Effects of Baking on the Structure and Functional Properties of Mung Bean Protein

Using mung beans as raw materials. In this paper,the structure and functional properties of mung bean protein extracted at different temperatures were determined. The total protein in mung bean was extracted by alkaline method,and the secondary structure and various functional properties of the protein were analyzed. The research results showed that when the baking temperature increasing,all the properties except the emulsification stability were significantly(P<0.05)improved. The emulsification was up to 38.46 m²/g. The foamability at 180 ℃ was up to 26%. The solubility increased by 47.72%. And the emulsion stability was significantly reduced. In comparison,mung bean protein had the best functional properties at 180 ℃. In the electrophoretic analysis,the roasting process causes various parts of mung bean protein to degrade in varying degrees. All the bands became shallow,and bands I,IV,and V almost disappeared. At 180 ℃,the deepening of the color of article Ⅱ subunit bands echoes the enhancement of functional properties at 180 ℃. By measuring Fourier infrared spectroscopy,it was found that the peaks at 1640 cm^-1 showed red shifts at 110 and 180 ℃,respectively. At other temperatures,the peaks of the protein showed blue shifts compared to the raw protein. At 150 and 180 ℃ protein maps,there are obvious peaks at 1050 cm^-1 wavelength. From the perspective of protein functional maintenance and regulation after thermal processing. After baking,the contents of β-folding structure increased significantly,while that of α-helix structure and β-angle structure decreased significantly. In conclusion,after high temperature baking,the structure of mung bean protein would change,and the basic functional properties would be more excellent. The baking strength at 180 ℃ for 20 min could improve the functional properties of mung bean protein to the optimal level.