Chemical composition and techno-functional properties of high-purity water-soluble keratein and its enzymatic hydrolysates
Abstract
This study compared the effectiveness of urea-containing and urea-free L-cysteine solutions in extracting high-quality feather keratin and evaluated commercial proteases for producing keratin-derived bioactive peptides. The urea-assisted extraction was crucial for achieving high structural integrity and yield of soluble keratin. The keratin isolate exhibited oil-holding capacity of 9.37 g/g, foaming capacity of up to 127 %, and emulsifying capacity of up to 49 %. Its proteolysis with trypsin, chymotrypsin, pepsin and subtilisin resulted in peptides with average molecular weight between 2.10 and 5.96 kDa and degree of hydrolysis from 6 to 36 %. The subtilisin hydrolysate had the highest degree of hydrolysis, 63 % of peptides <1 kDa, and excellent solubility across a wide pH range, but negligible water and oil-binding, foaming, and emulsifying properties. This study highlights the need to optimize each step in keratin extraction and hydrolysis processes to produce high-quality bioactive keratin preparations for diverse applications, including food and pharmaceutical.
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- DOI:
- Digital Object Identifier (open in new tab) 10.1016/j.foodchem.2024.142641
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- Category:
- Articles
- Type:
- artykuły w czasopismach
- Published in:
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FOOD CHEMISTRY
no. 472,
ISSN: 0308-8146 - Language:
- English
- Publication year:
- 2025
- Bibliographic description:
- Taraszkiewicz A., Sinkiewicz I., Sommer A., Kusznierewicz B., Giblin L., Staroszczyk H.: Chemical composition and techno-functional properties of high-purity water-soluble keratein and its enzymatic hydrolysates// FOOD CHEMISTRY -Vol. 472, (2025), s.142641-
- DOI:
- Digital Object Identifier (open in new tab) 10.1016/j.foodchem.2024.142641
- Sources of funding:
- Verified by:
- Gdańsk University of Technology
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