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Interaction of rice glutelin with soybean 7S globulin formed co-assemblies with improved functional properties
Yang Yang1, Ming-Qian Wu1, Peng-Yu Zhu2
1College of Food Engineering, Harbin University of Commerce, Harbin 150076, China.
Abstract:
Rice protein (RP) molecules tend to aggregate, limiting their functional properties and posing a significant challenge to the intensive processing of rice products. This study explored the interaction between soybean 7S globulin (7S) and rice glutelin (RG) to improve the structure and properties of RP. The results show that the tertiary structure of the RG-7S co-assemblies undergoes a certain degree of extension, increases the α-helix content, and reduces the β-sheet content in the secondary structure. Molecular dynamics provide further verification that hydrogen bonding and hydrophobic interactions are the main drivers of these conformational changes. When the RG-7S ratio was 1:1.500 (g/g), the solubility increased 20-fold, and the emulsifying activity index and foaming capacity increased by 3.33 and 1.89 times, respectively. This study confirms that 7S co-assembly with RG enhances the functional properties of RG, demonstrating the potential of this strategy for application in the food industry.
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