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PubMed1997

Purification of bacteriocins of lactic acid bacteria: problems and pointers.

Bacteriocins of lactic acid bacteria have been widely studied in recent years. However, there are relatively few studies that describes their biochemical structure. This study may be due to the many challenges associated with the purification of these antimicrobial peptides. This review focuses on the purification procedures used with bacteriocins of lactic acid bacteria and conveys some of the problems associated with this process as well as some of the lessons learned. An improvement in the efficiency of the purification process should contribute significantly to research at the understanding of the biochemical nature of bacteriocins.

Bacteriocins↗
PubMed1997

Autolysis of Lactococcus lactis ssp. lactis and Lactobacillus casei ssp. casei. Cell lysis induced by a crude bacteriocin.

Autolytic properties of Lactococcus lactis subsp. lactis IFPL359, its Lac Prt derivative Lc. lactis Tl and Lactobacillus casei subsp. casei IFPL731, used as starter and adjunct starter in goat's milk cheese making, have been studied. The lytic effect of a bacteriocin produced by a lactic acid bacterium isolated from raw goat's milk has also been analyzed. Lactococcal cells resuspended in phosphate buffer showed a peak of autolysis when they were harvested in the early growth phase. A more stable autolytic pattern through the exponential growth was obtained for Lb. casei IFPL731. Optimal autolysis was found in 0.1 M sodium phosphate buffer during incubation at 40 degrees C for Lb. casei IFPL731 and at 35 degrees C for the lactococci. Thermoinduction of cell lysis was not obtained in any of the cases under the conditions studied. Lytic effect of the crude bacteriocin assayed was strongest against Lc. lactis Tl. Lysis response to the bacteriocin seemed to be strain-dependent and related to growth conditions.

Bacteriocins↗
PubMed1997

Antilisterial activity of three bacteriocins used at sub minimal inhibitory concentrations and cross-resistance of the survivors.

The kinetics of inhibition of Listeria innocua strain Lin11 in a nutrient broth containing either nisin, pediocin AcH, or enterococcin EFS2 at concentrations ensuring a 2-3 log reduction of the population were first investigated. The rate of inhibition differed considerably between the bacteriocins. At the time that maximum viability loss occurred in the cultures containing either nisin (12 AU ml(-1)) or pediocin AcH (50 AU ml(-1)) the survivors resumed growth, although the medium retained most of its initial inhibitory activity. The survivors displayed increased resistance not only toward the bacteriocin they were in contact with, but toward the two other bacteriocins under study.

Bacteriocins↗
PubMedDate not supplied

Bacteriocin diversity: ecological and evolutionary perspectives.

The bacteriocin family is the most abundant and diverse group of bacterial defense systems. Bacteriocins range from the well-studied narrow spectrum, high molecular weight colicins produced by Escherichia coli and the short polypeptide lantibiotics of lactic acid bacteria to the relatively unknown halocins produced almost universally by the haolobacteria. The abundance and diversity of this potent arsenal of weapons is clear. Less clear is their evolutionary origins and the role they play in mediating microbial interactions. The goal of this review is to explore what we know about the evolution and ecology of the best-characterized family of bacteriocins, the colicins. We summarize current knowledge of how such extraordinary protein diversity arose and is maintained in microbial populations and what role these toxins play in mediating microbial population-level and community-level dynamics.

Bacteriocins↗
PubMed1998

Bacteriocin production by Fusobacterium isolates recovered from the oral cavity of human subjects with and without periodontal disease and of marmosets.

Bacteriocin production has been studied in very few anaerobic bacteria, and no report is available for Fusobacterium species. In the present study a total of 167 Fusobacterium isolates were tested for bacteriocin production: 70 isolates were obtained from the oral cavity of patients with periodontal disease, 47 were recovered from healthy oral sites of human subjects and 50 from the oral cavity of Callithrix penicillata. Autoantagonism and isoantagonism were observed when the bacteriocin-producing isolates were tested against themselves. Heteroantagonism was detected by testing the Fusobacterium isolates against 14 reference strains and 2 strains of Actinobacillus actinomycetemcomitans from our laboratory collection. The auto-, iso- and heteroantagonism phenomena observed in this comparative study suggest a possible ecological role for this (these) antagonistic substance(s) in the oral environment.

Animals↗
PubMed1991

Comparative biotyping, bacteriocin typing, and serogrouping (O-antigens) of Serratia liquefaciens.

A total of 83 clinical isolates of Serratia liquefaciens from 81 patients were biotyped, bacteriocin typed (with group A phage tail bacteriocins from S. marcescens), and serogrouped. Biotyping afforded least discrimination, because 71 of the 83 isolates (85.5%) comprised 2 biotypes; the remainder were of 5 different biotypes. Bacteriocin typing differentiated 70 of the 83 isolates (84.3%) into 20 types. Polyclonal rabbit anti-O immune sera identified 16 O-antigens, and all 83 isolates could be serogrouped.

Antigens, Bacterial↗
PubMed1990

Typing of Actinomyces pyogenes by its production and susceptibility to bacteriocin-like inhibitors.

A scheme for "fingerprinting" of Actinomyces pyogenes strains based on their production of (P-typing) and the sensitivity to (S-typing) bacteriocin-like substances has been developed. P-typing and S-typing of 42 A. pyogenes cultures with a set of 9 micrococcal and staphylococcal species as indicator strains and 9 streptococcal species as bacteriocin producer strains revealed 10 P types and 7 S types, respectively. The bacteriocin "fingerprinting" procedure might provide a means for subdividing A. pyogenes and may find application in epidemiological studies.

Actinomyces↗
PubMed1992

Differential activity of bacteriocins and cefotaxime against Serratia marcescens clinical isolate SMG40 and its pigmented variant.

Strain Serratia marcescens SMG40 was nonpigmented but yielded pigmented variants at low frequency. Of 15 tested bacteriocins, 10 were active against the original strain, but only 7 were active against the pigmented variant Pdg+. Moreover, active cephalosporins, e.g., cefotaxime, were more active against the Pdg+ variant than against strain SMG40. These reciprocal differences in susceptibility to some bacteriocins and to cefotaxime were maintained in subclones derived from Pdg+/- sectored colonies. However, mutants of pigmentation isolated from the Pdg+ variant were not modified with regard to bacteriocins and cefotaxime. Other clinical isolates of Serratia were examined for comparison, but strain SMG40 appeared to be unique.

Amoxicillin↗
PubMed1998

Instruments of microbial warfare: bacteriocin synthesis, toxicity and immunity.

Bacteria have devised ingenious enzymatic machinery to synthesize antibiotic molecules (bacteriocins) for their continuous warfare with other microorganisms. Synthesis and export of these toxic compounds are coordinated to ensure the proper extracellular activation of bacteriocin toxicity. In designing future antibiotics, some of the tricks used by bacteriocins might be exploited for the synthesis of novel compounds.

Amino Acid Sequence↗
PubMed1978

Lactostrepcins--acid bacteriocins produced by lactic streptococci.

All 47 non-nisin producing strains of Streptococcus lactis and 12/13 strains of Str. lactis subsp. diacetylactis examined produced bacteriocins, for which the term lactostrepcins is suggested. Seven strains of Str. cremoris examined produced no bacteriocins active against 3 lactic streptococci strains used as indicators. The strains examined were divided into 3 groups: I, those producing lactostrepcins active against only one streptomycin resistant mutant of Str. lactis 60 indicator strain; II, those producing lactostrepcins active against all 3 indicator strains; III, those not producing lactostrepcins active against the indicator strains employed. The lactostrepcins were sensitive to various proteolytic enzymes and to phospholipase D, but retained full or partial activity after dialysis. Most of the bacteriocins studied were fully active only within the pH range 4.2--5.0 and were reversibly inactivated at pH 7.0 or 8.0. Results suggested occurrence of 4 different lactostrepcins. The lactostrepcins produced by all group I strains were the same, but there were differences among the lactostrepcins produced by group II strains. Lactostrepcins killed some beta-haemolytic streptococci and some strains of Lactobacillus helveticus. One of the lactostrepcins was also active against certain Leuconostoc strains, but not against other Leuconostoc strains, nor against L. helveticus or other Gram-positive bacteria.

Bacteriocins↗
PubMed2004

Performance and applications of polyclonal antipeptide antibodies specific for the enterococcal bacteriocin enterocin P.

Polyclonal antibodies with specificity for enterocin P (EntP) have been generated by immunization of rabbits with two chemically synthesized N-terminal peptides (P1 and P2) and a C-terminal peptide (P3) of this bacteriocin conjugated to the carrier protein KLH. The sensitivity and specificity of the peptide-KLH-generated antibodies were evaluated by a noncompetitive indirect enzyme-linked immunosorbent assay (NCI-ELISA) and a competitive indirect (CI)-ELISA. The NCI-ELISA but not the CI-ELISA was valuable for detecting the existence of EntP specific antibodies in the sera of the P2-KLH and P3-KLH immunized animals and to detect and quantify the EntP in the supernatant of producer strains. The anti-P2-KLH sera cross-reacted with the supernatant of a strain producer of sakacin A, a bacteriocin closely related to EntP. Immunoaffinity chromatography columns with anti-P2-KLH or anti-P3-KLH immunoglobulins retained the EntP from the supernatant of the producer strain. Western blotting of EntP with the anti-P2-KLH-generated antibodies suggests that purified EntP tends to the formation of aggregates with no antimicrobial activity. Monitoring the purification of EntP with antipeptide antibodies suggests that while the performance of the evaluated purification procedures would be reasonably acceptable in terms of recovery of the antimicrobial activity of the bacteriocin, their yield is far from attractive in terms of recovery of the initial concentration of enterocin P.

Animals↗
PubMed2004

Purification and characterization of bacteriocin from Pediococcus pentosaceus ACCEL.

The Pediococcus pentosaceus ACCEL bacteriocin was purified to electrophoretical homogeneity by cell adsorption-desorption and Superose 12 fast performance liquid chromatography (FPLC). The purified bacteriocin, with a molecular mass of 17.5 kDa and an N-terminal sequence of -KYYGNGVTXGKHSXXVDXG-, belongs to class IIa and is designated pediocin ACCEL. It was inactivated by various proteases and stable at pH 2.0-6.0 and <100 degrees C. More than 80% activity was left even after 15 min of heating at 121 degrees C and pH 2.0-4.0. Gram-positive food-borne pathogens were inhibited by this bacteriocin, but Gram-negative ones were not. According to the storage stability study, the purified pediocin was stable at pH <6.0 and low temperature. No significant change in bactericidal activity was observed after freeze-drying and subsequent 1-month storage at room temperature.

Amino Acid Sequence↗
PubMed2001

Isolation of bacteriocins through expanded bed adsorption using a hydrophobic interaction medium.

Two lactic acid bacterium bacteriocins were isolated from fermentation medium through expanded bed adsorption using a hydrophobic interaction gel. First, amylovorin L471, produced by Lactobacillus amylovorus DCE 471, was selected for the optimisation of the loading and eluting conditions. Secondly, the results of the optimisation were applied for the isolation of enterocin RZS C5, a bacteriocin produced by Enterococcusfaecium RZS C5. Optimal adsorption was obtained for a medium with concentration of 1.0 M ammonium sulphate and adjusted to pH 4.0 (94.9% for amylovorin L471 and 75.0% for enterocin RZS C5). Elution with 50% ethanol, buffered at pH 6.0, resulted in an optimal total recovery of the bacteriocin activity of 47.6 and 57.6%, respectively. The highest fold purification expressed as the increase in specific activity (AU/mg) corresponded to the highest recovery, being 140- and 1677-fold, respectively. Nevertheless, a total recovery of only 25.6% with an increase of the specific activity of 121 times was obtained after conventional isolation by ammonium sulphate precipitation.

Bacteriocins↗
PubMed2005

Bacteriocins: developing innate immunity for food.

Bacteriocins are bacterially produced antimicrobial peptides with narrow or broad host ranges. Many bacteriocins are produced by food-grade lactic acid bacteria, a phenomenon which offers food scientists the possibility of directing or preventing the development of specific bacterial species in food. This can be particularly useful in preservation or food safety applications, but also has implications for the development of desirable flora in fermented food. In this sense, bacteriocins can be used to confer a rudimentary form of innate immunity to foodstuffs, helping processors extend their control over the food flora long after manufacture.

Amino Acid Sequence↗
PubMed2001

Effect of physical factors on the production of bacteriocin from Pediococcus acidilactici ITV 26.

The effect of pH, temperature and agitation on growth and bacteriocin production by Pediococcus acidilactici ITV 126 was investigated. Experiments were made in flasks containing MRS medium at 30 to 40 degrees C, pH 5 to 7 and agitation 0 to 200 rpm. Factor levels were arranged in a 2(3) factorial design with central and axial points. Anova and Tukey paired comparison tests showed that a temperature of 35 degrees C favored bacteriocin production, whereas 40 degrees C was best for cell growth. A statistical interaction of temperature and agitation was observed affecting microbial growth. pH 5 favored both cell growth and bacteriocin production.

Bacteriocins↗
PubMed1998

Antilisterial activity of enterocin 81, a bacteriocin produced by Enterococcus faecium WHE 81 isolated from cheese.

Enterocin 81, a bacteriocin produced by Enterococcus faecium WHE 81 previously isolated from cheese, exhibited a very narrow spectrum of activity, which is mainly directed against enterococci and Listeria spp. including Listeria monocytogenes. Enterocin 81 activity, which was extremely rapid with maximal effect achieved within 30 min, could not be detected after treatment with various proteolytic enzymes. This activity was bactericidal in nature and induced an important efflux of intracellular material, which was visualized under electron microscopy as filaments coming out of L. monocytogenes cells. However, enterocin 81 did not display bacterial lysis on sensitive cells, as no changes in cell morphology were detected following the bactericidal action. Furthermore, this bacteriocin was shown to be equally active at pH values ranging from 4.0 to 8.0, which, along with the narrow activity spectrum, are two factors of paramount interest with regards to possible use of this bacteriocin in fermented foods.

Bacteria↗
PubMed2000

Purification and some characteristics of enterocin ON-157, a bacteriocin produced by Enterococcus faecium NIAI 157.

Bacteriocin-like activity (BLA) was screened in 690 strains of lactic acid bacteria isolated from plant materials such as silages and fermented vegetables. Among them, a strain identified as Enterococcus faecium NIAI 157 showed a clear BLA against the indicator strain, Ent. faecium IFO 13712. The proteinaceous nature and antimicrobial activity against closely related species strongly indicated that this BLA was a bacteriocin and was designated enterocin ON-157. The bacteriocin activity of this strain was extracellularly produced in the logarithmic growth phase in MRS broth and purified by ultrafiltration, ammonium sulphate precipitation and cation-exchange chromatography. Purified enterocin ON-157 had a molecular weight of approximately 2500 Da in SDS-PAGE analysis and was easily inhibited by treatment with alpha-amylase and proteolytic enzymes. Enterocin ON-157 had a bactericidal mode of action and inhibited the growth of the enterococci, Lactobacillus sake and Listeria monocytogenes. Enterococcus faecium NIAI 157 harboured two plasmids, 49.0 kb and 43.7 kb, and a variant missing a larger plasmid by curing with novobiocin lost the bactriocin activity.

Anti-Bacterial Agents↗
PubMed2000

Anti-Listeria effect of enterocin A, produced by cheese-isolated Enterococcus faecium EFM01, relative to other bacteriocins from lactic acid bacteria.

Enterocin A produced by Enterococcus faecium EFM01 displayed a narrow antimicrobial spectrum, mainly directed against Listeria spp. In particular, the bacteriocin was extremely active against 13 Listeria monocytogenes strains. This high specificity of action of enterocin A for Listeria spp. relative to lactic acid bacteria, together with its broad range of activity from pH 4.0 to pH 9.0, are factors which may be of great interest with respect to the potential antilisterial use of this bacteriocin in fermented foods. Assessment of the effect of enterocin A concentration on the extent and kinetics of bactericidal activity on L. monocytogenes Lm 6 (107 cfu ml-1 in culture broth), suggested that viability losses of higher than 5 log10, and time intervals necessary for maximum loss of viability of less than 2 h, could not be obtained. Moreover, it was shown that both parameters are closely dependent on the Listeria strain used. On the other hand, at concentrations inducing destruction of approximately 2 log10 cycles, maximum loss of viability was achieved within time intervals which varied widely from one lactic acid bacteria bacteriocin to another.

Bacteriocins↗