A novel alcalase-hydrolyzed soybean meal hydrolysates prepared using by-product material: Structure, function property, sensory property, and biological activity

This work investigated the effects of different hydrolysis times (0.5, 1 and 2 h) on the structure, interface and sensory properties, and biological activity of soybean meal peptides obtained by alcalase protease hydrolysis. After hydrolyzation, the molecular weight of soybean meal hydrolysates (SMHs) was below 10 kDa. An increase in the number of β-turns and a decrease in α-helices suggested the unfolding of soybean meal proteins. The ultraviolet absorption and fluorescence intensities of SMHs increased, suggesting an increase in the content of free amino acids, which likely contributed to the biological activity of SMHs. Additionally, after hydrolyzation for 1 h, the SMHs showed the highest antioxidant and ACE inhibitory activity. LC-MS/MS-based peptidomics analysis showed 101 differential peptides in hydrolysates among different hydrolysis times with reliable potential biological activities. However, the emulsification of the SMHs decreased due to the exposure of hydrophilic amino acids. All in all, hydrolysis time is a factor that influences the peptide sequence and properties, resulting in different antioxidant and ACE inhibitory activities.