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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The Natural Science Foundation of China supported this study (fund number: 31972142 and 31571914).
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Zhaonan Chu, Qiyun Zhang: Conceptualization, Data curation, Writing-Original draft preparation. Tao Sun: Writing-Reviewing and Editing. Xiaohui Li: Resources. Bin Xue: Validation. Jing Xie: Funding acquisition.
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Chu, Z., Zhang, Q., Li, X. et al. Effect of Oat β-Glucan on the Structure and Properties of Soybean Protein Isolate During Maillard Reaction. Plant Foods Hum Nutr 78, 552–556 (2023). https://doi.org/10.1007/s11130-023-01092-4
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DOI: https://doi.org/10.1007/s11130-023-01092-4