Bovine liver hydrolysates based on six proteases: Physicochemical properties, emulsification characteristics, antioxidant capacity assessment, and peptide identification

This study aimed to study the physicochemical, antioxidant, and emulsifying properties of bovine liver hydrolysates based on pepsin, alkaline protease, neutral protease, trypsin, papain, and flavor proteinase, and to identify proteins and peptides in bovine liver hydrolysates. The physicochemical properties of bovine liver hydrolysate were evaluated using gel permeation chromatography, surface hydrophobicity, fourier transforms infrared and fluorescence spectroscopy, and the antioxidant and emulsifying capacity of six bovine liver hydrolysates were characterized. The results showed that enzymatic hydrolysis by the six proteases decreased the molecular weight of the hydrolysate while increasing the content of hydrophobic amino acids and negatively charged amino acids. Among all proteases tested, alkaline protease exhibited the highest DH (13.3%) and protein recovery (37.3%). The concentration levels (1–5 mg/mL) positively correlated with antioxidant properties in alkaline protease hydrolysate, the hydrolysis ability of pepsin is relatively weak, and there is a significant difference between pepsin and other proteases, which was also reflected in its antioxidant capacity. Thus, alkaline protease hydrolysates were chosen for identification, and information on 3894 peptides was obtained, these findings provide a basis for expanding the application potential of bovine liver hydrolysate as a bioactive component in the food or pharmaceutical industry. • Bovine liver hydrolysates obtained by six proteases. • To assess their physicochemical properties, antioxidant and emulsifying capacity. • Identification of proteins and peptides in bovine liver hydrolysates.