Betanin (BN) is a promising purple-red natural pigment, but its application is hindered by thermal instability. The complex plant protein (RP-SPI) constructed by rice protein (RP) and soy protein isolate (SPI) was used as raw material to investigate the thermal protection effect and protective mechanism of RP-SPI on BN. The results showed that RP-SPI significantly improved the thermal stability of BN, and the retention rate of BN increased from 5.63% to 48.08% when heated at 80 °C for 60 min. Subsequently, the fluorescence spectroscopy, isothermal titration calorimetry (ITC), and molecular docking were utilized to investigate the interaction mechanism between RP-SPI and BN. The results indicated that the main interaction between RP-SPI and BN was hydrogen bond. The interaction changed the secondary structure and reduced surface hydrophobicity of the protein. Meanwhile, morphological observation showed that RP-SPI was a flake protein with a network structure, and a large amount of aggregation occurred...

Keywords
RICE AGGREGATION SPECTROFLUOROMETRY CALORIMETRY BINDING RICE COMPLEXATION PROTEIN ISOLATES SOY PROTEINS CEREAL PROTEINS BETANIN PARTICLE SIZE THERMAL STABILITY HYDROPHOBICITY RICE STRUCTURE HEATING
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