College of Food Science & Technology, Shanghai Ocean University, Shanghai, 201306, China.
Plant Foods Hum Nutr. 2023 Sep;78(3):552-556. doi: 10.1007/s11130-023-01092-4. Epub 2023 Aug 18.
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.
美拉德反应（MR）与燕麦β-葡聚糖结合改变了大豆分离蛋白（SPI）的结构，进一步提高了其功能特性。MR 使 SPI 展开，鉴定到具有高分子量的 SPI 结合物。通过与亲水性β-葡聚糖交联，提高了 SPI 的水溶性，同时随着 SPI 的展开，疏水性也增加。与β-葡聚糖交联提高了 SPI 的粘度，从而增强了与粘度相关的生理活性，包括胆汁酸结合能力、脂肪结合能力和降血糖活性，并且随着 MR 中涉及的βG 含量的增加，功能特性也随之增加。
