Modulating structure and gelation properties of mung bean protein via controlled enzymatic hydrolysis

The limited functional properties of plant proteins, such as poor gelation, restrict their performance in food formulation. Limited enzymatic hydrolysis is an effective way to modify protein structure and enhance gelation. We systematically investigated the mechanism by which limited enzymatic hydrolysis with alcalase promoted heat-induced gelation of mung bean protein. A 100 g/L protein solution was enzymatically treated for varying durations and heated at 90 °C for 30 min to induce gel formation. Secondary structural analysis indicated that hydrolysis induced a transition from an ordered conformation to a more disordered state, accompanied by decreased surface hydrophobicity (H 0 ). Results indicated that samples hydrolysed for 1 and 3 min (degree of hydrolysis [DH] 1.26% and 2.48%) formed gels with elastic, solid-state characteristics. This suggests that appropriate hydrolysis facilitates gel formation, with hydrophobic interactions dominating protein hydrolysate gelation. In contrast, the unhydrolysed sample and those hydrolysed for >3 min (DH > 2.48%) did not form gels. Short-time hydrolysed samples formed dense and homogeneous gel network structures and enhanced the strength and water-holding capacity. This study provides a theoretical basis for processing plant proteins under mild conditions to fabricate gels with desirable structures and expand the high-value application of mung bean protein.