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This study investigates the effects of heat treatment on the molecular interactions and co-aggregation behavior of pea protein fractions, specifically legumin, vicilin, and albumins. The findings reveal that legumin and vicilin aggregate independently due to electrostatic repulsion, while albumins promote co-aggregation through attractive interactions prior to heat treatment. The research provides insights into the complex aggregation behavior of pea proteins, which is crucial for their application in food

Author

tansj

Language

EN