Determining the Optimal Conditions for Extracting Keratin Protein from Chicken Feathers by Hydrolysis

Optimization of Keratin Extraction from Chicken Feathers

Authors

  • D.Dugersuren Master student in Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia
  • B.Khongorzul Master student in Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia
  • B. Byambasuren Master student in Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia
  • Kh. Boldbaatar Research and Development Institute of Light Industry, Mongolian University of Science and technology
  • O.Ganzorig Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia
  • T.Khigshjargal Department of Chemical and Biological Engineering, School of Engineering and Technology, National University of Mongolia, Ulaanbaatar, Mongolia Center for Nanoscience and Nanotechnology, National University of Mongolia, Ulaanbaatar, Mongolia
  • B. Jambaldorj Department of Chemical and Biological Engineering, School of Engineering and Technology, National University of Mongolia, Ulaanbaatar, Mongolia Center for Nanoscience and Nanotechnology, National University of Mongolia, Ulaanbaatar, Mongolia

Keywords:

keratin, chicken feather, hydrolysis

Abstract

Chicken feathers, a byproduct of poultry farming, consist of approximately 90% keratin protein and are a protein-rich raw material [1]. Keratin is highly resistant to chemical and physical influences and degrades slowly in nature, causing environmental pollution when discarded. Currently, there are no industries or businesses in Mongolia processing waste chicken feathers. To extract keratin protein hydrolysates from chicken feathers, hydrolysis using sodium hydroxide (NaOH), hydrogen peroxide (H2O2), and a combination of NaOH and H2O2 was employed. The feather microstructure was analyzed by scanning electron microscopy (SEM), protein yield by Kjeldahl and gravimetric methods, molecular weight by SDS-PAGE electrophoresis, structural analysis by Fourier-transform infrared spectroscopy (FT-IR), and thermal properties by thermogravimetric analysis (TG/DTA). The study found that protein yield varied with hydrolysate composition and temperature. A 4% NaOH hydrolysate resulted in the highest yield of 74.8%, while a 2M H2O2 + NaOH hydrolysate produced a 61.5% yield. High-temperature, short-duration experiments produced gel-like protein hydrolysates. This research determined some optimal conditions for preparing high-yield keratin hydrolysates from discarded chicken feathers in Mongolia. These findings can serve as a foundation for future industrial applications and further research.

Downloads

Download data is not yet available.

Author Biographies

D.Dugersuren, Master student in Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia

Researcher in nanoscience and nanoengineering

B.Khongorzul, Master student in Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia

Researcher in nanoscience and nanoengineering

B. Byambasuren, Master student in Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia

Researcher in biotechnology and biomaterials

Kh. Boldbaatar, Research and Development Institute of Light Industry, Mongolian University of Science and technology

Researcher in Chemical technology and biomaterials

O.Ganzorig, Department of Biology, School of Arts and Sciences, National University of Mongolia, Ulaanbaatar, Mongolia

Researcher in food biotechnology

T.Khigshjargal, Department of Chemical and Biological Engineering, School of Engineering and Technology, National University of Mongolia, Ulaanbaatar, Mongolia Center for Nanoscience and Nanotechnology, National University of Mongolia, Ulaanbaatar, Mongolia

Researcher in nanoscience, nanoengineering and quantum simulation

B. Jambaldorj, Department of Chemical and Biological Engineering, School of Engineering and Technology, National University of Mongolia, Ulaanbaatar, Mongolia Center for Nanoscience and Nanotechnology, National University of Mongolia, Ulaanbaatar, Mongolia

Researcher in nanoscience and biomaterials

References

Alahyaribeik, S., Zubair, M. and Ullah, A. 2024. Eco-friendly innovations for enhancing value from farm to function using poultry feathers. Process Bi-ochemistry. 147, (Dec. 2024), 402–417. https://doi.org/10.1016/j.procbio.2024.10.007.

Yadav, S. and Khosla, B. 2021. Biodegradation of poultry feather waste by keratinase producing Bacil-lus cereus strain isolated from poultry farms waste disposal site. Case Studies in Chemical and Envi-ronmental Engineering. 4, (Dec. 2021), 100114. https://doi.org/10.1016/j.cscee.2021.100114.

Sharma, S. and Gupta, A. 2016. Sustainable Man-agement of Keratin Waste Biomass: Applications and Future Perspectives. Brazilian Archives of Biol-ogy and Technology. 59, 0 (2016). https://doi.org/10.1590/1678-4324-2016150684.

Chinta S.K., Landage S.M., Yadav Krati (2013). Application of Chicken Feathers in Technical Tex-tiles. International Journal of Innovative Research in Science, Engineering and Technology, 2(4), 1158-1165. ISSN: 2319-8753.

Chinta S.K., Landage S.M., Yadav Krati (2013). Application of Chicken Feathers in Technical Tex-tiles. International Journal of Innovative Research in Science, Engineering and Technology, 2(4), 1158-1165. ISSN: 2319-8753.

Chilakamarry, C.R., Mahmood, S., Saffe, S.N.B.M., Arifin, M.A.B., Gupta, A., Sikkandar, M.Y., Begum, S.S. and Narasaiah, B. 2021. Extraction and applica-tion of keratin from natural resources: a review. 3 Biotech. 11, 5 (May 2021), 220. https://doi.org/10.1007/s13205-021-02734-7.

Reddy, N. and Yang, Y. 2007. Structure and Proper-ties of Chicken Feather Barbs as Natural Protein Fi-bers. Journal of Polymers and the Environment. 15, 2 (Apr. 2007), 81–87. https://doi.org/10.1007/s10924-007-0054-7.

Kim, J.-D. 2005. Immobilization of Keratinase from Aspergillus flavus K-03 for Degradation of Feather Keratin. Mycobiology. 33, 2 (Jun. 2005), 121–123. https://doi.org/10.4489/MYCO.2005.33.2.121.

Kakkar, P., Madhan, B. and Shanmugam, G. 2014. Extraction and characterization of keratin from bo-vine hoof: A potential material for biomedical ap-plications. SpringerPlus. 3, 1 (Dec. 2014), 596. https://doi.org/10.1186/2193-1801-3-596.

Stępień, A. and Kennedy, J.F. 2008. Study on the structure and properties of wool keratin regenerated from formic acid. International Journal of Biologi-cal Macromolecules. 42, 4 (May 2008), 402. https://doi.org/10.1016/j.ijbiomac.2007.12.006.

Singh, S. 2021. Keratin - based materials in Bio-medical engineering. IOP Conference Series: Mate-rials Science and Engineering. 1116, 1 (Apr. 2021), 012024. https://doi.org/10.1088/1757-899X/1116/1/012024.

Ye, Y., Xue, X., Huang, L., Gan, M., Tong, C., Wang, K. and Deng, J. 2020. A new perspective to map the supply and demand of artificial night light based on Loujia1-01 and urban big data. Journal of Cleaner Production. 276, (Dec. 2020), 123244. https://doi.org/10.1016/j.jclepro.2020.123244.

Chiego, B. and Silver, H. 1942. The Effect of Alka-lis on the Stability of Keratins1. Journal of Investi-gative Dermatology. 5, 2 (Apr. 1942), 95–103. https://doi.org/10.1038/jid.1942.15.

Jones, J. and J, B. 1991. Kjeldahl Method for Nitro-gen Determination. MicroMacro Publishing Inc.

2024. Introduction to SDS-PAGE - Separation of Proteins Based on Size.

Mohammed, A. and Abdullah, A. 2018. Scanning Electron Microscopy (SEM): Review.

Fourier Transform Infrared Spectroscopy- an over-view | ScienceDirect Topics.

P, I. Thermogravimetric Analysis (TGA) TGA 8000 TGA 4000 STA 6000/ STA 8000 The Thermograv-imetric Instrument Family.

Mahmud, A.D., Aliyu, Z., Abdullahi Oluwatoyin, B., Ahmed, A., Yahaya A, S. and Mohammed Saleh, A. 2023. Extraction and Characterization of Keratin Protein from Chicken Feathers using Alkaline Hy-drolysis Method: Effects of Sodium Sulphide Con-centration and Shelf-life Evaluation. Malaysian Journal of Catalysis. 7, 2 (Dec. 2023), 37–41. https://doi.org/10.11113/mjcat.v7n2.173.

Downloads

Published

2026-04-28

How to Cite

[1]
D. Dugersuren, “Determining the Optimal Conditions for Extracting Keratin Protein from Chicken Feathers by Hydrolysis: Optimization of Keratin Extraction from Chicken Feathers ”, Mong. J. Eng. Appl. Sci., vol. 7, no. 1, Apr. 2026.

Issue

Vol. 7 No. 1 (2025)

Section

Articles

License

Copyright (c) 2025 D.Dugersuren, B.Khongorzul, B. Byambasuren, Kh. Boldbaatar, O.Ganzorig, T.Khigshjargal, B. Jambaldorj

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.