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Updated: Oct 2, 2026
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
New insights into modifying structure and techno-functional properties of sesame protein: high-pressure
Beatriz Lederman Valente1, Ingrid Alves de Moraes1, Douglas Fernandes Barbin1
1Department of Food Engineering and Technology, School of Food Engineering, University of Campinas (UNICAMP), Campinas, SP, Brazil.
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.
