Advertisement

Waste and Biomass Valorization

, Volume 7, Issue 5, pp 1147–1157 | Cite as

Microwave-Alkali Treatment of Chicken Feathers for Protein Hydrolysate Production

  • Yen Sze Lee
  • Lai-Yee PhangEmail author
  • Siti Aqlima Ahmad
  • Peck Toung Ooi
Original Paper

Abstract

Purpose

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.

Methods

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).

Results

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.

Conclusions

Microwave-alkali treatment was more efficient than conventional treatments in breaking down the disulphide bonds, disrupting the feather structure and producing protein hydrolysate.

Keywords

Chicken feathers Disulphide bonds Microwave-alkali treatment Morphological changes Thiols 

References

  1. 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
  2. 2.
    Forgacs, G., Lundin, M., Taherzadeh, M.J., Horvath, I.S.: Pretreatment of chicken feather waste for improved biogas production. Appl. Biochem. Biotechnol. 169, 2016–2028 (2013)CrossRefGoogle Scholar
  3. 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
  4. 4.
    Papadopoulos, M., El Boushy, A., Roodbeen, A., Ketelaars, E.: Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal. Anim. Feed Sci. Technol. 14, 279–290 (1986)CrossRefGoogle Scholar
  5. 5.
    Karthikeyan, R., Balaji, S., Sehgal, P.: Industrial applications of keratins: a review. J. Sci. Ind. Res. 66, 710–715 (2007)Google Scholar
  6. 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. 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
  8. 8.
    Bellagamba, F., Caprino, F., Mentasti, T., Vasconi, M., Moretti, V.M.: The impact of processing on amino acid racemization and protein quality in processed animal proteins of poultry origin. Ital. J. Anim. Sci. 14(2), 238–245 (2015)CrossRefGoogle Scholar
  9. 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. 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
  11. 11.
    Kratchanova, M., Pavlova, E., Panchev, I.: The effect of microwave heating of fresh orange peels on the fruit tissue and quality of extracted pectin. Carbohydr. Polym. 56(2), 181–185 (2004)CrossRefGoogle Scholar
  12. 12.
    Basile, F., Hauser, N.: Rapid online non-enzymatic protein digestion combining microwave heating acid hydrolysis and electrochemical oxidation. J. Anal. Chem. 83(1), 359–367 (2011)CrossRefGoogle Scholar
  13. 13.
    Sangali, S., Brandelli, A.: Feather keratin hydrolysis by a Vibrio sp. strain kr2. J. Appl. Microbiol. 89, 735–743 (2000)CrossRefGoogle Scholar
  14. 14.
    Lowry, O.H.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)Google Scholar
  15. 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
  16. 16.
    Costa, J.C., Barbosa, S.G., Sousa, D.Z.: Thermochemical pre- and biological co-treatments to improve hydrolysis and methane production from poultry litter. Bioresour. Technol. 111, 141–147 (2012)CrossRefGoogle Scholar
  17. 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. 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
  19. 19.
    Zhong, H.Y., Marcus, S.L., Li, L.: Microwave-assisted acid hydrolysis of proteins combined with liquid chromatography MALDI MS/MS for protein identification. J. Am. Soc. Mass Spectrom. 16, 471–481 (2005)CrossRefGoogle Scholar
  20. 20.
    Reiz, B., Li, L.: Microwave-assisted acid and base hydrolysis of intact proteins containing disulfide bonds for protein sequence analysis by mass spectrometry. J. Am. Soc. Mass Spectrom. 21, 1596–1605 (2010)CrossRefGoogle Scholar
  21. 21.
    Moritz, J.S., Latshaw, J.D.: Indicators of nutritional value of hydrolyzed feather meal. Poult. Sci. 80, 79–86 (2001)CrossRefGoogle Scholar
  22. 22.
    Coward-Kelly, G., Agbogbo, F.K., Holtzapple, M.T.: Lime treatment of keratinous materials for the generation of highly digestible animal feed: 2. Animal hair. Bioresour. Technol. 97, 1344–1352 (2006)CrossRefGoogle Scholar
  23. 23.
    Bond, T., Hughes, C.: A-level complete guide chemistry. Cosmic Services, London (1994)Google Scholar
  24. 24.
    Lieberman, M., Marks, A.D., Smith, C.: Marks’ Essentials of Medical Biochemistry. Lippincott Williams & Wilkins, USA (2007)Google Scholar
  25. 25.
    Goddard, E.D., Grubber, J.V.: Principle of Polymer Science and Technology in Cosmetics and Personal Care. Marcel Dekker Inc., USA (1999)CrossRefGoogle Scholar
  26. 26.
    Elhafi, G., Naylor, C.J., Savage, C.E., Jones, R.C.: Microwave or autoclave treatments destroy infectivity of infectious bronchitis virus and avian pnemovirus but allow detection by reverse transcriptase-polymerase chain reaction. Avian Pathol. 33(3), 303–306 (2004)CrossRefGoogle Scholar
  27. 27.
    Myers, R.: The Basics of Chemistry. Greenwood Publishing Group Inc., USA (2003)Google Scholar
  28. 28.
    Connor, J., Godfrey, S., Milsom, G.: Beauty Therapy Sciences. Heinemann Educational Publishers, UK (2004)Google Scholar
  29. 29.
    Judelson, H.: Operation of the Autoclaves. http://oomyceteworld.net/protocols/autoclave%20operation.pdf Accessed 6 Nov 2014
  30. 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. 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. 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
  33. 33.
    Trabocchi, A., Occhiato, E.G., Potenza, D., Guarna, A.: Synthesis and conformational analysis of small peptides containing 6-Endo-BT(t)L scaffolds as reverse turn mimetics. J. Org. Chem. 67, 7483–7492 (2002)CrossRefGoogle Scholar
  34. 34.
    Wang, X., Parsons, C.M.: Effect of processing systems on protein quality of feather meals and hog hair meals. Poult. Sci. 76(3), 491–496 (1997)CrossRefGoogle Scholar
  35. 35.
    Tiwary, E., Gupta, R.: Rapid conversion of chicken feather to feather meal using dimeric keratinase from Bacillus licheniformis ER- 15. J. Bioprocess. Biotech. 2, 123 (2012)CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  • Yen Sze Lee
    • 1
  • Lai-Yee Phang
    • 1
    Email author
  • Siti Aqlima Ahmad
    • 2
  • Peck Toung Ooi
    • 3
  1. 1.Department of Bioprocess TechnologyUniversiti Putra MalaysiaSerdangMalaysia
  2. 2.Department of Biochemistry, Faculty of Biotechnology and Biomolecular SciencesUniversiti Putra MalaysiaSerdangMalaysia
  3. 3.Department of Veterinary Clinical Studies, Faculty of Veterinary MedicineUniversiti Putra MalaysiaSerdangMalaysia

Personalised recommendations