ArticleEnvironmental science and pollution research international2017
Degradation and regeneration of feather keratin in NMMO solution.
Article in Environmental science and pollution research international, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Sustainable valorization of poultry waste through optimized keratin extraction and its prospective use in dye adsorption.BMC chemistry · 2026Article
- Extraction of keratin particles as intact protein sequences from chicken feathers and their characterization.Biomaterials and biosystems · 2026Article
- Affinity of Keratin Peptides for Cellulose and Lignin: A Fundamental Study toward Advanced Bio-Based Materials.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Development of novel and ecological keratin/cellulose-based composites for absorption of oils and organic solvents.Environmental science and pollution research international · 2021Article
- Ductile keratin films from deep eutectic solvent-fractionated feathers.RSC advances · 2021Article
- Green process to regenerate keratin from feathers with an aqueous deep eutectic solvent.RSC advances · 2019Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chicken feather, a potential source of keratin, is often disposed as waste material. Although some methods, i.e., hydrolysis, reduction, and oxidation, have been developed to isolate keratin for composites, it has been limited due to the rising environmental concerns. In this work, a green solvent N-methylmorpholine N-oxide (NMMO) was used to extract keratin from chicken feather waste. Eighty-nine percent of keratin was extracted using 75% NMMO solution. However, the result from size exclusion HPLC showed that most of the keratin degraded into polypeptide with molecular weight of 2189 and only 25.3% regenerated keratin was obtained with molecular weight of 14,485. Analysis of amino acid composition showed a severe damage to the disulfide bonds in keratin during the extraction procedure. Oxidization had an important effect on the reconstitution of the disulfide bonds, which formed a stable three-dimensional net structure in the regenerated keratins. Besides, Raman spectra, NMR, FT-IR, XRD, and TGA were used to characterize the properties of regenerated keratin and raw chicken feather. In the end, a possible mechanism was proposed based on the results.
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