Understanding the differences in heat-induced gel properties of twelve legume proteins: A comparative study.

This study aimed to investigate the rheological and textural properties of heat-induced gels from twelve legume protein isolates at pH 3.0 and 7.0, including black kidney bean (BKPI), speckled kidney bean (SKPI), panda bean (PDPI), cowpea (CPPI), mung bean (MPI), adzuki bean (API), rice bean (RPI), black soybean (BPI), soybean (SPI), chickpea (CPI), broad bean (BRPI) and pea (PPI). SDS-PAGE revealed that 7S globulin was prominent protein in BKPI, SKPI, PDPI, CPPI, MPI, API and RPI, the main protein fraction of CPI was 11S globulin, and BPI, SPI, BRPI and PPI contained both 7S and 11S globulins as major components. Based on the gel's Power Law constant (K') and hardness, twelve legume proteins were divided into three categories with high, medium and low gel strength. BKPI, SKPI and PDPI with Phaseolin being the major protein fraction showed high gel strength regardless of pH. Electrostatic interactions, hydrophobic interactions and hydrogen bonds were the most important intermolecular forces in the formation of legume protein gel networks, of which gel strength at pH 3.0 and pH 7.0 was significantly affected by electrostatic interactions and hydrogen bonds, respectively. Moreover, gel strength was also remarkably negatively influenced by the non-network proteins. SEM observation indicated that the microstructure of gels at pH 7.0 was denser and more homogeneous than that at pH 3.0, leading to better water holding capacity. These findings would be of great importance for understanding the differences in legume protein gels, and also laid the scientific support for expanding applications of legume proteins in gel-based foods.