Improving common vetch protein isolate flavor through glutaminase-mediated deamidation.

ABSTRACT

Common vetch protein, similar to pea protein, offers valuable qualities like being non-GMO, hypoallergenic, and nutritious. However, its strong beany flavor hinders consumer acceptance. This study explores enzymatic deamidation using glutaminase to address this issue. GC-MS analysis identified 54 volatile compounds in the raw material protein, with 2-pentylfuran, hexanal, and several nonenals contributing the most to the undesirable aroma. Principal component analysis (PCA) confirmed the effectiveness of glutaminase deamidation in removing these off-flavors. The study further reveals that deamidation alters the protein's secondary structure, with an increase in α - helix structure and a decrease in ß - sheet structure. The surface hydrophobicity increased from 587.33 ± 2.63 to 1855.63 ± 3.91 exposing hydrophobic clusters that bind flavor compounds. This disruption weakens the interactions that trap these undesirable flavors, ultimately leading to their release and a more pleasant aroma. These findings provide valuable insights for enzymatic deodorization of not only common vetch protein but also pea protein.