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Journal articles on the topic 'Sakacin A'

Author: Grafiati

Published: 9 March 2023

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1

Vaughan, Anne, Vincent G. H. Eijsink, and Douwe van Sinderen. "Functional Characterization of a Composite Bacteriocin Locus from Malt Isolate Lactobacillus sakei 5." Applied and Environmental Microbiology 69, no. 12 (December 2003): 7194–203. http://dx.doi.org/10.1128/aem.69.12.7194-7203.2003.

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ABSTRACT Lactobacillus sakei 5, isolated from malted barley, produces three bacteriocins. Genetic and functional analysis of the purified bacteriocins showed that this strain produces a plasmid-encoded bacteriocin that is identical to sakacin P, as well as two novel, chromosomally encoded bacteriocins, which were designated sakacin T and sakacin X. The structural genes specifying sakacin T and sakacin X are part of the sakacin TX locus, which consists of two adjacent but divergently oriented gene clusters. The first gene cluster includes stxP, stxR, stxK, and stxT, which, based on functional and comparative sequence analysis, are believed to encode an inducing peptide and proteins involved in regulation and secretion of these bacteriocins. The second gene cluster includes the structural and immunity genes for sakacin T, a class IIb two-peptide bacteriocin composed of SakTα and SakTβ, and sakacin X, a class IIa bacteriocin. Interestingly, a so-called transport accessory protein was absent from the locus, and based on our results it appears that a dedicated accessory protein is not required for processing and transport of sakacin T and sakacin X.

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2

Katla, T., K. Naterstad, M. Vancanneyt, J. Swings, and L. Axelsson. "Differences in Susceptibility of Listeria monocytogenes Strains to Sakacin P, Sakacin A, Pediocin PA-1, and Nisin." Applied and Environmental Microbiology 69, no. 8 (August 2003): 4431–37. http://dx.doi.org/10.1128/aem.69.8.4431-4437.2003.

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ABSTRACT Two hundred strains of Listeria monocytogenes collected from food and the food industry were analyzed for susceptibility to the class IIa bacteriocins sakacin P, sakacin A, and pediocin PA-1 and the class I bacteriocin nisin. The individual 50% inhibitory concentrations (IC50) were determined in a microtiter assay and expressed in nanograms per milliliter. The IC50 of sakacin P ranged from 0.01 to 0.61 ng ml−1. The corresponding values for pediocin PA-1, sakacin A, and nisin were 0.10 to 7.34, 0.16 to 44.2, and 2.2 to 781 ng ml−1, respectively. The use of a large number of strains and the accuracy of the IC50 determination revealed patterns not previously described, and for the first time it was shown that the IC50 of sakacin P divided the L. monocytogenes strains into two distinct groups. Ten strains from each group were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of whole-cell proteins and amplified fragment length polymorphism. The results from these studies essentially confirmed the grouping based on the IC50 of sakacin P. A high correlation was found between the IC50 of sakacin P and that of pediocin PA-1 for the 200 strains. Surprisingly, the correlation between the IC50 of the two class IIa bacteriocins sakacin A and sakacin P was lower than the correlation between the IC50 of sakacin A and the class I bacteriocin nisin.

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3

Tessema, Girum Tadesse, Trond Mï¿½retrï¿½, Achim Kohler, Lars Axelsson, and Kristine Naterstad. "Complex Phenotypic and Genotypic Responses of Listeria monocytogenes Strains Exposed to the Class IIa Bacteriocin Sakacin P." Applied and Environmental Microbiology 75, no. 22 (September 18, 2009): 6973–80. http://dx.doi.org/10.1128/aem.00608-09.

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ABSTRACT Sakacin P is a class IIa bacteriocin that is active against the food-borne pathogen Listeria monocytogenes, and use of this compound as a biopreservative in foods has been suggested. In the present study, we characterized 30 spontaneous sakacin P-resistant mutants of L. monocytogenes obtained after single exposure to sakacin P. The frequency of development of sakacin P resistance for all strains was in the range from 10−8 to 10−9. Using the 50% inhibitory concentration (IC50) of sakacin P, the strains could be grouped into strains with high levels of resistance (IC50, ≥104 ng ml−1) and strains with low levels of resistance (IC50, <104 ng ml−1). Resistant strains belonging to the same IC50 group also had similar physiological and genetic characteristics. Generally, the resistant strains showed substantial variations in many parameters, such as differences in the stability of the acquired resistance to sakacin P, growth fitness, food-related stress tolerance, and biofilm-forming ability. Fourier transform infrared spectroscopy revealed differences between wild-type and resistant strains in polysaccharide, fatty acid, and, protein regions. A mannose-specific phosphotransferase (PTS) operon has been described for class IIa bacteriocin resistance, and the sakacin P-resistant strains displayed both up- and downregulation of the expression of the mptA gene encoding the PTS system. This is the first comprehensive study of the diversity of a large number of spontaneous resistant mutants obtained after one exposure to a class IIa bacteriocin, particularly to sakacin P. The great diversity among the resistant strains exposed to the same stress conditions suggests that there are different resistance mechanisms.

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4

Mathiesen, Geir, Kathrin Huehne, Lothar Kroeckel, Lars Axelsson, and Vincent G. H. Eijsink. "Characterization of a New Bacteriocin Operon in Sakacin P-Producing Lactobacillus sakei, Showing Strong Translational Coupling between the Bacteriocin and Immunity Genes." Applied and Environmental Microbiology 71, no. 7 (July 2005): 3565–74. http://dx.doi.org/10.1128/aem.71.7.3565-3574.2005.

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ABSTRACT Previous studies of genes involved in the production of sakacin P by Lactobacillus sakei Lb674 revealed the presence of an inducible promoter downstream of the known spp gene clusters. We show here that this promoter drives the expression of an operon consisting of a bacteriocin gene (sppQ), a cognate immunity gene (spiQ), another gene with an unknown function (orf4), and a pseudoimmunity gene containing a frameshift mutation (orf5). The leader peptide of the new one-peptide bacteriocin sakacin Q contains consensus elements that are typical for so-called “double-glycine” leader peptides. The mature bacteriocin shows weak similarity to the BrcA peptide of the two-peptide bacteriocin brochocin C. Sakacin Q has an antimicrobial spectrum that differs from that of sakacin P, thus expanding the antimicrobial properties of the producer strain. The genes encoding sakacin Q and its cognate immunity protein showed strong translational coupling, which was investigated in detail by analyzing the properties of a series of β-glucuronidase fusions. Our results provide experimental evidence that production of the bacteriocin and production of the cognate immunity protein are tightly coregulated at the translational level.

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5

Eijsink, Vincent G. H., Marianne Skeie, P. Hans Middelhoven, May Bente Brurberg, and Ingolf F. Nes. "Comparative Studies of Class IIa Bacteriocins of Lactic Acid Bacteria." Applied and Environmental Microbiology 64, no. 9 (September 1, 1998): 3275–81. http://dx.doi.org/10.1128/aem.64.9.3275-3281.1998.

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ABSTRACT Four class IIa bacteriocins (pediocin PA-1, enterocin A, sakacin P, and curvacin A) were purified to homogeneity and tested for activity toward a variety of indicator strains. Pediocin PA-1 and enterocin A inhibited more strains and had generally lower MICs than sakacin P and curvacin A. The antagonistic activity of pediocin-PA1 and enterocin A was much more sensitive to reduction of disulfide bonds than the antagonistic activity of sakacin P and curvacin A, suggesting that an extra disulfide bond that is present in the former two may contribute to their high levels of activity. The food pathogen Listeria monocytogenes was among the most sensitive indicator strains for all four bacteriocins. Enterocin A was most effective in inhibitingListeria, having MICs in the range of 0.1 to 1 ng/ml. Sakacin P had the interesting property of being very active towardListeria but not having concomitant high levels of activity toward lactic acid bacteria. Strains producing class IIa bacteriocins displayed various degrees of resistance toward noncognate class IIa bacteriocins; for the sakacin P producer, it was shown that this resistance is correlated with the expression of immunity genes. It is hypothesized that variation in the presence and/or expression of such immunity genes accounts in part for the remarkably large variation in bacteriocin sensitivity displayed by lactic acid bacteria.

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6

Fimland, Gunnar, Line Johnsen, Lars Axelsson, May B. Brurberg, Ingolf F. Nes, Vincent G. H. Eijsink, and Jon Nissen-Meyer. "A C-Terminal Disulfide Bridge in Pediocin-Like Bacteriocins Renders Bacteriocin Activity Less Temperature Dependent and Is a Major Determinant of the Antimicrobial Spectrum." Journal of Bacteriology 182, no. 9 (May 1, 2000): 2643–48. http://dx.doi.org/10.1128/jb.182.9.2643-2648.2000.

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ABSTRACT Several lactic acid bacteria produce so-called pediocin-like bacteriocins that share sequence characteristics, but differ in activity and target cell specificity. The significance of a C-terminal disulfide bridge present in only a few of these bacteriocins was studied by site-directed mutagenesis of pediocin PA-1 (which naturally contains the bridge) and sakacin P (which lacks the bridge). Introduction of the C-terminal bridge into sakacin P broadened the target cell specificity of this bacteriocin, as illustrated by the fact that the mutants were 10 to 20 times more potent than the wild-type toward certain indicator strains, whereas the potency toward other indicator strains remained essentially unchanged. Like pediocin PA-1, disulfide-containing sakacin P mutants had the same potency at 20 and 37°C, whereas wild-type sakacin P was approximately 10 times less potent at 37°C than at 20°C. Reciprocal effects on target cell specificity and the temperature dependence of potency were observed upon studying the effect of removing the C-terminal disulfide bridge from pediocin PA-1 by Cys→Ser mutations. These results clearly show that a C-terminal disulfide bridge in pediocin-like bacteriocins contributes to widening of the antimicrobial spectrum as well as to higher potency at elevated temperatures. Interestingly, the differences between sakacin P and pediocin PA-1 in terms of the temperature dependency of their activities correlated well with the optimal temperatures for bacteriocin production and growth of the bacteriocin-producing strain.

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7

Leroy, Frédéric, and Luc de Vuyst. "The Presence of Salt and a Curing Agent Reduces Bacteriocin Production by Lactobacillus sakei CTC 494, a Potential Starter Culture for Sausage Fermentation." Applied and Environmental Microbiology 65, no. 12 (December 1, 1999): 5350–56. http://dx.doi.org/10.1128/aem.65.12.5350-5356.1999.

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ABSTRACT The specific conditions in the batter of raw fermented sausages may reduce the efficiency of bacteriocin-producing starter cultures. In this work, using in vitro fermentation, we found that sodium chloride and sodium nitrite interfere with the growth ofLactobacillus sakei CTC 494, an organism which produces the antilisterial bacteriocin sakacin K. Because sakacin K production follows primary metabolite kinetics, a decrease in cell formation resulted in a decrease in sakacin K production as well. Sodium chloride dramatically influenced bacteriocin production by decreasing both biomass production and specific bacteriocin production. Sodium nitrite, however, had no effect on specific bacteriocin production and decreased bacteriocin production only because of its effect on cell growth. Moreover, sodium nitrite enhanced the toxic effect of lactic acid on bacterial growth.

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8

Oust, Astrid, Trond Møretrø, Kristine Naterstad, Ganesh D. Sockalingum, Isabelle Adt, Michel Manfait, and Achim Kohler. "Fourier Transform Infrared and Raman Spectroscopy for Characterization of Listeria monocytogenes Strains." Applied and Environmental Microbiology 72, no. 1 (January 2006): 228–32. http://dx.doi.org/10.1128/aem.72.1.228-232.2006.

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ABSTRACT The purpose of this study was to characterize the variation in biochemical composition of 89 strains of Listeria monocytogenes with different susceptibilities towards sakacin P, using Fourier transform infrared (FTIR) spectroscopy and Raman spectroscopy. The strains were also analyzed using amplified fragment length polymorphism (AFLP) analysis. Based on their susceptibilities to sakacin P, the 89 strains have previously been divided into two groups. Using the FTIR spectra and AFLP data, the strains were basically differentiated into the same two groups. Analyses of the FTIR and Raman spectra revealed that the strains in the two groups contained differences in the compositions of carbohydrates and fatty acids. The relevance of the variation in the composition of carbohydrates with respect to the variation in the susceptibility towards sakacin P for the L. monocytogenes strains is discussed.

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9

Simon, L., C. Fremaux, Y. Cenatiempo, and J. M. Berjeaud. "Sakacin G, a New Type of Antilisterial Bacteriocin." Applied and Environmental Microbiology 68, no. 12 (December 2002): 6416–20. http://dx.doi.org/10.1128/aem.68.12.6416-6420.2002.

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ABSTRACT Sakacin G is a 37-amino-acid-residue-long class IIa bacteriocin produced by Lactobacillus sake 2512, which is encoded by the duplicated structural genes skgA1 and skgA2. Sakacin G appears to be unique and seems to be an intermediate between pediocin-like bacteriocins, according to its double-disulfide bridges required for antimicrobial activity, and mesentericin-like bacteriocins in terms of sequence homologies, inhibition spectrum, and specific activity.

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10

Musatti, Alida, Daniele Cavicchioli, Chiara Mapelli, Danilo Bertoni, Johannes A. Hogenboom, Luisa Pellegrino, and Manuela Rollini. "From Cheese Whey Permeate to Sakacin A: A Circular Economy Approach for the Food-Grade Biotechnological Production of an Anti-Listeria Bacteriocin." Biomolecules 10, no. 4 (April 12, 2020): 597. http://dx.doi.org/10.3390/biom10040597.

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Cheese Whey Permeate (CWP) is the by-product of whey ultrafiltration for protein recovery. It is highly perishable with substantial disposal costs and has serious environmental impact. The aim of the present study was to develop a novel and cheap CWP-based culture medium for Lactobacillus sakei to produce the food-grade sakacin A, a bacteriocin exhibiting a specific antilisterial activity. Growth conditions, nutrient supplementation and bacteriocin yield were optimized through an experimental design in which the standard medium de Man, Rogosa and Sharpe (MRS) was taken as benchmark. The most convenient formulation was liquid CWP supplemented with meat extract (4 g/L) and yeast extract (8 g/L). Although, arginine (0.5 g/L) among free amino acids was depleted in all conditions, its supplementation did not increase process yield. The results demonstrate the feasibility of producing sakacin A from CWP. Cost of the novel medium was 1.53 €/L and that of obtaining sakacin A 5.67 €/106 AU, with a significant 70% reduction compared to the corresponding costs with MRS (5.40 €/L, 18.00 €/106 AU). Taking into account that the limited use of bacteriocins for food application is mainly due to the high production cost, the obtained reduction may contribute to widening the range of applications of sakacin A as antilisterial agent.

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11

Møretrø, Trond, Kristine Naterstad, Ellen Wang, Inga M. Aasen, Stephane Chaillou, Monique Zagorec, and Lars Axelsson. "Sakacin P non-producing Lactobacillus sakei strains contain homologues of the sakacin P gene cluster." Research in Microbiology 156, no. 9 (November 2005): 949–60. http://dx.doi.org/10.1016/j.resmic.2005.05.005.

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12

Leroy, Frédéric, and Luc de Vuyst. "Temperature and pH Conditions That Prevail during Fermentation of Sausages Are Optimal for Production of the Antilisterial Bacteriocin Sakacin K." Applied and Environmental Microbiology 65, no. 3 (March 1, 1999): 974–81. http://dx.doi.org/10.1128/aem.65.3.974-981.1999.

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ABSTRACT Sakacin K is an antilisterial bacteriocin produced byLactobacillus sake CTC 494, a strain isolated from Spanish dry fermented sausages. The biokinetics of cell growth and bacteriocin production of L. sake CTC 494 in vitro during laboratory fermentations were investigated by making use of MRS broth. The data obtained from the fermentations was used to set up a predictive model to describe the influence of the physical factors temperature and pH on microbial behavior. The model was validated successfully for all components. However, the specific bacteriocin production rate seemed to have an upper limit. Both cell growth and bacteriocin activity were very much influenced by changes in temperature and pH. The production of biomass was closely related to bacteriocin activity, indicating primary metabolite kinetics, but was not the only factor of importance. Acidity dramatically influenced both the production and the inactivation of sakacin K; the optimal pH for cell growth did not correspond to the pH for maximal sakacin K activity. Furthermore, cells grew well at 35°C but no bacteriocin production could be detected at this temperature. L. sake CTC 494 shows special promise for implementation as a novel bacteriocin-producing sausage starter culture with antilisterial properties, considering the fact that the temperature and acidity conditions that prevail during the fermentation process of dry fermented sausages are optimal for the production of sakacin K.

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13

Katla, T., T. Moretro, I. Sveen, I. M. Aasen, L. Axelsson, L. M. Rorvik, and K. Naterstad. "Inhibition of Listeria monocytogenes in chicken cold cuts by addition of sakacin P and sakacin P-producing Lactobacillus sakei." Journal of Applied Microbiology 93, no. 2 (August 2002): 191–96. http://dx.doi.org/10.1046/j.1365-2672.2002.01675.x.

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14

Huhne, K., L. Axelsson, A. Holck, and L. Krockel. "Analysis of the sakacin P gene cluster from Lactobacillus sake Lb674 and its expression in sakacin-negative Lb. sake strains." Microbiology 142, no. 6 (June 1, 1996): 1437–48. http://dx.doi.org/10.1099/13500872-142-6-1437.

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15

Sørvig, Elisabeth, Geir Mathiesen, Kristine Naterstad, Vincent G. H. Eijsink, and Lars Axelsson. "High-level, inducible gene expression in Lactobacillus sakei and Lactobacillus plantarum using versatile expression vectors." Microbiology 151, no. 7 (July 1, 2005): 2439–49. http://dx.doi.org/10.1099/mic.0.28084-0.

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Vectors have been developed for inducible gene expression in Lactobacillus sakei and Lactobacillus plantarum in which expression of the gene of interest is driven by strong, regulated promoters from bacteriocin operons found in L. sakei strains. The activity of these promoters is controlled via a two-component signal transduction system, which responds to an externally added peptide pheromone. The vectors have a modular design, permitting easy exchange of all essential elements: the inducible promoter, the cognate regulatory system, the gene of interest, the antibiotic resistance marker and the replicon. Various variants of these so-called ‘pSIP’ vectors were constructed and tested, differing in terms of the bacteriocin regulon from which the regulatory elements were derived (sakacin A or sakacin P), the regulated promoter selected from these regulons, and the replicon (derived from p256 or pSH71). Using β-glucuronidase (GusA) and aminopeptidase N (PepN) as reporters, it was shown that the best vectors permitted inducible, pheromone-dose-dependent gene expression at very high levels, while displaying moderate basal activities when not induced. The most effective set-up was obtained using a vector containing the pSH71 replicon, the orfX promoter from the sakacin P regulon, and the cognate regulatory genes, in a L. sakei host. GusA levels obtained with this set-up were approximately ten times higher than the levels obtained with prototype pSIP versions, whereas PepN levels amounted to almost 50 % of total cellular protein.

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16

Gao, Yurong, Dapeng Li, Yan Sheng, and Xiaoyan Liu. "Mode of action of sakacin C2 against Escherichia coli." Food Control 22, no. 5 (May 2011): 657–61. http://dx.doi.org/10.1016/j.foodcont.2010.07.010.

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17

Bingxue Chang, Wenjie Ma, Zhaoxin Lu, Fengxia Lv, Fanqiang Meng, Liping Zheng, and Xiaomei Bie. "Design and Antibacterial Mechanism of Peptides Derived from Sakacin P." Russian Journal of Bioorganic Chemistry 48, no. 2 (April 2022): 399–410. http://dx.doi.org/10.1134/s1068162022020054.

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18

Holck, Askild L., Lars Axelsson, Kathrin HÃ¼hne, and Lothar KrÃ¶ckel. "Purification and cloning of sakacin 674, a bacteriocin fromLactobacillus sakeLb674." FEMS Microbiology Letters 115, no. 2-3 (January 1994): 143–49. http://dx.doi.org/10.1111/j.1574-6968.1994.tb06629.x.

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19

Sobrino, Odón J., Juan M. Rodríguez, Wagner L. Moreira, Luis M. Cintas, María F. Fernández, Bernabé Sanz, and Pablo E. Hernández. "Sakacin M, a bacteriocin-like substance from Lactobacillus sake 148." International Journal of Food Microbiology 16, no. 3 (July 1992): 215–25. http://dx.doi.org/10.1016/0168-1605(92)90082-e.

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20

JOFRÉ, ANNA, MARGARITA GARRIGA, and TERESA AYMERICH. "Inhibition of Listeria monocytogenes in Cooked Ham through Active Packaging with Natural Antimicrobials and High-Pressure Processing." Journal of Food Protection 70, no. 11 (November 1, 2007): 2498–502. http://dx.doi.org/10.4315/0362-028x-70.11.2498.

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Enterocins A and B and sakacin K at 200 and 2,000 activity units (AU)/cm2, nisin at 200 AU/cm2, 1.8% potassium lactate, and a combination of 200 AU/cm2 of nisin and 1.8% lactate were incorporated into interleavers, and their effectiveness against Listeria monocytogenes spiked in sliced, cooked ham was evaluated. Antimicrobial-packaged cooked ham was then subjected to high-pressure processing (HPP) at 400 MPa. In nonpressurized samples, nisin plus lactate–containing interleavers were the most effective, inhibiting L. monocytogenes growth for 30 days at 6°C, with counts that were 1.9 log CFU/g lower than in the control after 3 months. In the other antimicrobial-containing interleavers, L. monocytogenes did not exhibit a lag phase and progressively grew to levels of about 8 log CFU/g. HPP of actively packaged ham slices reduced Listeria populations about 4 log CFU/g in all batches containing bacteriocins (i.e., nisin, sakacin, and enterocins). At the end of storage, L. monocytogenes levels in the bacteriocin-containing batches were the lowest, with counts below 1.51 log CFU/g. In contrast, HPP moderately reduced L. monocytogenes counts in the control and lactate batches, with populations gradually increasing to about 6.5 log CFU/g at the end of storage.

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21

Aasen, Inga Marie, Sidsel Markussen, Trond Møretrø, Tone Katla, Lars Axelsson, and Kristine Naterstad. "Interactions of the bacteriocins sakacin P and nisin with food constituents." International Journal of Food Microbiology 87, no. 1-2 (October 2003): 35–43. http://dx.doi.org/10.1016/s0168-1605(03)00047-3.

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22

Cocolin, Luca, and Kalliopi Rantsiou. "Sequencing and expression analysis of sakacin genes in Lactobacillus curvatus strains." Applied Microbiology and Biotechnology 76, no. 6 (August 10, 2007): 1403–11. http://dx.doi.org/10.1007/s00253-007-1120-8.

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23

Trinetta, Valentina, Manuela Rollini, Sara Limbo, and Matilde Manzoni. "Influence of temperature and sakacin A concentration on survival ofListeria innocua cultures." Annals of Microbiology 58, no. 4 (December 2008): 633–39. http://dx.doi.org/10.1007/bf03175568.

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24

Moretro, T., I. M. Aasen, I. Storro, and L. Axelsson. "Production of sakacin P by Lactobacillus sakei in a completely defined medium." Journal of Applied Microbiology 88, no. 3 (March 2000): 536–45. http://dx.doi.org/10.1046/j.1365-2672.2000.00994.x.

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25

Barbiroli, Alberto, Alida Musatti, Giorgio Capretti, Stefania Iametti, and Manuela Rollini. "Sakacin-A antimicrobial packaging for decreasingListeriacontamination in thin-cut meat: preliminary assessment." Journal of the Science of Food and Agriculture 97, no. 3 (November 27, 2016): 1042–47. http://dx.doi.org/10.1002/jsfa.8120.

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26

Mohammed, SSD, D. Damisa, TV Balogu, and E. Bala. "Efficacy of Sakacin on Selected Food Pathogenic Microorganisms Isolated from Fermented Milk Products." Journal of Applied Sciences and Environmental Management 20, no. 1 (May 6, 2016): 97. http://dx.doi.org/10.4314/jasem.v20i1.12.

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27

Uteng, Marianne, Håvard H. Hauge, Phineus R. L. Markwick, Gunnar Fimland, Dimitris Mantzilas, Jon Nissen-Meyer, and Claudia Muhle-Goll. "Three-Dimensional Structure in Lipid Micelles of the Pediocin-like Antimicrobial Peptide Sakacin P and a Sakacin P Variant That Is Structurally Stabilized by an Inserted C-Terminal Disulfide Bridge†." Biochemistry 42, no. 39 (October 2003): 11417–26. http://dx.doi.org/10.1021/bi034572i.

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28

Samelis, J., Sibel Roller, and J. Metaxopoulos. "Sakacin B, a bacteriocin produced by Lactobacillus sake isolated from Greek dry fermented sausages." Journal of Applied Bacteriology 76, no. 5 (May 1994): 475–86. http://dx.doi.org/10.1111/j.1365-2672.1994.tb01105.x.

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29

Holck, A., L. Axelsson, S. E. Birkeland, T. Aukrust, and H. Blom. "Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706." Journal of General Microbiology 138, no. 12 (December 1, 1992): 2715–20. http://dx.doi.org/10.1099/00221287-138-12-2715.

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30

Trinetta, Valentina, Manuela Rollini, and Matilde Manzoni. "Development of a low cost culture medium for sakacin A production by L. sakei." Process Biochemistry 43, no. 11 (November 2008): 1275–80. http://dx.doi.org/10.1016/j.procbio.2008.07.011.

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31

Chen, Haiqin, Fengwei Tian, Shuo Li, Yan Xie, Hao Zhang, and Wei Chen. "Cloning and heterologous expression of a bacteriocin sakacin P from Lactobacillus sakei in Escherichia coli." Applied Microbiology and Biotechnology 94, no. 4 (January 31, 2012): 1061–68. http://dx.doi.org/10.1007/s00253-012-3872-z.

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32

Gao, Yurong, Dapeng Li, and Xiaoyan Liu. "Evaluation of the factors affecting the activity of sakacin C2 against E. coli in milk." Food Control 30, no. 2 (April 2013): 453–58. http://dx.doi.org/10.1016/j.foodcont.2012.07.013.

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33

Carvalho, Kátia G., Felipe H. S. Bambirra, Jacques R. Nicoli, Jamil S. Oliveira, Alexandre M. C. Santos, Marcelo P. Bemquerer, Antonio Miranda, and Bernadette D. G. M. Franco. "Characterization of multiple antilisterial peptides produced by sakacin P-producing Lactobacillus sakei subsp. sakei 2a." Archives of Microbiology 200, no. 4 (January 18, 2018): 635–44. http://dx.doi.org/10.1007/s00203-018-1477-3.

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34

Tichaczek, P. S., R. F. Vogel, and W. P. Hammes. "Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH 673." Microbiology 140, no. 2 (February 1, 1994): 361–67. http://dx.doi.org/10.1099/13500872-140-2-361.

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35

Halbmayr, Elisabeth, Geir Mathiesen, Thu-Ha Nguyen, Thomas Maischberger, Clemens K. Peterbauer, Vincent G. H. Eijsink, and Dietmar Haltrich. "High-Level Expression of Recombinant β-Galactosidases inLactobacillus plantarumandLactobacillus sakeiUsing a Sakacin P-Based Expression System." Journal of Agricultural and Food Chemistry 56, no. 12 (June 2008): 4710–19. http://dx.doi.org/10.1021/jf073260+.

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D'ANGELIS, C. E. M., A. C. M. POLIZELLO, M. C. NONATO, A. C. C. SPADARO, and E. C. P. DE MARTINIS. "PURIFICATION, CHARACTERIZATION AND N-TERMINAL AMINO ACID SEQUENCING OF SAKACIN 1, A BACTERIOCIN PRODUCED BYLACTOBACILLUS SAKEI1." Journal of Food Safety 29, no. 4 (November 2009): 636–49. http://dx.doi.org/10.1111/j.1745-4565.2009.00183.x.

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GOMES, BRUNA C., MARINA R. RODRIGUES, LIZZIANE K. WINKELSTRÖTER, AURO NOMIZO, and ELAINE C. P. DE MARTINIS. "In Vitro Evaluation of the Probiotic Potential of Bacteriocin Producer Lactobacillus sakei 1." Journal of Food Protection 75, no. 6 (June 1, 2012): 1083–89. http://dx.doi.org/10.4315/0362-028x.jfp-11-523.

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Lactobacillus sakei 1 is a food isolate that produces a heat-stable antimicrobial peptide (sakacin 1, a class IIa bacteriocin) inhibitory to the opportunistic pathogen Listeria monocytogenes. Bacterial isolates with antimicrobial activity may be useful for food biopreservation and also for developing probiotics. To evaluate the probiotic potential of L. sakei 1, it was tested for (i) in vitro gastric resistance (with synthetic gastric juice adjusted to pH 2.0, 2.5, or 3.0); (ii) survival and bacteriocin production in the presence of bile salts and commercial prebiotics (inulin and oligofructose); (iii) adhesion to Caco-2 cells; and (iv) effect on the adhesion of L. monocytogenes to Caco-2 cells and invasion of these cells by the organism. The results showed that L. sakei 1 survival in gastric environment varied according to pH, with the maximum survival achieved at pH 3.0, despite a 4-log reduction of the population after 3 h. Regarding the bile salt tolerance and influence of prebiotics, it was observed that L. sakei 1 survival rates were similar (P > 0.05) for all de Man Rogosa Sharpe (MRS) broth formulations when tests were done after 4 h of incubation. However, after incubation for 24 h, the survival of L. sakei 1 in MRS broth was reduced by 1.8 log (P <0.001), when glucose was replaced by either inulin or oligofructose (without Oxgall). L. sakei 1 was unable to deconjugate bile salts, and there was a significant decrease (1.4 log) of the L. sakei 1 population in regular MRS broth plus Oxgall (P < 0.05). In spite of this, tolerance levels of L. sakei 1 to bile salts were similar in regular MRS broth and in MRS broth with oligofructose. Lower bacteriocin production was observed in MRS broth when inulin (3,200 AU/ml) or oligofructose (2,400 AU/ml) was used instead of glucose (6,400 AU/ml). L. sakei 1 adhered to Caco-2 cells, and its cell-free pH-neutralized supernatant containing sakacin 1 led to a significant reduction of in vitro listerial invasion of human intestinal Caco-2 cells.

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Fimland, Gunnar, Ralph Jack, Günther Jung, Ingolf F. Nes, and Jon Nissen-Meyer. "The Bactericidal Activity of Pediocin PA-1 Is Specifically Inhibited by a 15-mer Fragment That Spans the Bacteriocin from the Center toward the C Terminus." Applied and Environmental Microbiology 64, no. 12 (December 1, 1998): 5057–60. http://dx.doi.org/10.1128/aem.64.12.5057-5060.1998.

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ABSTRACT A 15-mer peptide fragment derived from pediocin PA-1 (from residue 20 to residue 34) specifically inhibited the bactericidal activity of pediocin PA-1. The fragment did not inhibit the pediocin-like bacteriocins sakacin P, leucocin A, and curvacin A to nearly the same extent as it inhibited pediocin PA-1. Enterocin A, however, was also significantly inhibited by this fragment, although not as greatly as pediocin PA-1. This is consistent with the fact that enterocin A contains the longest continuous sequence identical to that of pediocin PA-1 in the region spanned by the fragment. The fragment inhibited pediocin PA-1 to a much greater extent than did the other 29 possible 15-mer fragments that span pediocin PA-1. The results suggest that the fragment—by interacting with the target cells and/or pediocin PA-1—interferes specifically with pediocin-target cell interaction.

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Rivas, Franco P., Marcela P. Castro, Marisol Vallejo, Emilio Marguet, and Carmen A. Campos. "Sakacin Q produced by Lactobacillus curvatus ACU-1: Functionality characterization and antilisterial activity on cooked meat surface." Meat Science 97, no. 4 (August 2014): 475–79. http://dx.doi.org/10.1016/j.meatsci.2014.03.003.

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Tichaczek, Petra S., Jon Nissen-Meyer, Ingolf F. Nes, Rudi F. Vogel, and Walter P. Hammes. "Characterization of the Bacteriocins Curvacin A from Lactobacillus curvatus LTH1174 and Sakacin P from L. sake LTH673." Systematic and Applied Microbiology 15, no. 3 (August 1992): 460–68. http://dx.doi.org/10.1016/s0723-2020(11)80223-7.

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41

Axelsson, L., and A. Holck. "The genes involved in production of and immunity to sakacin A, a bacteriocin from Lactobacillus sake Lb706." Journal of bacteriology 177, no. 8 (1995): 2125–37. http://dx.doi.org/10.1128/jb.177.8.2125-2137.1995.

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Mapelli, Chiara, Alida Musatti, Alberto Barbiroli, Seema Saini, Julien Bras, Daniele Cavicchioli, and Manuela Rollini. "Cellulose nanofiber (CNF)–sakacin‐A active material: production, characterization and application in storage trials of smoked salmon." Journal of the Science of Food and Agriculture 99, no. 10 (April 23, 2019): 4731–38. http://dx.doi.org/10.1002/jsfa.9715.

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43

Hugas, M., M. Garriga, M. Pascual, M. T. Aymerich, and J. M. Monfort. "Enhancement of sakacin K activity against Listeria monocytogenes in fermented sausages with pepper or manganese as ingredients." Food Microbiology 19, no. 5 (October 2002): 519–28. http://dx.doi.org/10.1006/fmic.2002.0497.

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da Costa, Roger J., Flávia L. S. Voloski, Rafael G. Mondadori, Eduarda H. Duval, and Ângela M. Fiorentini. "Preservation of Meat Products with Bacteriocins Produced by Lactic Acid Bacteria Isolated from Meat." Journal of Food Quality 2019 (January 10, 2019): 1–12. http://dx.doi.org/10.1155/2019/4726510.

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Bacteriocins are ribosomal-synthesized antimicrobial peptides that inhibit the growing of pathogenic and/or deteriorating bacteria. The most studied bacteriocin-producing microorganisms are lactic acid bacteria (LAB), as they have great potential application in food biopreservation, since the majority have GRAS (Generally Recognized as Safe) status. The LAB-producing bacteriocins and/or bacteriocins produced by these bacteria have been widely studied, with the emphasis on those derived from milk and dairy products. On the other hand, isolates from meat and meat products are less studied. The objective of this review is to address the main characteristics, classification, and mechanism of action of bacteriocins and their use in food, to highlight studies on the isolation of LAB with bacteriocinogenic potential from meat and meat products and also to characterize, purify, and apply these bacteriocins in meat products. In summary, most of the microorganisms studied areLactococcus,Enterococcus,Pediococcus, andLactobacillus, which produce bacteriocins such as nisin, enterocin, pediocin, pentocin, and sakacin, many with the potential for use in food biopreservation.

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Axelsson, L., A. Holck, S. E. Birkeland, T. Aukrust, and H. Blom. "Cloning and nucleotide sequence of a gene from Lactobacillus sake Lb706 necessary for sakacin A production and immunity." Applied and Environmental Microbiology 59, no. 9 (1993): 2868–75. http://dx.doi.org/10.1128/aem.59.9.2868-2875.1993.

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Tessema, Girum Tadesse, Trond Møretrø, Lars Snipen, Lars Axelsson, and Kristine Naterstad. "Global Transcriptional Analysis of Spontaneous Sakacin P-Resistant Mutant Strains of Listeria monocytogenes during Growth on Different Sugars." PLoS ONE 6, no. 1 (January 6, 2011): e16192. http://dx.doi.org/10.1371/journal.pone.0016192.

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Katla, T., T. Møretrø, I. M. Aasen, A. Holck, L. Axelsson, and K. Naterstad. "Inhibition of Listeria monocytogenes in cold smoked salmon by addition of sakacin P and/or liveLactobacillus sakei cultures." Food Microbiology 18, no. 4 (August 2001): 431–39. http://dx.doi.org/10.1006/fmic.2001.0420.

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MOTLAGH, ALI M., MONTY C. JOHNSON, and BIBEK RAY. "Viability Loss of Foodborne Pathogens by Starter Culture Metabolites." Journal of Food Protection 54, no. 11 (November 1, 1991): 873–78. http://dx.doi.org/10.4315/0362-028x-54.11.873.

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Antibacterial metabolites produced by starter culture bacteria were tested for inhibitory properties against foodborne pathogens capable of growing in foods at refrigeration temperature. Three culture preparations containing the bacteriocins pediocin AcH, nisin, and sakacin A produced by Pediococcus acidilactici H, Lactococcus lactis ssp. lactis DL 16, and Lactobacillus sake 706, respectively, were studied in addition to four commercial preparations: Nisaplin (similar to nisin), Na-lactate, diacetyl and Microgard. All bacteriocin preparations were bactericidal to the Listeria strains tested including nine strains of L. monocytogenes, but not to any of the gram-negative pathogens studied. Some strains of Listeria were lysed by pediocin AcH. Storage studies at 4°C indicated that the bacteriocin preparations did not have bacteriostatic properties against the surviving cells. Diacetyl produced some bactericidal effect against strains of Yersinia enterocolitica, Aeromonas hydrophila, pathogenic Escherichia coli, and Salmonella anatum, but not against Listeria. Lactate had limited bacteriostatic effect against gram-negative pathogens and none against the gram-positive bacteria. Microgard had neither bactericidal nor bacteriostatic action against the bacteria used in this study.

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Mechoud, Mónica Adriana, Ornella Estefanía Álvarez, María Elisa Cayré, Marcela Paola Castro, Carlos Minahk, and Lucila Saavedra. "Sakacin G is the main responsible bacteriocin for the anti-listerial activity of meat-borne Lactobacillus curvatus ACU-1." Annals of Microbiology 67, no. 9 (August 3, 2017): 615–21. http://dx.doi.org/10.1007/s13213-017-1288-9.

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TRINETTA, VALENTINA, JOHN D. FLOROS, and CATHERINE N. CUTTER. "SAKACIN A-CONTAINING PULLULAN FILM: AN ACTIVE PACKAGING SYSTEM TO CONTROL EPIDEMIC CLONES OFLISTERIA MONOCYTOGENESIN READY-TO-EAT FOODS." Journal of Food Safety 30, no. 2 (May 2010): 366–81. http://dx.doi.org/10.1111/j.1745-4565.2010.00213.x.

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