose in Pediococcus halophilus as demonstrated with a double mutant defective in phosphoenolpyruvate:mannose phosphotransferase system and in phosphofructokinase.

Pediococcus halophilus possesses phosphoenolpyruvate:mannose phosphotransferase system (man:PTS) as a main glucose transporter. A man:PTS defective (man:PTSd) strain X-160 could, however, utilize glucose. A possible glucose-transport mechanism other than PTS was studied with the strain X-160 and its derivative, man:PTSd phosphofructokinase defective (PFK-) strain M-13. Glucose uptake by X-160 at pH 5.5 was inhibited by any of carbonylcyanide m-chlorophenylhydrazone, nigericin, N,N'-dicyclohexylcarbodiimide, or iodoacetic acid. The double mutant M-13 could still transport glucose and accumulated intracellularly a large amount of hexose-phosphates (ca. 8 mM glucose 6-phosphate and ca. 2 mM fructose 6-phosphate). Protonophores also inhibited the glucose transport at pH 5.5, as determined by the amounts of accumulated hexose-phosphates (less than 4 mM). These showed involvement of proton motive force (delta P) in the non-PTS glucose transport. It was concluded that the non-PTS glucose transporter operated in concert with hexokinase or glucokinase for the metabolism of glucose in the man:PTSd strain.

Biological Transport, Active↗
PubMed1991

Release of glucose-mediated catabolite repression due to a defect in the membrane fraction of phosphoenolpyruvate: mannose phosphotransferase system in Pediococcus halophilus.

A spontaneous mutant 9R-4 resistant to 2-deoxyglucose (2DG) was derived from a wild-type strain Pediococcus halophilus I-13. Phosphoenolpyruvate (PEP)-dependent glucose-6-phosphate formation by the permeabilized 9R-4 cells was less than 5% of that observed with the parent I-13. In vitro complementation of PEP-dependent 2DG-6-phosphate formation was assayed with combination of the cytoplasmic and membrane fractions prepared from the I-13 and the mutants (9R-4, and X-160 isolated from nature), which were defective in PEP:mannose phosphotransferase system (man:PTS). The defects in man:PTS of both the strain 9R-4 and X-160 were restricted to the membrane fraction (e.g. EIIman), not to the cytoplasmic one. Kinetic studies on the glucose transport with intact cells and iodoacetate-treated cells also supported the presence of two distinct transport systems in this bacterium as follows: (i) The wild-type I-13 possessed a high-affinity man:PTS (Km = 11 microM) and a low-affinity proton motive force driven glucose permease (GP) (Km = 170 microM). (ii) Both 9R-4 and X-160 had only the low-affinity system (Km = 181 microM for 9R-4, 278 microM for X-160). In conclusion, a 2DG-induced selective defect in the membrane component (EIIman) of the man:PTS could partially release glucose-mediated catabolite repression but not fructose-mediated catabolite repression in soy pediococci.

Biological Transport↗
PubMed1992

Septicemia and hepatic abscess caused by Pediococcus acidilactici.

A case of postoperative Pediococcus acidilactici septicemia with parallel isolation of the organism from hepatic specimens is presented. Laboratory methods to identify this vancomycin-resistant gram-positive cocci are described. Very few cases of documented infections due to this bacterium have been reported in the literature.

Humans↗
PubMed2004

Isolation and partial characterization of bacteriocins from Pediococcus species.

Lactic acid bacteria have received increased attention as a potential food preservative due to their strong antagonistic activity against many food-spoilage and pathogenic organisms. Three Pediococcus species, P. acidilactici NCIM 2292 , P. pentosaceous. NCIM 2296 and P. cervisiae NCIM 2171, were evaluated for bacteriocin production. Inhibitory substance were produced during the late growth phase and maximum production occurred at 37 degrees after 36-48 h of incubation. Bacteriocins partially purified from these species by cold-acetone precipitation at 0 degrees C and cell adsorption desorption techniques have a broad inhibitory spectrum against microorganisms, including gram-negative bacteria such as Escherichia coli and Pseudomonas. Proteolytic enzymes inactivated these peptides, but amylase and lipase did not show any effect. The bacteriocins were stable over a wide pH range (3-8) and apparently most active at pH 4.0-5.0. They were heat-stable (1 h at approximately 80 degrees C and autoclaving) at pH 5.0. No loss in activity was observed when stored under refrigeration (4-8 degrees C). Tris-Tricine SDS-PAGE revealed the molecular masses of these peptides to be between 3.5 and 5.0 kDa.

Amylases↗
PubMed2002

Multilocus hybridization typing in Pediococcus acidilactici strains.

In previous a study we demonstrated the presence of several genomic subpopulations within a collection of Pediococcus acidilactici strains isolated from different environments, through a multilocus typing analysis taking into consideration housekeeping conserved loci and protein coding genes of the primary metabolism. In this study, representative strains of five genomic subpopulations previously described (I, II, III, V, VII) were analyzed by restriction analysis of chromosomal DNA and subsequent hybridization assays using as probes amplified fragments obtained from five housekeeping genes (16S rDNA, rpoC, ldhD, ldhL, and metS). A computer similarity and clustering analysis of hybridization data showed the subdivision of P. acidilactici strains in five distinct genotypes according to the grouping previously obtained confirming that pediocin AcH/PA-1 producer strains represent one genomic lineage within the species P. acidilactici.

5-Methyltetrahydrofolate-Homocysteine S-Methyltran↗
PubMed1997

Molecular analysis of the replication region of the theta-replicating plasmid pUCL287 from Tetragenococcus (Pediococcus) halophilus ATCC33315.

The complete nucleotide sequence of the 8.7-kb theta-replicating plasmid pUCL287 from Tetragenococcus halophilus (formerly Pediococcus halophilus) ATCC33315 has been determined. The replication region was identified and analyzed. Its nucleotide sequence contains an untranslated region, the replication origin, followed by two open reading frames (ORFs) encoding two proteins of 311 (RepA287) and 168 (RepB287) amino acids, respectively. Evidence is presented to show that RepA287 represents the plasmid replication protein. RepB287, which is non-essential for replication, is involved in the plasmid copy-number control and segregational stability. The roles of lactococcal proteins homologous to RepB287 have not been defined so far. Nevertheless, the structural organization of the pUCL287 replication region is remarkably similar to those of well known theta-replicating lactococcal plasmids despite the absence of homology of the replication origin and of the replication protein, and this suggests that pUCL287 uses the same mechanism of replication. Nucleotide sequence comparisons show that pSMB74, a pediococcal plasmid encoding bacteriocin production, is a member of the pUCL287 replicon family.

Amino Acid Sequence↗
PubMed1992

Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0.

The plasmid-encoded bacteriocin pediocin PA-1, produced by the gram-positive bacterium Pediococcus acidilactici strain PAC-1.0, was purified to homogeneity. The purified product exhibited antibacterial activity against several gram-positive bacterial strains, including the food pathogen Listeria monocytogenes. Pediocin PA-1 is a 4629-Da peptide with 44 amino acids and two disulfide bonds. The amino acid sequence and arrangement of the disulfide bonds were determined. Sequence data were used to calculate an isoelectric point of 10.0. The small and basic nature of PA-1 is comparable to several other bacteriocins produced by gram-positive bacteria. Reported sequences of other bacteriocins and of other antimicrobial peptides from diverse origins bear no resemblance to the sequence reported here.

Amino Acid Sequence↗
PubMed1990

Structure of an exocellular beta-D-glucan from Pediococcus sp., a wine lactic bacteria.

Pediococcus sp. produces an exocellular slime containing exclusively D-glucose. The structure of the polysaccharide was determined by methylation analysis, Smith degradation, enzymic hydrolysis, and 13C-n.m.r. spectroscopy as having a trisaccharide repeating unit, ----3)-beta-D-Glcp-(1---- 3)-[beta-D-Glcp-(1----2)]-beta-D-Glcp-(1----.

Carbohydrate Sequence↗
PubMed1991

Septicaemia caused by Pediococcus pentosaceus: a new opportunistic pathogen.

A case of septicaemia caused by Pediococcus pentosaceus is described. The role played by pediococci, and other vancomycin-resistant Gram-positive cocci, in disease states is examined. We suggest that in immunocompromised patients these organisms act as opportunist pathogens. This would appear to be the first reported case of P. pentosaceus septicaemia.

Ampicillin↗