Functional properties and structural changes of rice proteins with anthocyanins complexation.
Ting Li1, Li Wang1, Zhengxing Chen1
1Key Laboratory of Carbohydrate Chemistry and Biotechnology Ministry of Education, Jiangnan University, Lihu Road 1800, Wuxi 214122, China; National Engineering Laboratory for Cereal Fermentation Technology, School of Food Science and Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China; Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China.
Food Chemistry
|June 23, 2020
Summary
Rice protein (RP) complexed with anthocyanins (ACN) shows altered structure and enhanced antioxidant capacity. These RP-ACN particles exhibit optimal functional properties at pH 3, suggesting potential for health benefits.
Area of Science:
- Food Science
- Biochemistry
- Materials Science
Background:
- Proteins and anthocyanins are key components in food systems.
- Understanding their interactions is crucial for developing functional food ingredients.
- Rice protein (RP) and anthocyanins (ACN) are natural compounds with potential health benefits.
Purpose of the Study:
- To investigate the structural and functional changes in rice protein upon complexation with anthocyanins.
- To analyze the properties of RP-anthocyanin complexes and their isolated fractions.
- To determine the optimal conditions for RP-ACN complex formation and stability.
Main Methods:
- Complexation of rice protein with anthocyanins.
- Fractionation of RP-ACN complexes (albumin, globulin, prolamin, glutelin).
- Structural analysis using spectroscopy (FTIR, fluorescence).
- Functional property assessment at varying pH levels.
Main Results:
- Complexation induced structural changes in RP, including increased β-sheet content and spectral shifts.
- Hydrophobic and hydrogen bonds were identified as primary forces in RP-ACN complex formation.
- RP-ACN particles demonstrated optimal functional properties and enhanced antioxidant activity at pH 3.
- Conformational changes at pH 3 were linked to improved particle functionality.
Conclusions:
- RP-ACN complexation significantly modifies protein structure and enhances antioxidant properties.
- The optimal pH for RP-ACN particle functionality is 3, driven by specific conformational changes.
- These engineered RP-ACN particles show promise for stabilizing food-grade mesostructures like foams and emulsions, offering potential health advantages.
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