Abstract
Maillard reaction (MR) with oat β-glucan changed the structure of soybean protein isolate (SPI), further leading to the enhancement of its functional properties. SPI was unfolded by MR, and the SPI conjugates with high molecular weight were identified. The water solubility of SPI was improved by cross-linking with hydrophilic β-glucan, while the hydrophobicity also increased along with the unfolding of the SPI. Cross-linking with β-glucan elevated the viscosity of SPI, thus enhancing viscosity-related physiological activities, including bile acid binding ability, fat binding capacity, and hypoglycemic activity, and the functional properties increased as the βG content involved in MR increased.
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