Volume 10, Issue 4 (2019)
JMBS 2019, 10(4): 527-534 |
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Mehrban S, Bahreini M, Asoodeh A, Korozhdehi B. Identification of native isolation, FUM1, isolated from poultry farm of Mashhad countryside and improving its keratinolytic activity by optimizing of environmental conditions using one factor at a time methodology. JMBS 2019; 10 (4) :527-534
URL: http://biot.modares.ac.ir/article-22-16166-en.html
URL: http://biot.modares.ac.ir/article-22-16166-en.html
1- Department of Biology, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran
2- Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran
3- Agricultural Biotechnology Department, Agriculture Faculty, Agriculture & Natural Resources College, University of Tehran, Karaj, Iran
2- Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran
3- Agricultural Biotechnology Department, Agriculture Faculty, Agriculture & Natural Resources College, University of Tehran, Karaj, Iran
Abstract: (7068 Views)
Aims: Significant amounts of waste, including feathers, bones, blood, etc. are yearly produced by the poultry industry. Feathers are composed of 90% keratin protein, and the rest is composed of lipids and water. Keratinases are one of the most diverse and usable enzymes, which can be produced by bacterial and fungal microorganisms. These enzymes show a wide range of application in various fields.
Materials and Methods: In this study, the keratinolytic activity of the isolated strain from a poultry farm in Mashhad was evaluated and then the medium conditions for keratinase production were optimized. The strains were identified based on the morphological and biochemical methods. 16SrRNA gene of the strain was amplified by PCR and then sequenced. The strain proteolytic activity was examined and compared with its keratinolytic activity. Finally, strain growth ability tested in variety substrate.
Findings: Using 16SrRNA gene sequencing, morphological and biochemical identification, the strain shared 99.9% similarity with Bacillus mojavensis. Optimization of various factors, including temperature, pH, incubation time, carbon and nitrogen sources, aeration and inoculum size showed that the isolated strain has the highest keratinolytic activity at 37°C, 48 hour incubation period, pH=9.5, sucrose 1%, 3% substrate, aeration 75% and 6% (v/v) inoculum amount. None of the nitrogen sources had a positive effect.
Conclusion: The FUM-1 keratinolytic activity was increased approximately 3.38 fold by condition optimization of the medium, indicating the importance of environmental conditions. In the study, the strain with high keratinolytic activity was suggesting its potential use in biotechnological.
Materials and Methods: In this study, the keratinolytic activity of the isolated strain from a poultry farm in Mashhad was evaluated and then the medium conditions for keratinase production were optimized. The strains were identified based on the morphological and biochemical methods. 16SrRNA gene of the strain was amplified by PCR and then sequenced. The strain proteolytic activity was examined and compared with its keratinolytic activity. Finally, strain growth ability tested in variety substrate.
Findings: Using 16SrRNA gene sequencing, morphological and biochemical identification, the strain shared 99.9% similarity with Bacillus mojavensis. Optimization of various factors, including temperature, pH, incubation time, carbon and nitrogen sources, aeration and inoculum size showed that the isolated strain has the highest keratinolytic activity at 37°C, 48 hour incubation period, pH=9.5, sucrose 1%, 3% substrate, aeration 75% and 6% (v/v) inoculum amount. None of the nitrogen sources had a positive effect.
Conclusion: The FUM-1 keratinolytic activity was increased approximately 3.38 fold by condition optimization of the medium, indicating the importance of environmental conditions. In the study, the strain with high keratinolytic activity was suggesting its potential use in biotechnological.
Article Type: Research Paper |
Subject:
Agricultural Biotechnology
Received: 2017/11/20 | Accepted: 2019/05/15 | Published: 2019/12/21
Received: 2017/11/20 | Accepted: 2019/05/15 | Published: 2019/12/21
References
1. Agrawal BH, Dalal MI. Screening and characterization of keratinase enzyme obtained from keratin degrading microorganism isolated from Sanjan poultry waste dumping soil. Eur Acad Res. 2015;2(11):13986-94. [Link]
2. Gupta R, Rajput R, Sharma R, Gupta N. Biotechnological applications and prospective market of microbial keratinases. Appl Microbiol Biotechnol. 2013;97(23):9931-40. [Link] [DOI:10.1007/s00253-013-5292-0]
3. Brandelli A, Sala L, Kalil SJ. Microbial enzymes for bioconversion of poultry waste into added-value products. Food Res Int. 2015;73:3-12. [Link] [DOI:10.1016/j.foodres.2015.01.015]
4. Agrahari S. Production of enzymes and degradation of feathers by soil microbes [Internet]. Noida: Jaypee Institute of Information Technology; 2011 [cited 2016 Feb 20]. Available from: http://citeseerx.ist.psu.edu/viewdoc/download?doi=10.1.1.723.65&rep=rep1&type=pdf. [Link]
5. Florin NH, Maddocks AR, Wood S, Harris AT. High-temperature thermal destruction of poultry derived wastes for energy recovery in Australia. Waste Manag. 2009;29(4):1399-408. [Link] [DOI:10.1016/j.wasman.2008.10.002]
6. Font-Palma C. Characterisation, kinetics and modelling of gasification of poultry manure and litter: An overview. Energy Convers Manag. 2012;53(1):92-8. [Link] [DOI:10.1016/j.enconman.2011.08.017]
7. Allure N, Madhusudhan DN, Agsar D. Detection of keratinolytic Actinobacteria and evaluation of bioprocess for production of alkaline keratinase. Int J Curr Microbiol Appl Sci. 2015;4(7):907-18. [Link]
8. Wawrzkiewicz K, Łobarzewski J, Wolski T. Intracellular keratinase of Trichophyton gallinae. J Med Vet Mycol. 1987;25(4):261-8. [Link] [DOI:10.1080/02681218780000601]
9. Purchase D. Microbial keratinases: Characteristics, biotechnological applications and potential. In: Gupta VK, Sharma GD, Tuohy MG, Gaur R, editors. The handbook of microbial bioresources. Wallingford: CAB International Publishing; 2016. pp. 634-74. [Link] [DOI:10.1079/9781780645216.0634]
10. Laurila K. Optimization of growth conditions for a recombinant keratinase producing bacterial strain [Dissertation]. Borås: University of Borås; 2013. [Link]
11. Jalendran E, Dadvar Baygi SJ. Chromosomal integration of KerA gene in Bacillus megaterium for stable keratinase production [Dissertation]. Borås: University of Borås; 2011. [Link]
12. Daroit DJ, Brandelli A. A current assessment on the production of bacterial keratinases. Crit Rev Biotechnol. 2014;34(4):372-84. [Link] [DOI:10.3109/07388551.2013.794768]
13. Matikevičienė V, Grigiškis S, Levišauskas D, Sirvydytė K, Dižavičienė O, Masiliūnienė D, et al. Optimization of keratinase production by Actinomyces fradiae 119 and its application in degradation of keratin containing wastes. Environment. Technology. Resources. Proceedings of the International Scientific and Practical Conference, 2015, Ural State. Yekaterinburg: Ural State Agrarian University; 2016. pp. 294-300. [Link] [DOI:10.17770/etr2011vol1.905]
14. E Silva LA, Macedo AJ, Termignoni C. Production of keratinase by Bacillus subtilis S14. Ann Microbiol. 2014;64(4):1725-33. [Link] [DOI:10.1007/s13213-014-0816-0]
15. Queipo-Ortuño MI, De Dios Colmenero J, Macias M, Bravo MJ, Morata P. Preparation of bacterial DNA template by boiling and effect of immunoglobulin G as an inhibitor in real-time PCR for serum samples from patients with brucellosis. Clin Vaccine Immunol. 2008;15(2):293-6. [Link] [DOI:10.1128/CVI.00270-07]
16. Govarthanan M, Selvankumar T, Arunprakash S. Production of keratinolytic enzyme by a newly isolated feather degrading Bacillus sp. from chick feather waste. Int J Pharma Bio Sci. 2011;2(3):259-65. [Link]
17. Ramnani P, Gupta R. Optimization of medium composition for keratinase production on feather by Bacillus licheniformis RG1 using statistical methods involving response surface methodology. Biotechnol Appl Biochem. 2004;40(2):191-6. [Link] [DOI:10.1042/BA20030228]
18. Yang JK, Shih IL, Tzeng YM, Wang SL. Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes. Enzyme Microb Technol. 2000;26(5-6):406-13. [Link] [DOI:10.1016/S0141-0229(99)00164-7]
19. Badoei-dalfard A, Amiri P, Ramezanipour N, Karami Z, Ghanbari B. The production of alkaline protease by Bacillus tequilensis FJSH2 isolated from Jiroft's slaughterhouse wastes. J Microb World. 2015;8(1):54-63. [Persian] [Link]
20. Belarmino DD, Ladchumananandasivam R, Belarmino LD, Pimentel JR, Da Rocha BG, Galvão AO, et al. Physical and morphological structure of chicken feathers (keratin biofiber) in natural, chemically and thermally modified forms. Mater Sci Appl. 2012;3(12):887-93. [Link] [DOI:10.4236/msa.2012.312129]
21. Roberts MS, Nakamura LK, Cohan FM. Bacillus mojavensis sp. nov., distinguishable from Bacillus subtilis by sexual isolation, divergence in DNA sequence, and differences in fatty acid composition. Int J Syst Evol Microbiol. 1994;44(2):256-64. [Link] [DOI:10.1099/00207713-44-2-256]
22. Matikevičienė V, Masiliūnienė D, Grigiškis S. Degradation of keratin containing wastes by bacteria with keratinolytic activity. Environment. Technology. Resources. Proceedings of the 7th International Scientific and Practical Conference, 2015, Rēzekne, Latvia. Yekaterinburg: Ural State Agrarian University; 2015. pp. 284-9. [Link] [DOI:10.17770/etr2009vol1.1107]
23. Sivakumar T, Shankar T, Thangapand V, Ramasubram V. Optimization of cultural condition for keratinase production using Bacillus cereus TS1. Insight Microbiol. 2013;3(1):1-8. [Link] [DOI:10.5567/IMICRO-IK.2013.1.8]
24. Kazzaz AE, Hosseinpour Feizi Z, Guvenmez HK. Keratinolytic protease production and characterization from Bacillus sp. isolated from poultry wastes. Int J Appl Biol Pharm Technol. 2015;6(4):63-73. [Link]
25. Ni H, Chen QH, Chen F, Fu ML, Dong YC, Cai HN. Improved keratinase production for feather degradation by Bacillus licheniformis ZJUEL31410 in submerged cultivation. Afr J Biotechnol. 2011;10(37):7236-44. [Link]
26. Li Y, Fan Sh, Chen Sh, Er H, Du J, Lu F. Study on the fermentation conditions and the application in feather degradation of keratinase produced by Bacillus licheniformis. Proceedings of the International Conference on Applied Biotechnology (ICAB 2012), October 18-19, 2012, Tianjin, China. Heidelberg: Springer; 2014. pp. 89-98. [Link] [DOI:10.1007/978-3-642-37916-1_10]
27. Prakash P, Jayalakshmi SK, Sreeramulu K. Production of keratinase by free and immobilized cells of Bacillus halodurans strain PPKS-2: Partial characterization and its application in feather degradation and dehairing of the goat skin. Appl Biochem Biotechnol. 2010;160(7):1909-20. [Link] [DOI:10.1007/s12010-009-8702-0]
28. Brandelli A. Hydrolysis of native proteins by a keratinolytic protease of Chryseobacterium sp. Ann Microbiol. 2005;55(1):47-50. [Link]
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