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Optimization of Keratinase Production By Actinomyces Fradiae 119 and Its Application in Degradation of Keratin Containing Wastes

V. Matikevičienė, S. Grigiškis, D. Levišauskas, K. Sirvydytė, O. Dižavičienė, D. Masiliūnienė, O. Ančenko

Abstract


The aim of this study was to identify and optimize significant technological parameters influencing keratinolytic enzyme production by A. fradiae 119 and to study its ability to degrade keratin. In the present work chicken feathers meal (CFM) was found to be an excellent substrate for keratinase induction by A. fradiae 119. The strain produced 164 KU/mL keratinolytic activity in basal medium containing 7.5 g/L CFM as the sole source of carbon and nitrogen. Increased keratinolytic activity was achieved in media with ammonium sulfate as nitrogen source, the application of additional nitrogen sources to media containing CFM slightly decreased keratinase synthesis. Optimal parameters of the cultivation process were determined: pH of cultivation medium – 7.2, temperature – 34 ºC and inoculum’s size – 8 %, using the response surface methodology. The yield of keratinase activity was increased by 46 % (267 KU/mL) after optimization of the cultivation process. The good ability of cultural liquid to degrade feathers and wool was detected.

Keywords


actinomyces fradiae; keratin degradation; keratinase; optimization; response surface; methodology

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References


Radha, S., Gunasekaran, P. Cloning and expression of keratinase gene in Bacillus megaterium and optimization of fermentation conditions for the production of keratinase by recombinant strain. Journal of Applied Microbiology, 103. 2007, p. 1301-1310.

Matikevičienė, V., Masiliūnienė, D., Grigiškis, S. Degradation of keratin containing wastes by bacteria with keratinolytic activity. Proceedings of the 7th international scientific and practical conference “Environment. Technology. Resources”, June 25-27, 2009. Rezekne. 2009, p. 284-289.1 Shih, J. C. H.; Williams, C. M. 1992. Purified Bacillus licheniformis PWD–1 keratinase. United States Patent. Nr. 5171682. 14 p.

Hossain, M.S., Azad, A.K., Abu Sayem, S.M., Mostafa, G., Hoq, M.M. Production and partial characterization of feather-degrading keratinolytic serine protease from Bacillus licheniformis MZK-3. Journal of Biological Sciences, 7-4. 2007, p. 599-606.

Fakhfakh-Zouari, N., Haddar, A., Hmidet, N., Frikha, F., Nasri, M. Application of statistical experimental design for optimization of keratinases production by Bacillus pumilus A1 grown on chicken feather and some biochemical properties. Process Biochemistry, 45. 2010, p. 617-626.

Shih, J. C. H.; Williams, C. M. Purified Bacillus licheniformis PWD–1 keratinase. United States Patent. Nr. 5171682. 1992, p. 14.

Lanoë, J.; Dunnigan, J. Improvements of the Anson assay for measuring proteolytic activities in acidic pH range, Analytical Biochemistry, 89-2. 2004, p. 461-471.

Levišauskas, D., Tekorius, T., Čipinytė, V., Grigiškis, S. Experimental optimization of nutrient media for cultivation of Arthrobacter bacteria. Latvijas Kīmijas Žurnāls, 1. 2004, p. 75-80.

Fakhfakh, N., Kanoun, S., Manni, L., Nasri,M. Production and biochemical and molecular characterization of a keratinolytic serine protease from chicken feather-degrading Bacillus lichiniformis RPk. Canadian Journal of Microbiology, 55. 2009, p. 427-436.

Ignatova, Z., Gousterova, A., Spassov, G., and Nedkov, P. Isolation and partial characterization of extracellular keratinase from a wool degrading thermophilic actinomycete strain Thermoactinomyces candidus. Canadian Journal of Microbiology, 45. 1999, p. 217–222.

Nam, G.W., Lee, D.W., Lee, H.S., Lee, N.J., Kim, B.C., Choe, E.A., Hwang, J.K., Suhartono, M.T., and Pyun, Y.R. Native feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase producing thermophilic anaerobe. Archives of Microbiology, 178. 2002, p. 538–547.




DOI: https://doi.org/10.17770/etr2011vol1.905

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