Effects of Storage Methods on the Structure and Solubility of Mung Bean Globulin
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Graphical Abstract
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Abstract
In order to clarify the influence of different storage methods on the protein structure and solubility of mung beans, fresh mung beans and mung beans stored in a gas package at room temperature and 4 °C for 18 months were used as raw materials. Fourier infrared spectroscopy, DTNB colorimetric method and Folin method were used. The investigation found that the maximum α-helical structure of mung bean globulin increased by 4.73%, the maximum sulfhydryl content decreased by 0.00487, the maximum surface hydrophobicity decreased by 20.78667, and the maximum disulfide bond content increased by 0.00177 at room temperature. At 4 °C, the α-helix structure of mungbean globulin increased by 1.65%, the sulfhydryl content decreased by 0.00174, the surface hydrophobicity decreased by 5.48667, and the disulfide bond content increased by 0.00048. The solubility of mung bean globulin decreased after storage, and different storage methods have different changes. The structure and solubility of mung bean globulin after storage at room temperature were significantly different from that of fresh mung bean globulin (P>0.05), while the structure and solubility of mung bean globulin after storage at 4 °C were not significantly different from that of fresh mung bean (P<0.05). It showed that 4 ℃ and controlled atmosphere storage could reduce the changes of mung bean globulin structure and solubility, so as to better maintain its quality.
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