Studying the release of soybean taste-active peptides prepared by proteases derived from different fungi through...

This study investigated the release of taste-active peptides from soybean isolate catalyzed by proteases from Aspergillus flavus strains. The frequent presence of Leu at the C-terminus and the hydrophilic amino acids at the N-terminus related to bitterness and umami taste of hydrolysates, respectively. Detailly, H40650 demonstrating high umami, low bitterness, and a high peptide yield. During the hydrolysis of H40650, umami taste changes were associated with the content of peptides <1 kDa and 28 umami peptides, while bitterness was linked to the content of peptides <3 kDa and 30 bitter peptides. Additionally, most taste-active peptides were derived from the 7S globulin α subunit and 11S globulin G2. The protease produced by CGMCC 40650 has marked specificity for the region of 281-333 amino acids in protein P0D15, which contained 24.53 % umami amino acids. These findings could offer new insights into the preparation of taste-active peptides.