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<title>Valorisation of low-valued ray-finned fish (Labeobarbus nedgia) by enzymatic hydrolysis to obtain fish-discarded protein hydrolysates as functional foods</title>
<creator>Tadesse, Solomon Abebaw</creator>
<creator>Emire, Shimelis Admassu</creator>
<creator>Barea Gómez, Pedro</creator>
<creator>Illera Gigante, Alba Ester</creator>
<creator>Melgosa Gómez, Rodrigo</creator>
<creator>Beltrán Calvo, Sagrario</creator>
<creator>Sanz Díez, Mª Teresa</creator>
<subject>Low valued ray-finned fish</subject>
<subject>Protein enzymatic hydrolysate</subject>
<subject>Antioxidant activities</subject>
<subject>Functional properties</subject>
<description>This study investigated the valorisation of low-valued ray-finned fish (Labeobarbus nedgia) (LB) muscle into valuable protein hydrolysates using three commercial enzymes (Alcalase®, Novozym®, and Protease®). After testing different enzyme concentrations (0–3 %, v/w) and temperatures (50–70 °C), the best results, including the highest degree of hydrolysis (DH) and antioxidant activity, were achieved when using Alcalase® at 3 % (v/w) and a temperature of 60 °C. However, Novozym® was found to be more resistant to high temperatures than Alcalase®. Functional properties of freeze-dried protein hydrolysates prepared using Alcalase® and Novozym®, at an enzyme concentration of 3 % (v/w) and a temperature of 60 °C, were determined. Both hydrolysates exhibited similar solubility, water and oil holding capacity, and foaming capacity and stability. This study demonstrated that the low-valued LB muscle can be used to produce a valuable protein hydrolysate, which could be used as a functional ingredient in the food industry.</description>
<date>2024-05-25</date>
<date>2024-05-25</date>
<date>2023-09</date>
<type>info:eu-repo/semantics/article</type>
<identifier>0960-3085</identifier>
<identifier>http://hdl.handle.net/10259/9180</identifier>
<identifier>10.1016/j.fbp.2023.08.003</identifier>
<language>eng</language>
<relation>Food and Bioproducts Processing. 2023, V. 141, p. 167-184</relation>
<relation>https://doi.org/10.1016/j.fbp.2023.08.003</relation>
<rights>http://creativecommons.org/licenses/by/4.0/</rights>
<rights>info:eu-repo/semantics/openAccess</rights>
<rights>Atribución 4.0 Internacional</rights>
<publisher>Elsevier</publisher>
</thesis></metadata></record></GetRecord></OAI-PMH>