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http://dx.doi.org/10.5322/JESI.2014.23.6.1095

Characteristics of Bacteria-Originated Keratinase for Feather Waste Treatment  

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)
Publication Information
Journal of Environmental Science International / v.23, no.6, 2014 , pp. 1095-1100 More about this Journal
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
Feather; Keratin; Keratinase; Xanthomonas sp.;
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1 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.   DOI   ScienceOn
2 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.   DOI   ScienceOn
3 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.   DOI   ScienceOn
4 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.
5 Kornillowicz-Kowalska, T., Bohacz, J., 2011, Biodegradation of keratin waste: theory and practical aspects, Waste Manage., 31, 1689-1701.   DOI   ScienceOn
6 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.   DOI   ScienceOn
7 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.   DOI
8 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.   DOI   ScienceOn
9 Brandelli, A., Daroit, D. J., Riffel, A., 2010, Biochemical features of microbial keratinases and their production and applications, Appl. Microbiol. Biotechnol., 85, 1735-1750.   DOI   ScienceOn
10 Brandelli, A., 2008, Bacterial keratinase: useul enzyme for bioprocessing agroindustrial wastes and beyond, Food Bioprocess Technol., 1, 105-106.   DOI   ScienceOn
11 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.   DOI
12 Wawrzkiewicz, K., Lobarzewski, J., Wolski, T., 1987, Intracellular keratinase of Trichophyton gallinae, J. Med. Vet. Mycol., 25, 261-268.   DOI
13 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.   DOI   ScienceOn
14 Sangali, S., Brandelli, A., 2000, Feather keratin hydrolysis by a Vibrio sp. strain kr2, J. Appl. Microbiol., 89, 735-743.   DOI   ScienceOn
15 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.   DOI
16 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.   DOI   ScienceOn
17 Bertsch, A., Coello, N., 2005, A biotechnological process for treatment and recycling poultry feathers as a feed ingredient, Bioresour. Technol., 96, 1703-1708.   DOI   ScienceOn
18 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.
19 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.   DOI   ScienceOn
20 Gupta, R., Ramnani, P., 2006, Microbial kerationases and their prospective applications: an overview, Appl. Microbiol. Biotechnol., 70, 21-33.   DOI   ScienceOn
21 Bockle, B., Galunsky, B., Muller, R., 1995, Characterization of keratinolytic serine protease from Streptomyces pactum DSM40530, Appl. Environ. Microbiol., 61, 3705-3710.