Journal of Applied Biological Chemistry

The Korean Society for Applied Biological Chemistry (한국응용생명화학회)
권호 표지
DOI QR코드

DOI QR Code

Chitinase-producing Salinivibrio bacteria isolated from salt-fermented shrimp with antimicrobial and safety assessments

  • Le, Bao (Department of Biotechnology, Chonnam National University) ;
  • Chung, Gyuhwa (Department of Biotechnology, Chonnam National University) ;
  • Yang, Seung Hwan (Department of Biotechnology, Chonnam National University)
  • Received : 2018.05.23
  • Accepted : 2018.07.26
  • Published : 2018.09.29
Download PDF
⟨ Previous Next ⟩

Abstract

Chitinases are glycosyl hydrolases which cleave the ${\beta}$-1,4 linkage of chitin into oligo or monomers of N-acetylglucosamine. These bacterial enzymes have been used for a wide range of applications in the food and pharmaceutical industries. In this study, we isolated two potential chitinolytic strains, BAO-01 and BAO-02, from salt-fermented shrimp, which were shown to belong to the genus Salinivibrio through genetic characterization using 16S rRNA. These isolates were gram-positive, rod-shaped, and non-spore forming. BAO-01 showed greater growth and chitinase activity than BAO-02 after the incubation at $37^{\circ}C$ for 4 days. Both strains grew on a wide range of carbon and nitrogen sources, pH values, temperatures, and salt levels. However, they showed minor biochemical differences. In addition, their antimicrobial activities against foodborne pathogens and antibiotic susceptibilities were evaluated. These Salinivibrio spp. did not show bioamine production, hemolytic activity, and mucin degradation. Therefore, the in vitro screening results suggested that these bacteria could be widely used as new candidates for chitin hydrolyzation and seafood fermentation.

Keywords

References

  1. Koo OK, Lee SJ, Chung KR, Jang DJ, Yang HJ, Kwon DY (2016) Korean traditional fermented fish products: jeotgal. J Ethn Foods 3: 107-116 https://doi.org/10.1016/j.jef.2016.06.004
  2. Guan L, Cho KH, Lee J-H (2011) Analysis of the cultivable bacterial community in jeotgal, a Korean salted and fermented seafood, and identification of its dominant bacteria. Food Microbiol 28: 101-113
  3. Chandrasekaran M, Enzymes in food and beverage processing (2015) CRC Press, Boca Raton
  4. Adrangi S, Faramarzi MA (2013) From bacteria to human: a journey into the world of chitinases. Biotechnol Adv 31: 1786-1795 https://doi.org/10.1016/j.biotechadv.2013.09.012
  5. Yan Q, Fong SS (2015) Bacterial chitinase: nature and perspectives for sustainable bioproduction. Bioresour Bioprocess 2: 31 https://doi.org/10.1186/s40643-015-0057-5
  6. Bhattacharya D, Nagpure A, Gupta RK (2007) Bacterial chitinases: properties and potential. Crit Rev Biotechnol 27: 21-28 https://doi.org/10.1080/07388550601168223
  7. Lane D (1991) 16S/23S rRNA sequencing, Wiley, Chichester, UK
  8. Kumar S, Stecher G, Tamura K (2016) MEGA7: Molecular evolutionary genetics analysis version 7.0 for bigger datasets. Mol Biol Evol 33:1870-1874 https://doi.org/10.1093/molbev/msw054
  9. Monreal J, Reese ET (1969) The chitinase of Serratia marcescens. Can J Microbiol 15: 689-696 https://doi.org/10.1139/m69-122
  10. Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31: 426-428 https://doi.org/10.1021/ac60147a030
  11. Wiegand I, Hilpert K, Hancock REW (2008) Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances. Nat Protoc 3: 163-175 https://doi.org/10.1038/nprot.2007.521
  12. Bauer AW, Kirby WM, Sherris JC, Turck M (1966) Antibiotic susceptibility testing by a standardized single disk method. Am J Clin Pathol 45: 493 https://doi.org/10.1093/ajcp/45.4_ts.493
  13. Bover-Cid S, Holzapfel WH (1999) Improved screening procedure for biogenic amine production by lactic acid bacteria. Int J Food Microbiol 53: 33-41 https://doi.org/10.1016/S0168-1605(99)00152-X
  14. Zhou JS, Gopal PK, Gill HS (2001) Potential probiotic lactic acid bacteria Lactobacillus rhamnosus (HN001), Lactobacillus acidophilus (HN017) and Bifidobacterium lactis (HN019) do not degrade gastric mucin in vitro. Int J Food Microbiol 63: 81-90 https://doi.org/10.1016/S0168-1605(00)00398-6
  15. Semedo T, Santos MA, Martins P, Lopes MFS, Marques JJF, Tenreiro R, Crespo MTB (2003) Comparative study using type strains and clinical and food isolates to examine hemolytic activity and occurrence of the cyl operon in enterococci. J Clin Microbiol 41: 2569-2576 https://doi.org/10.1128/JCM.41.6.2569-2576.2003
  16. Kumar S, Karan R, Kapoor S, Singh SP, Khare SK (2012) Screening and isolation of halophilic bacteria producing industrially important enzymes. Braz J Microbiol 43: 1595-1603 https://doi.org/10.1590/S1517-83822012000400044
  17. Gorriti MF, Dias GM, Chimetto LA, Trindade-Silva AE, Silva BS, Mesquita MMA, Gregoracci GB, Farias ME, Thompson CC, Thompson FL (2014) Genomic and phenotypic attributes of novel salinivibrios from stromatolites, sediment and water from a high altitude lake. BMC Genomics 15: 473 https://doi.org/10.1186/1471-2164-15-473
  18. Sanchart C, Benjakul S, Rattanaporn O, Haltrich D, Maneerat S (2015) Efficiency of the V3 region of 16S rDNA and the rpoB gene for bacterial community detection in Thai traditional fermented shrimp (Kung-Som) using PCR-DGGE techniques. Songklanakarin J Sci Technolog 37: 291-297
  19. Wang C-Y, Hsieh Y-R, Ng C-C, Chan H, Lin H-T, Tzeng W-S, Shyu YT (2009) Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05. Enzyme Microb Technol 44: 373-379 https://doi.org/10.1016/j.enzmictec.2009.02.006
  20. Amoozegar MA, Salehghamari E, Khajeh K, Kabiri M, Naddaf S (2008) Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA2. J Basic Microbiol 48:160-167 https://doi.org/10.1002/jobm.200700361
  21. Lama L, Romano I, Calandrelli V, Nicolaus B, Gambacorta A (2005) Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus. Res Microbiol 156: 478-484 https://doi.org/10.1016/j.resmic.2004.12.004
  22. Aunpad R, Panbangred W (2003) Cloning and characterization of the constitutively expressed chitinase C gene from a marine bacterium, Salinivibrio costicola strain 5SM-1. J Biosci Bioeng 96: 529-536 https://doi.org/10.1016/S1389-1723(04)70145-0
  23. Vaidya RJ, Shah IM, Vyas PR, Chhatpar HS (2001) Production of chitinase and its optimization from a novel isolate Alcaligenes xylosoxydans: potential in antifungal biocontrol. World J Microbiol Biotechnol 17: 691-696 https://doi.org/10.1023/A:1012927116756
  24. Han KI, Patnaik BB, Kim YH, Kwon HJ, Han YS, Han MD (2014) Isolation and characterization of chitinaseproducing Bacillus and Paenibacillus strains from salted and fermented shrimp, Acetes japonicus. J Food Sci 79
  25. Kim TI, Ki KS, Lim DH, Vijayakumar M, Park SM, Choi SH, Kim KY, Im SK, Park BY (2017) Novel Acinetobacter parvus HANDI 309 microbial biomass for the production of N-acetyl-$\beta$-D-glucosamine (GlcNAc) using swollen chitin substrate in submerged fermentation. Biotechnology for biofuels 10: 59 https://doi.org/10.1186/s13068-017-0740-1
  26. Kapat A, Rakshit SK, Panda T (1996) Optimization of carbon and nitrogen sources in the medium and environmental factors for enhanced production of chitinase by Trichoderma harzianum. Bioprocess Eng 15:13-20 https://doi.org/10.1007/BF00435522
  27. Kuddus M, Ahmad I (2013) Isolation of novel chitinolytic bacteria and production optimization of extracellular chitinase. Journal of Genetic Engineering and Biotechnology 11: 39-46 https://doi.org/10.1016/j.jgeb.2013.03.001
  28. Singh A, Mehta G, Chhatpar H (2009) Optimization of medium constituents for improved chitinase production by Paenibacillus sp. D1 using statistical approach. Lett Appl Microbiol 49: 708-714 https://doi.org/10.1111/j.1472-765X.2009.02731.x
  29. Amoozegar MA, Schumann P, Hajighasemi M, Fatemi AZ, Karbalaei-Heidari HR (2008) Salinivibrio proteolyticus sp. nov., a moderately halophilic and proteolytic species from a hypersaline lake in Iran. Int J Syst Evol Microbiol 58: 1159-1163 https://doi.org/10.1099/ijs.0.65423-0
  30. Chamroensaksri N, Tanasupawat S, Akaracharanya A, Visessanguan W, Kudo T, Itoh T (2009) Salinivibrio siamensis sp. nov., from fermented fish (pla-ra) in Thailand. Int J Syst Evol Microbiol 59: 880-885 https://doi.org/10.1099/ijs.0.001768-0

Cited by

  1. Anti-aging skin and antioxidant assays of protein hydrolysates obtained from salted shrimp fermented with Salinivibrio cibaria BAO-01 vol.63, pp.3, 2020, https://doi.org/10.3839/jabc.2020.028