Microwave-Alkali Treatment of Chicken Feathers for Protein Hydrolysate Production
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Conversion of chicken feathers into valuable products like protein and amino acids is very challenging due to the rigid structure of keratins extensively cross-linked by disulphide, hydrogen and hydrophobic bonds. An efficient treatment is necessary for reducing the disulphide bonds and increasing the feathers solubilisation. This study investigated the effects of microwave-alkali treatment on disulphide bond reduction and morphological changes of chicken feathers for protein hydrolysate production.
Feathers were treated at different sodium hydroxide concentrations (0.1, 0.5, 1.0, 1.5, 2.0 M), various microwave power levels (100, 300, 450, 600, 800 W) and residence times (2, 4, 6, 8, 10 min).
The most efficient conditions for microwave-alkali treatment of feathers were (1) 10 min; (2) 0.5 M NaOH and (3) 800 W which produced 24.72 mM thiol and 26.74 mg/mL protein. In comparison to the autoclave-alkali and the conventional heating-alkali method, the microwave-alkali treatment denatured the feather keratins and reduced the disulphide bonds in feathers to a greater extent. Scanning electron microscope and fourier transform infrared analyses showed that the structure of the microwave-alkali treated feathers was highly disrupted and significantly changed from fibers into an amorphous structure. Based on the amino acid profile, the protein hydrolysate from the microwave-alkali treatment contained a significantly higher concentration of amino acids (69.4 mg/g of feathers) compared to the autoclave-alkali (19.0 mg/g of feathers) and the conventional heating-alkali (27.8 mg/g of feathers) treatments.
Microwave-alkali treatment was more efficient than conventional treatments in breaking down the disulphide bonds, disrupting the feather structure and producing protein hydrolysate.
KeywordsChicken feathers Disulphide bonds Microwave-alkali treatment Morphological changes Thiols
- 1.Food and Agriculture Organization: food outlook biannual report on global food markets. http://www.fao.org/docrep/019/i3751e/i3751e.pdf. Accessed 8 Sept 2014
- 3.Onuoha, S.C., Chukwura, E.I.: Effect of temperature and pH on bacterial degradation of chicken feather waste (CFW). Int. J. Sci. Nat. 2(3), 538–544 (2011)Google Scholar
- 5.Karthikeyan, R., Balaji, S., Sehgal, P.: Industrial applications of keratins: a review. J. Sci. Ind. Res. 66, 710–715 (2007)Google Scholar
- 6.Krilova, V., Popov, V.: A method for production of protein hydrolysate from a keratin source. SU Patent 1, 161-064 (1983)Google Scholar
- 7.Kumar, D.M., Lavanya, S., Priya, S.: Production of feather protein concentrate from feathers by in vitro enzymatic treatment, its biochemical characterization and antioxidant nature. Middle-East J. Sci. Res. 11(7), 881–886 (2012)Google Scholar
- 9.Sharma, R., Rajak, R.C.: Keratinophilic fungi: natures keratin degrading machines! Their isolation, identification and ecological role. Resonance 4, 28–40 (2013)Google Scholar
- 10.Wanitwattanarumlug, B., Luengnaruemitchai, A., Wongkasemjit, S.: Characterization of corn cobs from microwave and potassium hydroxide pretreatment. World Acad. Sci. Eng. Technol. 64, 592–596 (2012)Google Scholar
- 14.Lowry, O.H.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)Google Scholar
- 15.Kormin, F., Abdurahma, N.H., Yunus, R.M., Riyai, M.: Study the heating mechanisms of temperature controlled microwave closed systems (TCMCS). Int. J. Eng. Sci. Innov. Technol. 2(5), 417–429 (2013)Google Scholar
- 17.Gupta, A., Kamarudin, N.B., Chua, Y.G.K., Yunus, R.B.M.: Extraction of keratin protein from chicken feather. J. Chem. Chem. Eng. 6(8), 732 (2012)Google Scholar
- 18.Hauser, N.J.: Non-enzymatic Site-Specific Cleavage of Proteins for the Identification of Bacteria with Mass Spectrometry. ProQuest LLC, Michigan (2008)Google Scholar
- 23.Bond, T., Hughes, C.: A-level complete guide chemistry. Cosmic Services, London (1994)Google Scholar
- 24.Lieberman, M., Marks, A.D., Smith, C.: Marks’ Essentials of Medical Biochemistry. Lippincott Williams & Wilkins, USA (2007)Google Scholar
- 27.Myers, R.: The Basics of Chemistry. Greenwood Publishing Group Inc., USA (2003)Google Scholar
- 28.Connor, J., Godfrey, S., Milsom, G.: Beauty Therapy Sciences. Heinemann Educational Publishers, UK (2004)Google Scholar
- 29.Judelson, H.: Operation of the Autoclaves. http://oomyceteworld.net/protocols/autoclave%20operation.pdf Accessed 6 Nov 2014
- 30.Calabro, E., Magazu, S.: Comparison between conventional convective heating and microwave heating: an FTIR spectroscopy study of the effects of microwave oven cooking of bovine breast meat. J. Electromagn. Anal. Appl. 4, 433–439 (2012)Google Scholar
- 31.Hernandez, A.L.M., Santos, C.V.: Keratin fibers from chicken feathers: structure and advances in polymer composites. In: Dullaart, R., Mousquès, J. (eds.) Keratin: Structure, Properties and Applications. Nova Science Publishers, New York (2012)Google Scholar
- 32.Khosa, M.A., Wu, J., Ullah, A.: Chemical modification, characterization, and application of chicken feathers as novel biosorbents. R. Soc. Chem. 3, 20800–20810 (2013)Google Scholar