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BioMed Research International
Volume 2015, Article ID 140726, 10 pages
http://dx.doi.org/10.1155/2015/140726
Review Article

Biotechnological Aspects and Perspective of Microbial Keratinase Production

1Institute of Nano Electronic Engineering (INEE), Universiti Malaysia Perlis, 01000 Kangar, Perlis, Malaysia
2Advanced Medical & Dental Institute (AMDI), Universiti Sains Malaysia, 13200 Kepala Batas, Penang, Malaysia
3Department of Oral Biology & Biomedical Sciences and OCRCC, Faculty of Dentistry, University of Malaya, 50603 Kuala Lumpur, Malaysia
4Department of Biological Engineering, College of Engineering, Inha University, Incheon 402-751, Republic of Korea

Received 14 October 2014; Accepted 10 December 2014

Academic Editor: Bidur P. Chaulagain

Copyright © 2015 Subash C. B. Gopinath 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. A. L. Martínez-Hernández and C. Velasco-Santos, “Keratin fibers from chicken feathers: structure and advances in polymer composites,” in Keratin: Structure, Properties and Applications, R. Dullaart and J. Mousquès, Eds., pp. 149–211, Nova Science Publishers, 2012. View at Google Scholar
  2. A. M. Fortier and M. Cadrin, “Simple epithelial keratins k8 and k18: from structural to regulatory protein,” in Keratin: Structure, Properties and Applications, R. Dullaart and J. Mousquès, Eds., pp. 1–35, Nova Science Publishers, 2012. View at Google Scholar
  3. R. Kanchana, “Farm waste recycling through microbial keratinases,” Journal of Applied Sciences in Environmental Sanitation, vol. 7, no. 2, pp. 103–108, 2012. View at Google Scholar
  4. C.-H. Lee, M.-S. Kim, B. M. Chung, D. J. Leahy, and P. A. Coulombe, “Structural basis for heteromeric assembly and perinuclear organization of keratin filaments,” Nature Structural and Molecular Biology, vol. 19, no. 7, pp. 707–715, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. P. Anbu, S. C. B. Gopinath, A. Hilda, T. Lakshmi Priya, and G. Annadurai, “Purification of keratinase from poultry farm isolate-Scopulariopsis brevicaulis and statistical optimization of enzyme activity,” Enzyme and Microbial Technology, vol. 36, no. 5-6, pp. 639–647, 2005. View at Publisher · View at Google Scholar · View at Scopus
  6. M. N. Acda, “Waste chicken feather as reinforcement in cement-bonded composites,” Philippine Journal of Science, vol. 139, no. 2, pp. 161–166, 2010. View at Google Scholar · View at Scopus
  7. M. A. Ganaie, S. Sood, G. Rizvi, and T. A. Khan, “Isolation and identification of keratinophilic fungi from different soil samples in Jhansi City (India),” Plant Pathology Journal, vol. 9, no. 4, pp. 194–197, 2010. View at Publisher · View at Google Scholar
  8. R. Kumar, R. Mishra, S. Maurya, and H. B. Sahu, “Isolation and identification of keratinophilic fungi from garbage waste soils of Jharkhand region of India,” European Journal of Experimental Biology, vol. 3, no. 3, pp. 600–604, 2013. View at Google Scholar
  9. H. C. Gugnani, “Non-dermatophytic filamentous keratinophilic fungi and their role in human infections,” in Biology of Dermatophytes and Other Keratinophilic Fungi, R. K. S. Kushwaha and J. Guarro, Eds., pp. 109–114, Revista Iberoamericana de Micologia Apartado, Bilbao, Spain, 2000. View at Google Scholar
  10. K. Pakshir, M. Rahimi Ghiasi, K. Zomorodian, and A. R. Gharavi, “Isolation and molecular identification of keratinophilic fungi from public parks soil in Shiraz, Iran,” BioMed Research International, vol. 2013, Article ID 619576, 5 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  11. V. M. Ramesh and A. Hilda, “Incidence of keratinophilic fungi in the soil of primary schools and public parks of Madras city, India,” Mycopathologia, vol. 143, no. 3, pp. 139–145, 1998. View at Publisher · View at Google Scholar · View at Scopus
  12. S. Shadzi, M. Chadeganipour, and M. Alimoradi, “Isolation of keratinophilic fungi from elementary schools and public parks in Isfahan, Iran,” Mycoses, vol. 45, no. 11-12, pp. 496–499, 2002. View at Publisher · View at Google Scholar · View at Scopus
  13. P. Anbu, A. Hilda, and S. C. B. Gopinath, “Keratinophilic fungi of poultry farm and feather dumping soil in Tamil Nadu, India,” Mycopathologia, vol. 158, no. 3, pp. 303–309, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. H. C. Gugnani, S. Sharma, B. Gupta, and S. Gaddam, “Prevalence of keratinophilic fungi in soils of St. Kitts and Nevis,” Journal of Infection in Developing Countries, vol. 6, no. 4, pp. 347–351, 2012. View at Google Scholar · View at Scopus
  15. R. Kachuei, M. Emami, B. Naeimi, and K. Diba, “Isolation of keratinophilic fungi from soil in Isfahan province, Iran,” Journal de Mycologie Medicale, vol. 22, no. 1, pp. 8–13, 2012. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Z. Mahmoudabadi and M. Zarrin, “Isolation of dermatophytes and related keratinophilic fungi from the two public parks in Ahvaz,” Jundishapur Journal of Microbiology, vol. 1, no. 1, pp. 20–23, 2008. View at Google Scholar
  17. R. J. Yu, S. R. Harmon, and F. Blank, “Isolation and purification of an extracellular keratinase of Trichophyton mentagrophytes,” Journal of Bacteriology, vol. 96, no. 4, pp. 1435–1436, 1968. View at Google Scholar · View at Scopus
  18. M. Asahi, R. Lindquist, K. Fukuyama, G. Apodaca, W. L. Epstein, and J. H. McKerrow, “Purification and characterization of major extracellular proteinases from Trichophyton rubrum,” Biochemical Journal, vol. 232, no. 1, pp. 139–144, 1985. View at Google Scholar · View at Scopus
  19. C. M. Williams, C. S. Richter, J. M. MacKenzie Jr., and J. C. H. Shih, “Isolation, identification and characterization of a feather-degrading bacterium,” Applied and Environmental Microbiology, vol. 56, no. 6, pp. 1509–1515, 1990. View at Google Scholar · View at Scopus
  20. V. Matikevicienė, D. Masiliuniene, and S. Grigiskis, “Degradation of keratin containing wastes by bacteria with keratinolytic activity,” in Proceedings of the 7th International Scientific and Practical Conference, vol. 1, pp. 284–289, 2009.
  21. R. Gupta and P. Ramnani, “Microbial keratinases and their prospective applications: an overview,” Applied Microbiology and Biotechnology, vol. 70, no. 1, pp. 21–33, 2006. View at Publisher · View at Google Scholar · View at Scopus
  22. H. Korkmaz, H. Hür, and S. Dinçer, “Dincer, Characterization of alkaline keratinase of Bacillus licheniformis strain HK-1 from poultry waste,” Annals of Microbiology, vol. 54, no. 2, pp. 201–211, 2004. View at Google Scholar · View at Scopus
  23. M. M. Hoq, K. A. Z. Siddiquee, H. Kawasaki, and T. Seki, “Keratinolytic activity of some newly isolated Bacillus species,” Journal of Biological Sciences, vol. 5, no. 2, pp. 193–200, 2005. View at Publisher · View at Google Scholar
  24. S. G. Joshi, M. M. Tejashwini, N. Revati, R. Sridevi, and D. Roma, “Isolation, identification and characterization of a feather degrading bacterium,” International Journal of Poultry Science, vol. 6, no. 9, pp. 689–693, 2007. View at Publisher · View at Google Scholar · View at Scopus
  25. C.-G. Cai, B.-G. Lou, and X.-D. Zheng, “Keratinase production and keratin degradation by a mutant strain of Bacillus subtilis,” Journal of Zhejiang University Science B, vol. 9, no. 1, pp. 60–67, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Cortezi, J. Contiero, C. J. B. de Lima, R. B. Lovaglio, and R. Monti, “Characterization of a feather degrading by Bacillus amyloliquefaciens protease: a new strain,” World Journal of Agricultural Sciences, vol. 4, no. 5, pp. 648–656, 2008. View at Google Scholar
  27. R. Sapna and V. Yamini, “Study of keratin degradation by some potential bacterial isolates from soil,” Journal of Soil Science, vol. 1, no. 1, pp. 1–3, 2011. View at Google Scholar
  28. A. Riffel and A. Brandelli, “Keratinolytic bacteria isolated from feather waste,” Brazilian Journal of Microbiology, vol. 37, no. 3, pp. 395–399, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. T. Korniłłowicz-Kowalska and J. Bohacz, “Biodegradation of keratin waste: theory and practical aspects,” Waste Management, vol. 31, no. 8, pp. 1689–1701, 2011. View at Publisher · View at Google Scholar · View at Scopus
  30. P. Jeevana Lakshmi, C. M. Kumari Chitturi, and V. V. Lakshmi, “Efficient degradation of feather by keratinase producing Bacillus sp.,” International Journal of Microbiology, vol. 2013, Article ID 608321, 7 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  31. J. Kunert, “Physiology of keratinophilic fungi,” in Revista Iberoamericana de Micología, R. K. S. Kushawaha and and J. Guarro, Eds., pp. 77–85, Bilbao, Spain, 2000. View at Google Scholar
  32. N. Jain and M. Sharma, “Biodiversity of keratinophilic fungal flora in university campus, Jaipur, India,” Iranian Journal of Public Health, vol. 41, no. 11, pp. 27–33, 2012. View at Google Scholar · View at Scopus
  33. A. B. Friedricht and G. Antranikian, “Keratin degradation by Feividobacterium pennavomns, a novel thermophilic anaerobic species of the order thermotogales,” Applied and Environmental Microbiology, vol. 62, no. 8, pp. 2875–2882, 1996. View at Google Scholar · View at Scopus
  34. S. Riessen and G. Antranikian, “Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity,” Extremophiles, vol. 5, no. 6, pp. 399–408, 2001. View at Publisher · View at Google Scholar · View at Scopus
  35. G.-W. Nam, D.-W. Lee, H.-S. Lee et al., “Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe,” Archives of Microbiology, vol. 178, no. 6, pp. 538–547, 2002. View at Publisher · View at Google Scholar · View at Scopus
  36. I. N. S. Dozie, C. N. Okeke, and N. C. Unaeze, “A thermostable, alkaline-active, keratinolytic proteinase from Chrysosporium keratinophilum,” World Journal of Microbiology and Biotechnology, vol. 10, no. 5, pp. 563–567, 1994. View at Publisher · View at Google Scholar · View at Scopus
  37. A. Brandelli, D. J. Daroit, and A. Riffel, “Biochemical features of microbial keratinases and their production and applications,” Applied Microbiology and Biotechnology, vol. 85, no. 6, pp. 1735–1750, 2010. View at Publisher · View at Google Scholar · View at Scopus
  38. P. Anbu, S. C. B. Gopinath, A. Hilda, N. Mathivanan, and G. Annadurai, “Secretion of keratinolytic enzymes and keratinolysis by Scopulariopsis brevicaulis and Trichophyton mentagrophytes: regression analysis,” Canadian Journal of Microbiology, vol. 52, no. 11, pp. 1060–1069, 2006. View at Publisher · View at Google Scholar · View at Scopus
  39. W. Laba and A. Rodziewicz, “Keratinolytic potential of feather-degrading Bacillus polymyxa and Bacillus cereus,” Polish Journal of Environmental Studies, vol. 19, no. 2, pp. 371–378, 2010. View at Google Scholar · View at Scopus
  40. T. Sivakumar, T. Shankar, V. Thangapand, and V. Ramasubram, “Optimization of cultural condition for keratinase production using Bacillus cereus TS1,” Insight Microbiology, vol. 3, no. 1, pp. 1–8, 2013. View at Publisher · View at Google Scholar
  41. E. Tiwary and R. Gupta, “Rapid conversion of chicken feather to feather meal using dimeric keratinase from Bacillus licheniformis ER-15,” Journal of Bioprocessing & Biotechniques, vol. 2, no. 4, Article ID 1000123, 2012. View at Google Scholar
  42. G. S. Molyneux, “The digestion of wool by a keratinolytic Bacillus,” Australian Journal of Biological Sciences, vol. 12, no. 3, pp. 274–281, 1959. View at Google Scholar
  43. J.-S. Kim, L. D. Kluskens, W. M. de Vos, R. Huber, and J. Van Der Oost, “Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin,” Journal of Molecular Biology, vol. 335, no. 3, pp. 787–797, 2004. View at Publisher · View at Google Scholar · View at Scopus
  44. W. Suntornsuk, J. Tongjun, P. Onnim et al., “Purification and characterisation of keratinase from a thermotolerant feather-degrading bacterium,” World Journal of Microbiology and Biotechnology, vol. 21, no. 6-7, pp. 1111–1117, 2005. View at Publisher · View at Google Scholar · View at Scopus
  45. B. Zhang, Z. W. Sun, D. D. Jiang, and T. G. Niu, “Isolation and purification of alkaline keratinase from Bacillus sp. 50-3,” African Journal of Biotechnology, vol. 8, no. 11, pp. 2598–2603, 2009. View at Google Scholar · View at Scopus
  46. V. Saibabu, F. N. Niyonzima, and S. S. More, “Isolation, partial purification and characterization of keratinase from Bacillus magaterium,” International Research Journal of Biological Sciences, vol. 22, no. 2, pp. 13–20, 2013. View at Google Scholar
  47. A. M. Farag and M. A. Hassan, “Purification, characterization and immobilization of a keratinase from Aspergillus oryzae,” Enzyme and Microbial Technology, vol. 34, no. 2, pp. 85–93, 2004. View at Publisher · View at Google Scholar · View at Scopus
  48. H. Gradišar, J. Friedrich, I. Križaj, and R. Jerala, “Similarities and specificities of fungal keratinolytic proteases: comparison of keratinases of Paecilomyces marquandii and Doratomyces microsporus to some known proteases,” Applied and Environmental Microbiology, vol. 71, no. 7, pp. 3420–3426, 2005. View at Publisher · View at Google Scholar · View at Scopus
  49. K. C. Raju, U. Neogi, R. Saumya, and N. R. Goud, “Studies on extra cellular enzyme keratinase from dermatophyte Microsporum gypseum,” International Journal of Biological Chemistry, vol. 1, no. 3, pp. 174–178, 2007. View at Publisher · View at Google Scholar
  50. F. G. Moreira-Gasparin, C. G. M. de Souza, A. M. Costa et al., “Purification and characterization of an efficient poultry feather degrading-protease from Myrothecium verrucaria,” Biodegradation, vol. 20, no. 5, pp. 727–736, 2009. View at Publisher · View at Google Scholar · View at Scopus
  51. L. Cao, H. Tan, Y. Liu, X. Xue, and S. Zhou, “Characterization of a new keratinolytic Trichoderma atroviride strain F6 that completely degrades native chicken feather,” Letters in Applied Microbiology, vol. 46, no. 3, pp. 389–394, 2008. View at Publisher · View at Google Scholar · View at Scopus
  52. E. Ionata, F. Canganella, G. Bianconi et al., “A novel keratinase from Clostridium sporogenes bv. pennavorans bv. nov., a thermotolerant organism isolated from solfataric muds,” Microbiological Research, vol. 163, no. 1, pp. 105–112, 2008. View at Publisher · View at Google Scholar · View at Scopus
  53. R. C. S. Thys, F. S. Lucas, A. Riffel, P. Heeb, and A. Brandelli, “Characterization of a protease of a feather-degrading Microbacterium species,” Letters in Applied Microbiology, vol. 39, no. 2, pp. 181–186, 2004. View at Publisher · View at Google Scholar · View at Scopus
  54. C. M. Longshaw, J. D. Wright, A. M. Farrell, and K. T. Holland, “Kytococcus sedentarius, the organism associated with pitted keratolysis, produces two keratin-degrading enzymes,” Journal of Applied Microbiology, vol. 93, no. 5, pp. 810–816, 2002. View at Publisher · View at Google Scholar · View at Scopus
  55. Z.-J. Cao, Q. Zhang, D.-K. Wei et al., “Characterization of a novel Stenotrophomonas isolate with high keratinase activity and purification of the enzyme,” Journal of Industrial Microbiology and Biotechnology, vol. 36, no. 2, pp. 181–188, 2009. View at Publisher · View at Google Scholar · View at Scopus
  56. L. Vidal, P. Christen, and M. N. Coello, “Feather degradation by Kocuria rosea in submerged culture,” World Journal of Microbiology and Biotechnology, vol. 16, no. 6, pp. 551–554, 2000. View at Publisher · View at Google Scholar · View at Scopus
  57. C. H. de Toni, M. F. Richter, J. R. Chagas, J. A. P. Henriques, and C. Termignoni, “Purification and characterization of an alkaline serine endopeptidase from a feather-degrading Xanthomonas maltophilia strain,” Canadian Journal of Microbiology, vol. 48, no. 4, pp. 342–348, 2002. View at Publisher · View at Google Scholar · View at Scopus
  58. R. R. Chitte, V. K. Nalawade, and S. Dey, “Keratinolytic activity from the broth of a feather-degrading thermophilic Streptomyces thermoviolaceus strain SD8,” Letters in Applied Microbiology, vol. 28, no. 2, pp. 131–136, 1999. View at Publisher · View at Google Scholar · View at Scopus
  59. X.-Q. Han and S. Damodaran, “Purification and characterization of Protease Q: a detergent- and urea-stable serine endopeptidase from bacillus pumilus,” Journal of Agricultural and Food Chemistry, vol. 46, no. 9, pp. 3596–3603, 1998. View at Publisher · View at Google Scholar · View at Scopus
  60. I. Hanukoglu and E. Fuchs, “The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins,” Cell, vol. 31, no. 1, pp. 243–252, 1982. View at Publisher · View at Google Scholar · View at Scopus
  61. I. Hanukoglu and E. Fuchs, “The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins,” Cell, vol. 33, no. 3, pp. 915–924, 1983. View at Publisher · View at Google Scholar · View at Scopus
  62. X. Lin, D. W. Kelemen, E. S. Miller, and J. C. H. Shih, “Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1,” Applied and Environmental Microbiology, vol. 61, no. 4, pp. 1469–1474, 1995. View at Google Scholar · View at Scopus
  63. L. D. Johnson, W. W. Idler, X.-M. Zhou, D. R. Roop, and P. M. Steinert, “Structure of a gene for the human epidermal 67-kDa keratin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 82, no. 7, pp. 1896–1900, 1985. View at Publisher · View at Google Scholar · View at Scopus
  64. S. C. B. Gopinath, P. Anbu, T. Lakshmipriya, and A. Hilda, “Strategies to characterize fungal lipases for applications in medicine and dairy industry,” BioMed Research International, vol. 2013, Article ID 154549, 10 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  65. S. M. Harde, I. B. Bajaj, and R. S. Singhal, “Optimization of fermentative production of keratinase from Bacillus subtilis NCIM 2724,” Agriculture, Food and Analytical Bacteriology, vol. 1, no. 1, pp. 54–65, 2011. View at Google Scholar
  66. T. Shankar, P. Thangamathi, C. Sathiya, and T. Sivakumar, “Statistical optimization of keratinase production by Bacillus thuringiensis,” Journal of Global Biosciences, vol. 3, no. 2, pp. 477–483, 2014. View at Google Scholar
  67. P. Ramnani and R. Gupta, “Optimization of medium composition for keratinase production on feather by Bacillus licheniformis RGI using statistical methods involving response surface methodology,” Biotechnology and Applied Biochemistry, vol. 40, no. 2, pp. 191–196, 2004. View at Publisher · View at Google Scholar · View at Scopus
  68. T. Sivakumar, T. Shankar, P. Vijayabaskar, and V. Ramasubramanian, “Statistical optimization of keratinase production by Bacillus cereus,” Global Journal of Biotechnology and Biochemistry, vol. 6, no. 4, pp. 197–202, 2011. View at Google Scholar
  69. P. Anbu, S. C. B. Gopinath, A. Hilda, T. Lakshmipriya, and G. Annadurai, “Optimization of extracellular keratinase production by poultry farm isolate Scopulariopsis brevicaulis,” Bioresource Technology, vol. 98, no. 6, pp. 1298–1303, 2007. View at Publisher · View at Google Scholar · View at Scopus
  70. S. C. B. Gopinath, K. Awazu, J. Tominaga, and P. K. R. Kumar, “Monitoring biomolecular interactions on a digital versatile disk: a BioDVD platform technology,” ACS Nano, vol. 2, no. 9, pp. 1885–1895, 2008. View at Publisher · View at Google Scholar · View at Scopus
  71. S. C. B. Gopinath, R. Kumaresan, K. Awazu et al., “Evaluation of nucleic acid duplex formation on gold over layers in biosensor fabricated using Czochralski-grown single-crystal silicon substrate,” Analytical and Bioanalytical Chemistry, vol. 398, no. 2, pp. 751–758, 2010. View at Publisher · View at Google Scholar · View at Scopus
  72. S. C. B. Gopinath, K. Awazu, and M. Fujimaki, “Waveguide-mode sensors as aptasensors,” Sensors, vol. 12, no. 2, pp. 2136–2151, 2012. View at Publisher · View at Google Scholar · View at Scopus
  73. S. C. B. Gopinath, K. Awazu, M. Fujimaki, K. Shimizu, and T. Shima, “Observations of immuno-gold conjugates on influenza viruses using waveguide-mode sensors,” PLoS ONE, vol. 8, no. 7, Article ID e69121, 2013. View at Publisher · View at Google Scholar · View at Scopus
  74. T. S. Dhahi, U. Hashim, N. M. Ahmed, and H. Nazma, “Fabrication and characterization of gold nano-gaps for ssDNA immobilization and hybridization detection,” Journal of New Materials for Electrochemical Systems, vol. 14, no. 3, pp. 191–196, 2011. View at Google Scholar · View at Scopus
  75. M. E. Ali, U. Hashim, S. Mustafa et al., “Nanoparticle sensor for label free detection of swine DNA in mixed biological samples,” Nanotechnology, vol. 22, no. 19, Article ID 195503, 2011. View at Publisher · View at Google Scholar · View at Scopus
  76. M. E. Ali, U. Hashim, S. Mustafa, Y. B. Che Man, and K. N. Islam, “Gold nanoparticle sensor for the visual detection of pork adulteration in meatball formulation,” Journal of Nanomaterials, vol. 2012, Article ID 103607, 7 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  77. T. Lakshmipriya, M. Fujimaki, S. C. B. Gopinath, K. Awazu, Y. Horiguchi, and Y. Nagasaki, “A high-performance waveguide-mode biosensor for detection of factor IX using PEG-based blocking agents to suppress non-specific binding and improve sensitivity,” Analyst, vol. 138, no. 10, pp. 2863–2870, 2013. View at Publisher · View at Google Scholar · View at Scopus
  78. D. J. Daroit and A. Brandelli, “A current assessment on the production of bacterial keratinases,” Critical Reviews in Biotechnology, vol. 34, no. 4, pp. 372–384, 2014. View at Publisher · View at Google Scholar
  79. S. Gupta and R. Singh, “Hydrolyzing proficiency of keratinases in feather degradation,” Indian Journal of Microbiology, vol. 54, no. 4, pp. 466–470, 2014. View at Publisher · View at Google Scholar