Fava bean protein hydrolysate improves gel quality and freeze–thaw stability of threadfin bream surimi gel

Information from the abstract

ABSTRACT Fava bean ( Vicia faba L. ) protein hydrolysates (FBPH) of various degrees of hydrolysis (DH; 20%, and 30%,) were produced using alcalase. Regardless of antioxidant assays, FBPH of DH 30 (FB-30) showed the highest antioxidant activities than the FBPH of DH 20% (FB-20). Similarly, FB-30 demonstrated cryoprotective potential, as indicated by thermal properties and enhanced Candida rugosa survival during freeze–thaw cycles in a yeast cell model than FB-20. Selected fava bean protein hydrolysate (FB-30) had higher polar amino and non-essential amino acids contents than their counterparts. Peptide profiling revealed dominant peptides of 16.01, 2.49, and 0.14 kDa. When added to surimi gel, 2% FBPH produced the highest breaking force (429.9 g), deformation (1.08 cm), and lowest expressible moisture (4.67%). Moreover, the rheology and microstructure also showed an elastic and denser structure. Furthermore, after being subjected to FT cycles, fewer ice crystals and lower lipid oxidation was noticed in gel added with 2% FB-30. Although the whiteness was slightly decreased, 2% FB-30 effectively enhanced surimi gel quality, highlighting its potential as a natural additive with antioxidant, gelling and cryoprotective agent for frozen food applications.

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Related topics: Protein Hydrolysis and Bioactive Peptides · Proteins in Food Systems · Insect Utilization and Effects