Alcalase hydrolysis modulates the techno-functional properties of dry-fractionated pea protein, reduces the off-flavor compounds and refines the aroma profile.

Dry fractionation is recognized as one of the most sustainable protein extraction methods, but dry-fractionated proteins often show limited techno-functional versatility and unfavorable sensory profile typical of raw legumes. In this study, Alcalase hydrolysis of dry-fractionated pea protein was evaluated under different processing time (15, 97.5,140,180 min) and temperature (50-60 °C) to assess its effects on protein structure, techno-functional properties, volatile and odor-active compounds. Hydrolysis markedly increased the degree of hydrolysis (up to ⁓48 % after 180 min at 60 °C) and total free amino acids, leading to the formation of smaller and polar peptides, as also confirmed by fluorescence spectroscopy. The structural modifications directly affected the techno-functional properties. In fact, hydrolyzed samples exhibited higher water solubility and lower viscosity than non-hydrolyzed proteins, indicating improved dispersion properties. Conversely, prolonged hydrolysis negatively affected foaming ability and foam stability, due to the formation of low-molecular-weight peptides. A significant reduction was observed in marker volatile compounds associated with green and beany notes, including hexanal, 2-heptanone, 1-hexanol, and 1-penten-3-ol. GC-MS-O analysis identified 22 odor-active compounds. Most undesired odor-active compounds decreased following hydrolysis, whereas compounds contributing to more pleasant notes remained largely unaffected. Overall, Alcalase hydrolysis modulates the techno-functional properties and refines the aroma profile of dry-fractionated pea protein. These findings support the use of enzymatic hydrolysis to expand the use of dry-fractionated pulse proteins in food formulations while mitigating sensory limitations.