Valorisation of low-valued ray-finned fish (Labeobarbus nedgia) by enzymatic hydrolysis to obtain fish-discarded protein hydrolysates as functional foods
2023
Tadesse, Solomon Abebaw | Emire, Shimelis Admassu | Barea Gómez, Pedro | Illera Gigante, Alba Ester | Melgosa Gómez, Rodrigo | Beltrán Calvo, Sagrario | Sanz Díez, Mª Teresa
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.
Show more [+] Less [-]This work was funded by the Agencia Estatal de Investigación (AEI) and Ministerio de Ciencia e Innovación (MICINN) [grant number PID2019-104950RB-I00], by the AEI, MICINN, UE NextGenerationEU (Plan de Recuperación, Transformación y Resiliencia) [grant numbers TED2021-129311B-I00 and PDC2022-133443-I00] and by the Junta de Castilla y León (JCyL) and the European Regional Development Fund (ERDF) [grant number BU050P20]. P. Barea predoctoral contract was funded by JCyL and the European Social Fund (ESF) by ORDEN EDU/1868/2022, de 19 de diciembre. A.E. Illera post-doctoral contracts were funded by JCyL and ERDF through project BU050P20. R. Melgosa contract was funded by a Beatriz Galindo Research Fellowship [BG20/00182].
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