New insights into modifying structure and techno-functional properties of sesame protein: high-pressure homogenization coupled with pH-shifting.

Abstract

High-pressure homogenization (HPH) was investigated as a strategy to modify sesame protein isolate (SMPI) combined with pH shifting. SMPI was adjusted to pH 2.0, 7.0, and 11.0 and processed at 50, 100, or 150 MPa (1 cycle, 25 °C). HPH induced pH-dependent structural rearrangements that affected the techno-functional properties of SMPI. At pH 2.0, HPH at 150 MPa increased Ho by 131% and promoted random-coil structures, accompanied by changes in solubility (135%), EAI (43%) and WHC (21%), relative to its respective control., At 50 MPa/pH 7.0, structural rearrangements were reflected by changes in zeta potential, fluorescence, and secondary structure, resulting in improved OHC (108%) and EAI (67%), compared to the control. 150 MPa/pH 11.0 promoted β-sheet structure, solubility (178%), EAI (5%) and OHC (19%) increase relative to the control. Overall, HPH combined with pH-shifting offers a condition-dependent strategy for tailoring SMPI functionality for specific food applications.