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| Effect of extrusion temperature on antigenicity and structure of soybean protein isolate |
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| DOI：10.19902/j.cnki.zgyz.1003-7969.230260 |
| KeyWord:soybean protein isolate extrusion antigenicity protein structure |
| FundProject:河南省自然科学基金面上项目（242300421317）；国家自然科学基金项目（32472289，31871748）；河南省高等学校青年骨干教师培养计划（2019GGJS084）；河南工业大学青年骨干教师培育计划（21420064）；郑州市科技协同创新专项（21ZZXTCX17）；中国博士后科学基金面上项目（2021M701112）；河南工业大学创新基金支持计划专项资助（2021ZKCJ03） |
| Author Name | Affiliation | | CHANG Yongfeng1, CHEN Yixuan1, BU Guanhao1, GAO Xueli2,
ZHAO Qingqing1, LUO Qiong1 | （1.College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China
2.School of Food and Pharmacy, Xuchang University, Xuchang 461000, Henan, China) |
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| Abstract: |
| In order to provide reference for the development of desensitization technology of soybean protein, the antigenicity, SDS-PAGE, amino acid composition, solubility, UV absorption spectra, endogenous fluorescence spectra and surface hydrophobicity of the soybean protein isolate (SPI) extruded at different extrusion temperatures. The results showed that the antigenicity of SPI decreased first and then increased with the increase of extrusion temperature, and the antigenicity of SPI decreased most significantly at 145 ℃. The α, α′ and β subunits of the antigen protein β-conglycinin and the acidic and basic subunits of glycinin in SPI were significantly degraded. The amino acid composition and the ratio of essential amino acids to total amino acids of SPI had no obvious change, and the nutritional characteristics of SPI remained good. After extrusion, the solubility of SPI decreased, and hydrogen bond, disulfide bond and hydrophobic interaction were the molecular forces that maintained SPI spatial structure, in which hydrogen bond played the main role. The UV and endogenous fluorescence spectra of SPI extruded showed different degrees of redshift, the UV absorption intensity and fluorescence intensity changed, the surface hydrophobicity decreased significantly, and the tertiary structure of SPI changed. In conclusion, extrusion can reduce the antigenicity of SPI to a certain extent and affect its spatial structure. |
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