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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:
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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