Production of hydrolysates and peptides from a new protein source: Diplodus annularis

Hamed, Fatma, et al. “Production of hydrolysates and peptides from a new protein source: Diplodus annularis.” Food Bioscience 50 (2022): 102129.


In the present study, Diplodus proteins were hydrolyzed using one of two proteases alcalase and savinase, then, the hydrolysates were characterized by their chemical composition, functional properties and peptide content. Protein hydrolysates of Diplodus annularis with different degrees of hydrolysis (DH of 8.14% and 15.42%) were prepared using the enzymes alcalase® and savinase®. The protein hydrolysates obtained by treatment with savinase® had a higher protein content than that produced with alcalase®. Both hydrolysates showed great heterogeneity in their peptide composition. In comparison with the alcalase generated hydrolysate, savinase hydrolysate is richer in hydrophobic peptides as shown by RP-HPLC results. Also, the RP-HPLC-MS/MS, according to database survey, allowed the identification of 906 peptides in this hydrolysate against only 536 peptides in the alcalase hydrolysate. Regarding the functional properties, the maximum solubility values, the best foaming properties and the greatest oil and water retention capacities were obtained with the hydrolysate produced by savinase action. The emulsifying property and emulsion stability showed higher values for the alcalase generated hydrolysate with a lower degree of hydrolysis. As a consequence of increasing hydrolysate concentrations, the emulsifying activity index decreased. Conversely, the foaming abilities increased as the hydrolysate concentrations increased. The results of the present study suggest that alcalase and savinase can be used for the conversion of Diplodus annularis proteins into numerous peptides with promising functional properties.