Enhancement of Amylase and Lipase Production from Bacillus licheniformis 016 Using Waste Chicken Feathers as Peptone Source
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Peptones are accepted as one of the most expensive medium components of microorganisms. The present study was undertaken to investigate the effect of chicken feather peptone (CFP) on enzyme (lipase and amylase) production by Bacillus licheniformis 016. In order to assess its effectiveness on enzyme production, CFP was compared with commercial fish peptone (FP) and protease peptone (PP). The optimum concentration of CFP for lipase and amylase production was determined as 5 and 6 g/L, respectively. The optimum concentration of both FP and PP was found as 4 g/L for lipase production and 5 g/L for amylase production. In all the peptone media, the optimal incubation times for amylase and lipase production were determined as 24 and 48 h, respectively. CFP was found to be more favorable for lipase and amylase production. In CFP, PP and FP media, the maximum lipase activities were 1870, 1582 and 1831 U/L, and the maximum amylase activities were 1680, 1505 and 632 U/L, respectively. On the other hand, better cell growth performance was achieved in CFP media compared to PP and FP media. The least pH change was detected in CFP-containing media. CFP was also found to prevent starch aggregation in the medium in contrast to FP and PP. This study exhibited that CFP was a better nitrogen source or an inducer for lipase and amylase production as well as cell growth in comparison to the tested commercial peptones.
KeywordsWaste chicken feathers Peptone Lipase Amylase Production
The authors alone are responsible for the content and writing of the paper.
This work was supported by a grant from the research funds appropriated to Ataturk University, Erzurum, Turkey (FAD-2018-6352).
Compliance with Ethical Standards
Conflict of interest
The authors report no conflicts of interest.
Research Involving Human and Animal Participants
The manuscript does not contain experiments involving human participants and/or animals.
- 2.Sundarram, A., Murthy, T.P.K.: α-Amylase production and applications: a review. J. Appl. Environ. Microbiol. 2, 166–175 (2014)Google Scholar
- 5.Taskin, M., Ucar, M.H., Unver, Y., Kara, A.A., Ozdemir, M., Ortucu, S.: Lipase production with free and immobilized cells of cold-adapted yeast Rhodotorula glutinis HL25. Biocatal. Agric. Biotechnol. 8, 97–103 (2016)Google Scholar
- 6.Sivaramakrishnan, S., Gangadharan, D., Nampoothiri, K.M., Soccol, C.R., Pandey, A.: a-Amylases from microbial sources—an overview on recent developments. Food Technol. Biotechnol. 44, 173–184 (2006)Google Scholar
- 8.Saranraj, P., Stella, D.: Fungal amylase—a review. Int. J. Microbiol. Res. 4, 203–211 (2013)Google Scholar
- 9.Ait Kaki El-Hadef El-Okki, A., Gagaoua, M., Bennamoun, L., Djekrif, S., Hafid, K., El-Hadef El-Okki, M., Meraihi, Z.: Statistical optimization of thermostable α-amylase production by a newly isolated Rhizopus oryzae strain FSIS4 using decommissioned dates. Waste Biomass Valoriz. 8, 2017–2027 (2017)CrossRefGoogle Scholar
- 13.Silva, M.F., Freire, D.M.G., de Castro, A.M., Di Luccio, M., Mazutti, M.A., Oliveira, J.V.: Production of multifunctional lipases by Penicillium verrucosum and Penicillium brevicompactum under solid state fermentation of babassu cake and castor meal. Bioprocess Biosyst. Eng. 34, 145–152 (2011)CrossRefGoogle Scholar
- 15.Erdal, S., Taskin, M.: Production of alpha-amylase by Penicillium expansum MT-1 in solid-state fermentation using waste Loquat (Eriobotrya japonica Lindley) kernels as substrate. Romanian Biotechnol. Lett. 15, 5342–5350 (2010)Google Scholar
- 21.Juwon, A.D., Emmanuel, O.F.: Experimental investigations on the effects of carbon and nitrogen sources on concomitant amylase and polygalacturonase production by Trichoderma viride BITRS-1001 in submerged fermentation. Biotechnol. Res. Int. (2012). https://doi.org/10.1155/2012/904763 CrossRefGoogle Scholar
- 27.Kshetri, P., Roy, S.S., Sharma, S.K., Singh, T.S., Ansari, M.A., Prakash, N., Ngachan, S.V.: Transforming chicken feather waste into feather protein hydrolysate using a newly isolated multifaceted keratinolytic bacterium Chryseobacterium sediminis RCM-SSR-7. Waste Biomass Valoriz. (2017). https://doi.org/10.1007/s12649-017-0037-4 CrossRefGoogle Scholar
- 39.Lima, V.M., Krieger, N., Sarquis, M.I.M., Mitchell, D.A., Ramos, L.P., Fontana, J.D.: Effect of nitrogen and carbon sources on lipase production by Penicillium aurantiogriseum. Food Technol. Biotechnol. 41, 105–110 (2003)Google Scholar
- 42.Srivastava, R.A.K., Baruah, J.N.: Culture conditions for production of thermostable amylase by Bacillus stearothermophilus. Appl. Environ. Microbiol. 52, 179–184 (1986)Google Scholar
- 43.Shanmughapriya, S., Kiran, G.S., Selvin, J., Gandhimathi, R., Baskar, T.B., Manilal, A.: Optimization, production, and partial characterization of an alkalophilic amylase produced by sponge associated marine bacterium Halobacterium salinarum MMD047. Biotechnol. Bioprocess Eng. 14, 67–75 (2009)CrossRefGoogle Scholar
- 44.Unakal, C., Kallur, R.I., Kaliwal, B.B.: Production of α-amylase using banana waste by Bacillus subtilis under solid state fermentation. Eur. J. Exp. Biol. 2, 1044–1052 (2012)Google Scholar
- 46.Facchini, F.D.A., Vici, A.C., Pereira, M.G., Jorge, J.A., de Moraes, Md.L.T.: Enhanced lipase production of Fusarium verticillioides by using response surface methodology and wastewater pretreatment application. J. Chem. Technol. Biotechnol. 6, 996–1002 (2016)Google Scholar
- 48.Akcan, N.: High level production of extracellular α-amylase from Bacillus licheniformis ATCC 12759 in submerged fermentation. Rom. Biotechnol. Lett. 16, 6833–6840 (2011)Google Scholar