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PubMed1980

Comparison of the antibacterial activity of the hypothiocyanite anion towards Streptococcus lactis and Escherichia coli.

It has been suggested that the antibacterial activity of the lactoperoxidase/thiocyanate/hydrogen peroxide system is due to the hypothiocyanite anion. Relatively pure solutions of hypothiocyanite can be prepared using an immobilized enzyme. These preparations have been used to examine the effect of the anion on the growth and on the membranes of Escherichia coli and Streptococcus lactis. Escherichia coli is killed in the presence of the anion whereas the effect on Streptococcus lactis is only bacteriostatic. As similar effects have been noted with the lactoperoxidase/thiocyanate/hydrogen peroxide system the hypothesis that the action of the two systems is similar is supported.

Amino Acids↗

PubMed1973

Transduction of lactose metabolism in Streptococcus lactis C2.

Ultraviolet (UV)-induced phage lysates, from lactose-positive (lac(+)) Streptococcus lactis C2, transduced lactose fermenting ability to lac(-) recipient cells of this organism. Although the phage titer could not be determined due to the absence of an appropriate indicator strain, the number of transductants was proportional to the amount of phage lysate added. Treatment of the lysate with deoxyribonuclease had no effect on this conversion, indicating the observed genetic change was not mediated by free deoxyribonucleic acid. When the lac(+) transductants were isolated and exposed to UV irradiation, lysates with higher transducing ability were obtained. The transducing ability of this lysate was about 100-fold higher than that observed in the original lysates. The lac(+) transductants were unstable since lac(-) segregants occurred at high frequency. The phage lysate from S. lactis C2 also transduced maltose and mannose metabolism to the respective negative recipient cells. The results demonstrate the transduction of carbohydrate markers by a streptococcal phage and establish a genetic transfer system in group N streptococci.

Bacteriophages↗

PubMed1984

Plasmid transformation of Streptococcus lactis protoplasts: optimization and use in molecular cloning.

The parameters affecting polyethylene glycol-induced plasmid transformation of Streptococcus lactis LM0230 protoplasts were examined to increase the transformation frequency. In contrast to spreading protoplasts over the surface of an agar medium, their incorporation into soft agar overlays enhanced regeneration of protoplasts and eliminated variability in transformation frequencies. Polyethylene glycol with a molecular weight of 3,350 at a final concentration of 22.5% yielded optimal transformation. A 20-min polyethylene glycol treatment of protoplasts in the presence of DNA was necessary for maximal transformation. The number of transformants recovered increased as the protoplast and DNA concentration increased over a range of 3.0 X 10(6) to 3.0 X 10(8) protoplasts and 0.25 to 4.0 micrograms of DNA per assay, respectively. With these parameters, transformation was increased to 5 X 10(3) to 4 X 10(4) transformants per microgram of DNA. Linear and recombinant plasmid DNA transformed, but at frequencies 10- to 100-fold lower than that of covalently closed circular DNA. Transformation of recombinant DNA molecules enabled the cloning of restriction endonuclease fragments coding for lactose metabolism into S. lactis LM0230 with the Streptococcus sanguis cloning vector, pGB301. These results demonstrated that the transformation frequency is sufficient to clone plasmid-coded genes which should prove useful for strain improvement of dairy starter cultures.

Base Sequence↗

PubMed1982

Electron microscopy of Streptococcus lactis phage plaque margins.

Ultrathin sections of plaques produced by Streptococcus lactis phages O712 and m13 were examined by transmission electron microscopy. The clear central area of the plaque was found to contain hardly any cellular material but the turbid margin contained abundant plasma membranes and some partially lysed cells whose appearance suggests a novel mechanism for the termination of plaque growth.

Bacteriolysis↗

PubMed1974

Localization of proteinase(s) near the cell surface of Streptococcus lactis.

Two criteria suggest that most of the proteinase of Streptococcus lactis is localized in the cell wall. (i) Intact cells possess proteinase activity when incubated with a high-molecular-weight substrate. (ii) Most of the cell-bound proteinase activity is released during spheroplast formation under conditions which result in the release of only 1% of the intracellular enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase. The solubilized cell wall, plasma membrane, and cytoplasm fractions contained 84, 0, and 16%, respectively, of the total proteinase activity with casein as substrate. The physiological role of a surface-bound proteinase in this organism is discussed.

Caseins↗

PubMed1987

Regulation of the glutamate-glutamine transport system by intracellular pH in Streptococcus lactis.

Various methods of manipulation of the intracellular pH in Streptococcus lactis result in a unique relationship between the rate of glutamate and glutamine transport and the cytoplasmic pH. The initial rate of glutamate uptake by S. lactis cells increases more than 30-fold when the intracellular pH is raised from 6.0 to 7.4. A further increase of the cytoplasmic pH to 8.0 was without effect on transport. The different levels of inhibition of glutamate and glutamine transport at various external pH values by uncouplers and ionophores, which dissipate the proton motive force, can be explained by the effects exerted on the intracellular pH. The dependence of glutamate transport on the accumulation of potassium ions in potassium-filled and -depleted cells is caused by the regulation of intracellular pH by potassium movement.

Biological Transport, Active↗

PubMed1976

Isolation and examination of transducing bacteriophage particles from Streptococcus lactis C2.

Two defective transducing bacteriophages induced by exposure of Streptococcus lactis C2 to ultraviolet irradiation have been isolated and characterized. These temperate phages designated c2t1 and c2t2 were isolated by cesium chloride equilibrium density gradient centrifugation of phage preparations concentrated by polyethylene glycol precipitation. The equilibrium gradient contained two visually apparent phage bands positioned at densities of 1.487 and 1.463 g cm-3 respective for c2t1 and c2t2. Particle morphology and phenol extracted phage deoxyribonucleic acid were examined by electron microscopy for each phage. Head diameter, deoxyribonucleic acid length, and molecular weight for c2t1 were 60 nm, 10.9 mum, and 22.6 x 10(6) daltons, respectively. Phage c2t2 had a head diameter of 70nm, a deoxribonucleic acid length of 11.4 mum, and a molecular weight of 23.8 x 10(6) daltons. Comparing head diameter and phage deoxyribonucleic acid length suggests that the variation in c2t1 and c2t2 density was due to difference in head size. Phage c2t2 exhibited high frequency transduction of lactose metabolism based on preparations equilibrated by adjustment of optical density at 260 nm. Maltose and proteinase markers also were transduced by both phages. The transducing phage was defective, requiring a helper for the formation of transducing particles but not for the transduction process. Superinfection immunity was not conferred on post-infecting phage. The results demonstrated transduction by two nonidentical phage particles lysogenic for S. lactis C2.

Bacteriophages↗

PubMed1978

Mutants of Streptococcus lactis subsp. diacetylactis lacking diacetyl reductase activity.

Three strains of Streptococcus lactis subsp. diacetylactis, namely DRC-1, DRC-2 and DRC-3 which produced diacetyl up to 120 h of incubation were exposed to the ultraviolet irradiation as well as N-methyl-N'-nitro-N-nitrosoguanidine (NTG) to isolate mutants lacking diacetyl reductase activity. UV irradiation did not produce any isolate completely devoid of diacetyl reductase activity, though, 99.5% loss in activity could be achieved. NTG treatment proved to be more effective and seven survivors exhibiting complete loss of diacetyl reductase activity were recovered. These altered characteristics were retained on repeated subculturing.

Acetoin Dehydrogenase↗

PubMed1985

Cloning and expression of a Streptococcus cremoris proteinase in Bacillus subtilis and Streptococcus lactis.

Previously, curing experiments suggested that plasmid pWV05 (17.5 megadaltons [Md]) of Streptococcus cremoris Wg2 specifies proteolytic activity. A restriction enzyme map of pWV05 was constructed, the entire plasmid was subcloned in Escherichia coli with plasmids pBR329 and pACYC184. A 4.3-Md HindIII fragment could not be cloned in an uninterrupted way in E. coli but could be cloned in two parts. Both fragments showed homology with the 9-Md proteinase plasmid of S. cremoris HP. The 4.3-Md HindIII fragment was successfully cloned in Bacillus subtilis on plasmid pGKV2 (3.1 Md). Crossed immunoelectrophoresis of extracts of B. subtilis carrying the recombinant plasmid (pGKV500; 7.4 Md) showed that the fragment specifies two proteins of the proteolytic system of S. cremoris Wg2. PGKV500 was introduced in a proteinase-deficient Streptococcus lactis strain via protoplast transformation. Both proteins were also present in cell-free extracts of S. lactis(pGKV500). In S. lactis, pGKV500 enables the cells to grow normally in milk with rapid acid production, indicating that the 4.3-Md HindIII fragment of plasmid pWV05 specifies the proteolytic activity of S. cremoris Wg2.

Animals↗

PubMed1968

Proteinase enzyme system of lactic streptococci. 3. Substrate specificity of Streptococcus lactis intracellular proteinase.

The substrate specificity of an intracellular proteinase from Streptococcus lactis was investigated in an effort to understand the role of the enzyme in the cell. Peptides in which the N-terminal residue was glycine were not hydrolyzed by the enzyme (exceptions were glycyl-alanine, glycyl-aspartic acid, and glycyl-asparagine), but the peptide was hydrolyzed if the N-terminal residue was alanine. The enzyme also showed activity toward peptides containing aspartic acid or asparagine. Hydrolysis of only the peptide bonds of alanyl, aspartyl, or asparaginyl residues was confirmed by the action of the enzyme on oxidized bovine ribonuclease A- and B- chain insulin. The N-terminal residues of the peptide fragments liberated were identified. The enzyme attacked both substrates only at alanyl, aspartyl, and asparaginyl residues, releasing these as free amino acids. In addition to alanine, aspartic acid, and asparagine, certain other amino acids were liberated from ribonuclease A, but these were accounted for by the relation of their position to alanine, aspartic acid, and asparagine residues.

Amino Acid Sequence↗

PubMed1988

Characterization of a cloned chromosomal fragment affecting the proteinase activity of Streptococcus lactis ssp. lactis.

Plasmid pVS8 (14.3 kbp) contains a 9.3 kbp fragment of Streptococcus lactis ssp. lactis SSL135 chromosomal DNA associated with the ability of this strain to grow in milk. In this study, it was found that pVS8 complements a defective plasmid-linked proteinase gene of SSL135. Using deletions and insertions, it was found that the size of the complementing region of pVS8 is approximately 6.0 kbp, and that its main part is located within a 5.7 kbp BglII fragment.

Animals↗

PubMed1987

Conjugal transfer of nisin plasmid genes from Streptococcus lactis 7962 to Leuconostoc dextranicum 181.

Acriflavine-generated mutants of Streptococcus lactis 7962 with various combinations of plasmid molecular masses were screened for nisin production. Nisin was produced by both the wild type and mutants that contained a 17.5-megadalton plasmid, which was obscured by chromosomal fragments. No nisin was produced by plasmid-free mutants. Sucrose fermentation and nisin production were simultaneously expressed. A transconjugant obtained from nisin-producing donor S. lactis 7962 and recipient Leuconostoc dextranicum 181 was a "supernisin" producer. The L. dextranicum Nis+ transconjugant was resistant to S. lactis 7962 phage and vancomycin (greater than 1,000 micrograms/ml), and it contained an extra 17.5-megadalton plasmid.

Centrifugation, Density Gradient↗

PubMed1983

Regulation of glycolysis and sugar phosphotransferase activities in Streptococcus lactis: growth in the presence of 2-deoxy-D-glucose.

Streptococcus lactis K1 has the capacity to grow on many sugars, including sucrose and lactose, in the presence of high levels (greater than 500 mM) of 2-deoxy-D-glucose. Initially, growth of the organism was transiently halted by the addition of comparatively low concentrations (less than 0.5 mM) of the glucose analog to the culture. Inhibition was coincident with (i) rapid accumulation of 2-deoxy-D-glucose 6-phosphate (ca. 120 mM) and preferential utilization of phosphoenolpyruvate via the mannose:phosphotransferase system, (ii) depletion of phosphorylated glycolytic intermediates, and (iii) a 60% reduction in intracellular ATP concentration. During the 5- to 10-min period of bacteriostasis the intracellular concentration of 2-deoxy-D-glucose 6-phosphate rapidly declined, and the concentrations of glycolytic intermediates were restored to near-normal levels. When growth resumed, the cell doubling time (Td) and the steady-state levels of 2-deoxy-D-glucose 6-phosphate maintained by the cells were dependent upon the medium concentration of 2-deoxy-D-glucose. Resistance of S. lactis K1 to the potentially toxic analog was a consequence of negative regulation of the mannose:phosphotransferase system by two independent mechanisms. The first, short-term response occurred immediately after the initial "overshoot" accumulation of 2-deoxy-D-glucose 6-phosphate, and this mechanism reduced the activity (fine control) of the mannose:phosphotransferase system. The second, long-term mechanism resulted in repression of synthesis (coarse control) of enzyme IImannose. The two regulatory mechanisms reduced the rate of 2-deoxy-D-glucose translocation via the mannose:phosphotransferase system and minimized the activity of the phosphoenolpyruvate-dependent futile cycle of the glucose analog (J. Thompson and B. M. Chassy, J. Bacteriol. 151:1454-1465, 1982). Phosphoenolpyruvate was thus conserved for transport of the growth sugar and for generation of ATP required for biosynthetic and work functions of the growing cell.

Chloramphenicol↗

PubMed1986

N5-(1-carboxyethyl)-ornithine, a new amino acid from the intracellular pool of Streptococcus lactis.

Intracellular concentrations of amino acids were determined in cells of Streptococcus lactis 133 during growth in complex, spent, and chemically defined media. Glutamic and aspartic acids represented the major constituents of the amino acid pool. However, organisms grown in spent medium or in defined medium supplemented with ornithine also contained unusually high levels of two additional amino acids. One of these amino acids was ornithine. The second compound exhibited properties of a neutral amino acid by coelution with valine from the amino acid analyzer. The compound did not, however, comigrate with valine or any other standard amino acid by two-dimensional thin-layer chromatography. The unknown amino acid was purified by paper and thin-layer chromatography, and its molecular structure was determined by 1H and 13C nuclear magnetic resonance spectroscopy. This new amino acid was shown to be N5-(1-carboxyethyl)-ornithine. The 14C-labeled compound was formed by cells of S. lactis 133 during growth in spent medium or defined medium containing [14C]ornithine. Formation of the derivative by resting cells required ornithine and the presence of a metabolizable sugar. N5-(1-Carboxyethyl)-ornithine was synthesized chemically from both poly-S-ornithine and (2S)-N2-carbobenzyloxy-ornithine as a 1:1 mixture of two diastereomers. The physical and chemical properties of the amino acid purified from S. lactis 133 were identical to those of one of the synthetic diastereomers. The bis-N-trifluoroacetyl-di-n-butyl esters of the natural and synthetic compounds generated identical gas chromatography-mass spectrometry spectra. A mechanism is suggested for the in vivo synthesis of N5-(1-carboxyethyl)-ornithine, and the possible functions of this new amino acid are discussed.

Gas Chromatography-Mass Spectrometry↗

PubMedDate not supplied

[Procedure for isolating nisin from Streptococcus lactis].

The paper describes a method for obtaining the antibiotic nisine from Streptococcus lactis str. MSU via 50% acetic acid extraction. The concentrate is dried in the Anhydro spray drier (Denmark). The preparation is inactivated during a one-year storage in the refrigerator by 20-25%.

Drug Stability↗

PubMedDate not supplied

[Changes in the intracellular pool of free amino acids of Streptococcus lactis under different cultivation conditions].

The intracellular pool of free amino of Streptococcus lactis--lysine producer contains a good number of amino acids when cultivated on the corn medium. Glutamic acid, proline, alanine, lysine, leucine, histidine and arginine are in predominance. An almost complete amino acid pool develops at an early exponential phase of Str. lactis growth under stationary cultivation conditions. The content of free amino acids increases 4-fold during the transition from the early exponential phase to the stationary phases under submerged cultivation conditions. This can be attributed to a more intensive amino acid exchange during the medium stirring than during stationary cultivation.

Amino Acids↗

PubMed1973

Fractionation of dipeptidase activities of Streptococcus lactis and dipeptidase specificity of some lactic acid bacteria.

Proteins in sonic extracts of Streptococcus lactis were separated by starch-gel electrophoresis at high voltage. Each slab was sliced longitudinally, and half was stained for peptidases in a mixture containing a peptide, L-amino acid oxidase (snake venom), peroxidase, and o-dianisdine; the other half was stained in amido black for protein. In addition to sonic treatment, trypsin also released enzyme from acetone-treated cells. Glycyl-L-phenylalanine, L-phenylalanyl-glycine, L-alanyl-L-phenylalanine, and L-phenylalanyl-L-alanine served as substrates in characterizing the enzymes. Five different fractions of various specificities appeared in the gels. Broad-range substrate specificities were found for sonic extracts of S. lactis, S. cremoris, S. durans, and Lactobacillus acidophilus.

Alanine↗

PubMed1982

Transformation of Streptococcus lactis Protoplasts by Plasmid DNA.

Polyethylene glycol-treated protoplasts prepared from Streptococcus lactis LM3302, a lactose-negative (Lac) derivative of S. lactis ML3, were transformed to lactose-fermenting ability by a transductionally shortened plasmid (pLM2103) coding for lactose utilization.

Journal Article↗