Heat-time-controlled chickpea protein aggregates: structure-function-digestibility interplay and Pickering emulsion performance.

This study systematically investigated the modulation effects of heating duration (0-60 min) on the structure, functional properties, and Pickering emulsion performance of chickpea protein aggregates (CPAs). CPAs heated for 30 min (CPAs-30) exhibited favorable properties: the smallest particle size (534.67 nm) and zeta potential (-26.6 mV), and enhanced colloidal stability compared to other heating durations. Further mechanistic analysis revealed that a synergistic stabilization mechanism involving enhanced hydrophobic interactions (contact angle increased from 71.75° to 77.8°, surface hydrophobicity rose 10.47-fold, β-sheet content increased from 36.9% to 46.7%), disulfide cross-linking, and hydrogen bonding. Consequently, emulsifying activity and stability increased by 1.42-fold and 3.79-fold, respectively, while interfacial adsorption capacity improved 1.07-fold, forming an elastic network (G' > G″). In vitro digestion assays further confirmed that CPAs-30 exhibited enhanced gastrointestinal resistance. This work establishes a structure-function framework for the rational design of high-performance plant protein colloids through controlled thermal aggregation.