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Biochemistry Research International
Volume 2016 (2016), Article ID 9237418, 10 pages
http://dx.doi.org/10.1155/2016/9237418
Research Article

Halophilic Bacteria of Lunsu Produce an Array of Industrially Important Enzymes with Salt Tolerant Activity

Faculty of Applied Sciences and Biotechnology, Shoolini University of Biotechnology and Management Sciences, Solan, Himachal Pradesh 173212, India

Received 28 September 2015; Revised 8 December 2015; Accepted 16 December 2015

Academic Editor: Angel Catalá

Copyright © 2016 Sonika Gupta et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. Kamekura and M. Enache, “Hydrolytic enzymes of halophilic microorganisms and their economic values,” The Journal of Biochemistry, vol. 47, no. 1, pp. 47–59, 2010. View at Google Scholar
  2. C. S. Sánchez-Porro, S. Martín, E. Mellado, and A. Ventosa, “Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes,” Journal of Applied Microbiology, vol. 94, no. 2, pp. 295–300, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. A. Oren, “Industrial and environmental applications of halophilic microorganisms,” Environmental Technology, vol. 31, no. 8-9, pp. 825–834, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. M. A. Amoozegar, E. Salehghamari, K. Khajeh, M. Kabiri, and S. Naddaf, “Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2,” Journal of Basic Microbiology, vol. 48, no. 3, pp. 160–167, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. D. M. Ruiz and R. E. De Castro, “Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii,” Journal of Industrial Microbiology and Biotechnology, vol. 34, no. 2, pp. 111–115, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. M. De Lourdes Moreno, M. T. García, A. Ventosa, and E. Mellado, “Characterization of Salicola sp. IC10, a lipase- and protease-producing extreme halophile,” FEMS Microbiology Ecology, vol. 68, no. 1, pp. 59–71, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. B. Prakash, M. Vidyasagar, M. S. Madhukumar, G. Muralikrishna, and K. Sreeramulu, “Production, purification, and characterization of two extremely halotolerant, thermostable, and alkali-stable α-amylases from Chromohalobacter sp. TVSP 101,” Process Biochemistry, vol. 44, no. 2, pp. 210–215, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. X. Li and H.-Y. Yu, “Purification and characterization of novel organic-solvent-tolerant β-amylase and serine protease from a newly isolated Salimicrobium halophilum strain LY20,” FEMS Microbiology Letters, vol. 329, no. 2, pp. 204–211, 2012. View at Publisher · View at Google Scholar · View at Scopus
  9. A. Gupta, I. Roy, R. K. Patel, S. P. Singh, S. K. Khare, and M. N. Gupta, “One-step purification and characterization of an alkaline protease from haloalkaliphilic Bacillus sp.,” Journal of Chromatography A, vol. 1075, no. 1-2, pp. 103–108, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. T. Fukushima, T. Mizuki, A. Echigo, A. Inoue, and R. Usami, “Organic solvent tolerance of halophilic α-amylase from a haloarchaeon, Haloarcula sp. strain S-1,” Extremophiles, vol. 9, no. 1, pp. 85–89, 2005. View at Publisher · View at Google Scholar · View at Scopus
  11. F. C. Marhuenda-Egea and M. J. Bonete, “Extreme halophilic enzymes in organic solvents,” Current Opinion in Biotechnology, vol. 13, no. 4, pp. 385–389, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. J. T. Thumar and S. P. Singh, “Organic solvent tolerance of an alkaline protease from salt-tolerant alkaliphilic Streptomyces clavuligerus strain Mit-1,” The Journal of Industrial Microbiology and Biotechnology, vol. 36, no. 2, pp. 211–218, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Gupta, P. Sharma, K. Dev, M. Srivastava, and A. Sourirajan, “A diverse group of halophilic bacteria exist in Lunsu, a natural salt water body of Himachal Pradesh, India,” SpringerPlus, vol. 4, article 274, 2015. View at Publisher · View at Google Scholar
  14. R. Gulati, R. K. Saxena, and R. Gupta, “A rapid plate assay for screening L-asparaginase producing micro-organisms,” Letters in Applied Microbiology, vol. 24, no. 1, pp. 23–26, 1997. View at Publisher · View at Google Scholar · View at Scopus
  15. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Publisher · View at Google Scholar · View at Scopus
  16. G. L. Miller, “Use of dinitrosalicylic acid reagent for determination of reducing sugar,” Analytical Chemistry, vol. 31, no. 3, pp. 426–428, 1959. View at Publisher · View at Google Scholar · View at Scopus
  17. T. Kuberan, S. Sangaralingam, and V. Thirumalaiarasu, “Isolation and optimization of protease producing bacteria from halophilic soil,” Journal of Biosocial Science, vol. 1, no. 3, pp. 163–174, 2010. View at Google Scholar
  18. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951. View at Google Scholar · View at Scopus
  19. A. Imada, S. Igarasi, K. Nakahama, and M. Isono, “Asparaginase and glutaminase activities of micro-organisms,” Journal of General Microbiology, vol. 76, no. 1, pp. 85–99, 1973. View at Publisher · View at Google Scholar · View at Scopus
  20. U. K. Winkler and M. Stuckmann, “Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens,” Journal of Bacteriology, vol. 138, no. 3, pp. 663–670, 1979. View at Google Scholar · View at Scopus
  21. R. Rohban, M. A. Amoozegar, and A. Ventosa, “Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran,” Journal of Industrial Microbiology and Biotechnology, vol. 36, no. 3, pp. 333–340, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Y. Jayachandra, A. B. Parameshwar, R. K. Mohan, and M. B. Sulochana, “Characterization of extracellular hydrolytic enzymes producing extremely halophilic bacterium Virgibacillus sp,” World Journal of Science and Technology, vol. 2, no. 2, pp. 23–26, 2012. View at Publisher · View at Google Scholar
  23. M.-J. Coronado, C. Vargas, J. Hofemeister, A. Ventosa, and J. J. Nieto, “Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana,” FEMS Microbiology Letters, vol. 183, no. 1, pp. 67–71, 2000. View at Publisher · View at Google Scholar · View at Scopus
  24. X. Li and H.-Y. Yu, “Characterization of an organic solvent-tolerant α-amylase from a halophilic isolate, Thalassobacillus sp. LY18,” Folia Microbiologica, vol. 57, no. 5, pp. 447–453, 2012. View at Publisher · View at Google Scholar · View at Scopus
  25. J. Kim and J. S. Dordick, “Unusual salt and solvent dependence of a protease from an extreme halophile,” Biotechnology and Bioengineering, vol. 55, no. 3, pp. 471–479, 1997. View at Publisher · View at Google Scholar · View at Scopus
  26. M. I. Giménez, C. A. Studdert, J. J. Sánchez, and R. E. De Castro, “Extracellular protease of Natrialba magadii: purification and biochemical characterization,” Extremophiles, vol. 4, no. 3, pp. 181–188, 2000. View at Publisher · View at Google Scholar · View at Scopus
  27. C. A. Studdert, M. K. Herrera Seitz, M. I. Plasencia Gil, J. J. Sanchez, and R. E. de Castro, “Purification, biochemical characterization of the haloalkaliphilic archeon Natronococcus occultus extracellular serine protease,” Journal of General Microbiology, vol. 41, no. 6, pp. 375–383, 2001. View at Google Scholar
  28. H. R. Karbalaei-Heidari, M. A. Amoozegar, M. Hajighasemi, A.-A. Ziaee, and A. Ventosa, “Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis,” Journal of Industrial Microbiology & Biotechnology, vol. 36, no. 1, pp. 21–27, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. M. S. Dodia, R. H. Joshi, R. K. Patel, and S. P. Singh, “Characterization and stability of extracellular alkaline proteases from halophilic and alkaliphilic bacteria isolated from saline habitat of coastal Gujarat, India,” Brazilian Journal of Microbiology, vol. 37, no. 3, pp. 276–282, 2006. View at Publisher · View at Google Scholar · View at Scopus
  30. Y. Ghasemi, S. Rasoul-Amini, A. Kazemi, G. Zarrini, M. H. Morowvat, and M. Kargar, “Isolation and characterization of some moderately halophilic bacteria with lipase activity,” Microbiology, vol. 80, no. 4, pp. 483–487, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. R. M. Camacho, J. C. Mateos, O. González-Reynoso, L. A. Prado, and J. Córdova, “Production and characterization of esterase and lipase from Haloarcula marismortui,” Journal of Industrial Microbiology and Biotechnology, vol. 36, no. 7, pp. 901–909, 2009. View at Publisher · View at Google Scholar · View at Scopus
  32. R. M. Camacho, J. C. Mateos-Díaz, D. M. Diaz-Montaño, O. González-Reynoso, and J. Córdova, “Carboxyl ester hydrolases production and growth of a halophilic archaeon, Halobacterium sp. NRC-1,” Extremophiles, vol. 14, no. 1, pp. 99–106, 2010. View at Publisher · View at Google Scholar · View at Scopus
  33. X. Li and H. Y. Yu, “Characterization of novel extracellular lipase from a halophilic isolate Chromohalobacter sp. LY7-8,” African Journal of Microbiology Research, vol. 6, pp. 3516–3522, 2012. View at Google Scholar
  34. W. Kanlayakrit and A. K. Boonpan, “Screening of halophilic lipase-producing bacteria and characterization of enzyme for fish sauce quality improvement,” Kasetsart Journal: Natural Science, vol. 41, pp. 576–585, 2007. View at Google Scholar
  35. M. Wakayama, T. Yamagata, A. Kamemura et al., “Characterization of salt-tolerant glutaminase from Stenotrophomonas maltophilia NYW-81 and its application in Japanese soy sauce fermentation,” Journal of Industrial Microbiology and Biotechnology, vol. 32, no. 9, pp. 383–390, 2005. View at Publisher · View at Google Scholar · View at Scopus
  36. K. Koibuchi, H. Nagasaki, A. Yuasa, J. Kataoka, and K. Kitamoto, “Molecular cloning and characterization of a gene encoding glutaminase from Aspergillus oryzae,” Applied Microbiology and Biotechnology, vol. 54, no. 1, pp. 59–68, 2000. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Moriguchi, K. Sakai, R. Tateyama, Y. Furuta, and M. Wakayama, “Isolation and characterization of salt-tolerant glutaminases from marine Micrococcus luteus K-3,” Journal of Fermentation and Bioengineering, vol. 77, no. 6, pp. 621–625, 1994. View at Publisher · View at Google Scholar · View at Scopus