Effects of deamidation by protein glutaminase on the flavor binding properties of pea protein isolate

Abstract

° values suggested that the interactions are entropy-driven and primarily hydrophobic in nature, which was confirmed using molecular docking studies, with stronger bonding to vanillin observed for PPI than for deamidated PPI. Sensory evaluation revealed that deamidation promoted flavor release. Thus, PG deamidation enhances flavor delivery performance, positioning deamidated PPI as promising protein-based component for improving flavor interactions in food applications.