Limited enzymatic hydrolysis induced pea protein gelation at low protein concentration with less heat requirement

Heat-induced plant protein gels commonly require high concentration and temperatures. However, hydrolysis of some proteins may promote their gelation under milder conditions. In this study, Alcalase (EC No. 3.4.21.62) was used to quickly (3 min) hydrolyze pea proteins, the physicochemical properties gelling capacity hydrolysates were investigated. Hydrolysates showed a degree more than 6.5%, most peptides smaller 15 kDa. Their intrinsic fluorescence intensity surface hydrophobicity lower compared those solutions, indicating increased water accessibility polarity. Differential scanning calorimetry (DSC) onset denaturation temperatures higher in proteins. But former unstable at (85 °C) aggregated form 5% concentration. Pea hydrolysate exhibited an average G’ ?170 Pa ?15 pH7 pH8, respectively. viscosities ?30–80 times solution low shear rate (<0.1 s?1) same pH heating The addition NaCl, urea, thiourea, dithiothreitol decreased gel strength remarkably, suggesting electrostatic hydrophobic interactions, hydrogen disulfide bonds contributed gelation. Confocal electron microscopy that hydrolysates-based either formed network composed thread-like structure (pH7) or large coarse aggregates with irregular shapes (pH8). findings shed light on mechanisms enzymatically modified