Penicillin Binding Protein from Pediococcus acidilactici Isolated from Nuruk for Food Biopreservative
Abstract
Background: Korean traditional nuruk, consisting of a variety of microorganisms, is widely used in traditional liquor materials. The present study evaluated the antimicrobial activity of strains isolated from Korean traditional nuruk in 2016.
Methods: The strain was isolated from Korea traditional nuruk and performed antimicrobial activities using the paper disc test and phylogenetic analysis using 16S rRNA sequencing. The bacteriocin was identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
Results: The isolate, S-2, demonstrated highest antibacterial activity against various gram-positive and gram-negative pathogens, including Klebsiella pneumoniae, Salmonella enterica subsp. enterica, Bacillus subtilis, B. cereus, Escherichia coli and Shigella flexneri. The isolated was identified as P. acidilactici, by 16S rRNA sequence analysis. Antibacterial activity of P. acidilactici was retained over a wide temperature range. And the P. acidilactici strains remained active over a wide pH range. However, reduced activities were obtained at alkaline pH. When the bacteriocins from this strain were treated with proteolytic enzymes, loss of antibacterial activity was observed. No effect in the activity, however, was observed upon treatment with α-amylase, β-amylase, lipases, proteases, and proteinase K. The molecular weight of bacteriocins was estimated to be approximately 51 kDa. Using MALDI-TOF/MS, the bacteriocins were identified as a putative penicillin binding protein.
Conclusion: This study is the first report of isolation of bacteriocin with the above mode of actions from Korean traditional nuruk. The bacteriocins produced by the strain have potential applications in food preservation.
2. Erkkila S, Petaja E (2000). Screening of commercial meat starter cultures at low pH and in the presence of bile salts for potential probiotic use. Meat Sci, 55(3): 297–300.
3. Albano H, Todorov SD, van Reenen CA, et al (2007). Characterization of two bacteriocins produced by Pediococcus acidilactici isolated from "Alheira", a fermented sausage traditionally produced in Portugal. Int J Food Microbiol, 116(2): 239-47.
4. Milkulski D, Jankowski J, Naczmanski J, et al (2012). Effects of dietary probiotic (Pediococcus acidilactici) supplementation on performance, nutrient digestibility, egg traits, egg yolk cholesterol, and fatty acid profile in laying hens. Poult Sci, 91(10): 2691-700.
5. Cardona E, Gueguen Y, Magre K, et al (2016). Bacterial community characteriza-tion of water and intestine of the shrimp Litopenaeus stylirostris in a biofloc system. BMC Microbiol, 16:157.
6. Cleveland J, Montville TJ, Nes IF, Chikindas ML (2001). Bacteriocins : safe, natural antimicrobials for food preservation. Int J Food Microbiol, 71(1): 1-20.
7. Perez RH, Zendo T, Sonomoto K (2014). Novel bacteriocins from lactic acid bacteria (LAB) various structures and applications. Microb Cell fact, 13(Suppl 1):S3.
8. Prabhu SS, Mohan RK, Sanhita P, Ravindra R (2014). Production of bacteriocin and biosynthesis of silver nanoparticle by lactic acid bacteria isolated from yoghurt and its antibacterial activity. SIRJ-MBT, 1(3): 7-14.
9. Rajaram G, Manivasagan P, Thilagavathi B, Saravanakumar A (2010). Purification and Characterization of a Bacteriocin Produced by Lactobacillus lactis Isolated from Marine Environment. Adv J Food Sci Technol, 2(2): 138-44.
10. Nghe DV, Nguyen THK (2014). Characterization of antimicrobial activities of Pediococcus pentosaceus Vtcc-B-601. J App Pharm Sci, 4(5): 061-064.
11. Jack RW, Tagg JR, Ray B (1995). Bacteriocins of gram-positive bacteria. Microbiol Rev, 59(2): 171-200.
12. Jimenez DR, Rios-Sánchez RM, Desmazeaud M, et al (1993). Plantaricins S and T, two new bacteriocins produced by lactobacillus plantarum LPCO 10 isolated from a green olive fermentation. Appl Environ Microbiol, 59(5): 1416-24.
13. Klaenhammer TR (1988). Bacteriocins of lactic acid bacteria. Biochimie, 70(3): 337-49.
14. Tagg JR, Daiani AS, Wannamaker LW (1976). Bacteriocin of gram-positive bacteria. Bacteriol Rev, 40(3): 722-56.
15. Lv LX, Li YD, Hu XJ, et al. (2014). Whole-genome sequence assembly of Pediococcus pentosaceus LI05 (CGMCC 7049) from the human gastrointestinal tract and comparative analysis with representative sequences from three food-borne strains. Gut Pathog, 6: 36.
16. Suzuki H, Nishimura Y, Hirota Y (1978). On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc Natl Acad Sci U S A, 75(2): 664–8.
17. Abbasiliasi S, Tan JS, Ibrahim TA, et al (2012). Isolation of Pediococcus acidilactici Kp10 with ability to secrete bacteriocin-like inhibitory substance from milk products for applications in food industry. BMC Microbiol, 12: 260.
18. Cosansu S, Geornaras I, Ayhan K, Sofos JN (2010). Control of Listeria monocyto-genes by bacteriocin-producing Pediococcus acidilactici 13 and its antimicrobial sub-stance in a dry fermented sausage sucuk and in turkey breast. J Food Nutr Res, 49(4): 206-14.
19. Schved F, Lalazar Y, Henis Y, Juven BJ (1993). Purification, partial characterization and plasmid-linkage of pediocin SJ-1, a bacteriocin produced by Pediococcus acidilactici. J Appl Bacteriol, 74(1): 67-77.
20. Specht KM, Sheetz KH, Alexander CM, et al (2010). Expression and Characterization of Penicillin-Binding Proteins in Burkholderia cenocepacia. Curr Microbiol, 60(4): 274–79.
21. Vashist J, Tiwari V, Das R, et al. (2011). Analysis of penicillin-binding proteins (PBPs) in carbapenem resistant Acinetobacter baumannii. Indian J Med Res, 133: 332-38.
22. el Kharroubi A, Jacques P, Piras G, et al. (1991). The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2' are similar. Biochem J, 280(Pt 2): 463-69.
23. Rattanachaikunsopon P, Phumkhachorn P (2010). Lactic acid bacteria: their antimicrobial compounds and their uses in food production. Ann Biol Res, 1(4): 218-28
24. Goffin C, Ghuysen JM (2002). Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox : presence of penicillin-susceptible target protein versus lack of efficiency of penicillin as therapeutic agent. Microbiol Mol Biol Rev, 66(4): 702-38.
| Files | ||
| Issue | Vol 47 No 11 (2018) | |
| Section | Original Article(s) | |
| Keywords | ||
| Nuruk, Pediococcus acidilactici, Bacteriocin, Penicillin binding protein | ||
| Rights and permissions | |
|
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License. |
