Abstract
In this study, extrusion was used to induce Maillard reaction between soy protein isolate (SPI) and oat β-glucan (OG) and effect of extrusion temperature (70, 90, 110 and 130°C) on the structure and emulsifying properties of extruded SPI-OG was investigated. SDS-PAGE and fluorescence spectroscopy provided evidence for the formation of SPI-OG conjugates during extrusion. The results showed that 90°C and 110°C extruded SPI-OG had the highest level of degree of glycosylation (were 14.34% and 13.70%, respectively, p>0.05). Structural analysis found that α-helix content of extruded SPI-OG decreased by 8.93-13.14% compared to mixture of SPI and OG. Meanwhile, extruded SPI-OG had lower protein solubility (29.83-34.38%) and surface hydrophobicity (1549-2027), larger average particle size (2363-4807nm) and higher emulsion stability (74.33-90.15%). Therefore, these findings may provide a theoretical basis for the development of novel food emulsion stabilizers.
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