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Characteristics of Bacteria-Originated Keratinase for Feather Waste Treatment

가금폐기물 처리를 위한 세균유래 케라틴 분해효소의 특성

  • Go, Tae-Hun (College of Natural Resources & Life Science, Life and Industry Convergence Institute, Pusan National University) ;
  • Lee, Sang-Mee (College of Natural Resources & Life Science, Life and Industry Convergence Institute, Pusan National University) ;
  • Cho, Kwang-Sik (College of Natural Resources & Life Science, Life and Industry Convergence Institute, Pusan National University) ;
  • Lee, Ye-Ram (College of Natural Resources & Life Science, Life and Industry Convergence Institute, Pusan National University) ;
  • Park, Soo-Yun (College of Natural Resources & Life Science, Life and Industry Convergence Institute, Pusan National University) ;
  • Jang, Eun-Young (College of Natural Resources & Life Science, Life and Industry Convergence Institute, Pusan National University) ;
  • Jeong, Seong-Yun (Department of Medical Life Science, Catholic University of Daegu) ;
  • Son, Hong-Joo (College of Natural Resources & Life Science, Life and Industry Convergence Institute, Pusan National University)
  • 고태훈 (부산대학교 생명자원과학대학 및 생명산업융합연구원) ;
  • 이상미 (부산대학교 생명자원과학대학 및 생명산업융합연구원) ;
  • 조광식 (부산대학교 생명자원과학대학 및 생명산업융합연구원) ;
  • 이예람 (부산대학교 생명자원과학대학 및 생명산업융합연구원) ;
  • 박수연 (부산대학교 생명자원과학대학 및 생명산업융합연구원) ;
  • 장은영 (부산대학교 생명자원과학대학 및 생명산업융합연구원) ;
  • 정성윤 (대구가톨릭대 의생명과학과) ;
  • 손홍주 (부산대학교 생명자원과학대학 및 생명산업융합연구원)
  • Received : 2014.02.28
  • Accepted : 2014.05.21
  • Published : 2014.06.30

Abstract

Keratin wastes are generated in excess of million tons per year worldwide and biodegradation of keratin by microorganisms possessing keratinase activity can be used as an alternative tool to prevent environmental pollution. For practical use of keratinase, its physicochemical properties should be investigated in detail. In this study, we investigated characteristics of keratinase produced by Xanthomonas sp. P5 which is isolated from rhizospheric soil of soybean. The level of keratinase produced by the strain P5 increased with time and reached its maximum (10.6 U/ml) at 3 days. The production of soluble protein had the same tendency as the production of keratinase. Optimal temperature and pH of keratinase were $40^{\circ}C-45^{\circ}C$ and pH 9, respectively. The enzyme showed broad temperature and pH stabilities. Thermostability profile showed that the enzyme retained 94.6%-100% of the original activity after 1 h treatment at $10^{\circ}C-40^{\circ}C$. After treatment for 1 h at pH 6-10, 89.2%-100% of the activity was remained. At pH 11, 71.6% of the original activity was retained after 1 h treatment. Although the strain P5 did not degrade human hair, it degraded duck feather and chicken feather. These results indicate that keratinase from Xanthomonas sp. P5 could be not only used to upgrade the nutritional value of feather hydrolysate but also useful in situ biodegradation of feather.

Keywords

References

  1. Balaji, S., Kumar, M. S., Karthikeyan, R., 2008, Purification and characterization of an extracellular keratinase from a hornmeal-degrading Bacillussubtilis MTCC (9102), World J. Microbiol. Biotechnol., 24, 2741-2745. https://doi.org/10.1007/s11274-008-9782-7
  2. Bertsch, A., Coello, N., 2005, A biotechnological process for treatment and recycling poultry feathers as a feed ingredient, Bioresour. Technol., 96, 1703-1708. https://doi.org/10.1016/j.biortech.2004.12.026
  3. Bockle, B., Galunsky, B., Muller, R., 1995, Characterization of keratinolytic serine protease from Streptomyces pactum DSM40530, Appl. Environ. Microbiol., 61, 3705-3710.
  4. Bradford, M. M., 1976, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72, 248-254. https://doi.org/10.1016/0003-2697(76)90527-3
  5. Brandelli, A., Daroit, D. J., Riffel, A., 2010, Biochemical features of microbial keratinases and their production and applications, Appl. Microbiol. Biotechnol., 85, 1735-1750. https://doi.org/10.1007/s00253-009-2398-5
  6. Brandelli, A., 2008, Bacterial keratinase: useul enzyme for bioprocessing agroindustrial wastes and beyond, Food Bioprocess Technol., 1, 105-106. https://doi.org/10.1007/s11947-007-0025-y
  7. da Rosa Gioppo, N. M., Moreira-Gasparin, F. G., Costa, A. M., Alexandrino, A. M., de Souza, C. G. M, Peralta, R. M., 2009, Influence of the carbon and nitrogen sources on keratinase production by Myrothecium verrucaria in submerged and solid state cultures, J. Ind. Microbiol. Biotechnol., 36, 705-711. https://doi.org/10.1007/s10295-009-0540-0
  8. Fakhfakh, N., Kanoun, S., Manni, L., Nasri, M., 2009, Production and biochemical and molecular characterization of a keratinolytic serine protease from chicken feather-degrading Bacillus licheniformis RPk, Can. J. Microbiol., 55, 427-436. https://doi.org/10.1139/W08-143
  9. Gupta, R., Ramnani, P., 2006, Microbial kerationases and their prospective applications: an overview, Appl. Microbiol. Biotechnol., 70, 21-33. https://doi.org/10.1007/s00253-005-0239-8
  10. Han, X. Q., Damodaran, S., 1998, Purification and characterization of protease Q: a detergent- and urea-stable serine endopeptidase from Bacillus pumilus, J. Agric. Food Chem., 46, 3596-3603. https://doi.org/10.1021/jf980361m
  11. Jeong, J. H., Park, K. H., Oh, D. J., Hwang, D. Y., Kim, H. S., Lee, C. Y., Son, H. H., 2010, Keratinolytic enzyme-mediated biodegradation of recalcitrant feather by a newly isolated Xanthomonas sp. P5, Polym. Degra, Stab., 95, 1969-1977. https://doi.org/10.1016/j.polymdegradstab.2010.07.020
  12. Korkmaz, H., Unaldi, M. N., Aslan, B., Coral, G., Arikan, B., Colak, O., 2003, Keratinolytic activity of Streptomyces strain BA7, a new isolate from Turkey, Annal. Microbiol., 53, 85-93.
  13. Kornillowicz-Kowalska, T., Bohacz, J., 2011, Biodegradation of keratin waste: theory and practical aspects, Waste Manage., 31, 1689-1701. https://doi.org/10.1016/j.wasman.2011.03.024
  14. Langeveld, J. P. M., Wang, J. J., Van de Wiel, D. F. M., Shih, G. C. , Garssen, G. J., Bossers, A., Shih, J. C. H., 2003, Enzymatic degradation of prion protein in brain stem from infected cattle and sheep, J. Infect. Dis., 188, 1782-1789. https://doi.org/10.1086/379664
  15. Lin, X., Lee, C. G., Casale, E. S., Shih, J. C. H., 1992. Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain, Appl. Environ. Microbiol., 58, 3271-3275.
  16. Mocedo, A. J., Da Silva, B. W. O., Termignoni, C., 2008, Properties of a non collagen-degrading Bacillus subtilis keratinase, Can. J. Microbiol., 54, 180-188. https://doi.org/10.1139/W07-124
  17. Onifade, A. A., Al-Sane, N. A., Al-Musallam, A. A., Al-Zarban, S., 1998, Potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources, Bioresour. Technol., 66, 1-11. https://doi.org/10.1016/S0960-8524(98)00033-9
  18. Papadoulos, M. C., Ketelaars, E. H., 1986, Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal, Anim. Feed Sci. Technol., 14, 279-290. https://doi.org/10.1016/0377-8401(86)90100-8
  19. Sangali, S., Brandelli, A., 2000, Feather keratin hydrolysis by a Vibrio sp. strain kr2, J. Appl. Microbiol., 89, 735-743. https://doi.org/10.1046/j.1365-2672.2000.01173.x
  20. Tatineni, R., Doddapaneni, K. K., Potumarthi, R. C., Vellanki, R. N., Kandathil, M. T., Kolli, N., Mangamoori, L. N., 2008, Purification and characterization of an alkaline keratinase from Streptomyces sp., Bioresour. Technol., 99, 1596-1602. https://doi.org/10.1016/j.biortech.2007.04.019
  21. Wawrzkiewicz, K., Lobarzewski, J., Wolski, T., 1987, Intracellular keratinase of Trichophyton gallinae, J. Med. Vet. Mycol., 25, 261-268. https://doi.org/10.1080/02681218780000601