大豆蛋白
共价键
化学
圆二色性
没食子酸
化学改性
奶油
蛋白质二级结构
没食子酸表没食子酸酯
乳状液
多酚
食品科学
有机化学
生物化学
核化学
抗氧化剂
作者
Fei Tao,Jiang He,Wenwei Chen,Yongyong Zhang,Pan Jia-rong,Jiaxin Jiang,Zhenbao Jia
摘要
Soy protein isolate (SPI) has promising applications in various food products because of its excellent functional properties and nutritional quality. The structural and emulsifying properties of covalently modified SPI by (-)-epigallocatechin-3-gallate (EGCG) were investigated.SPI was covalently modified by EGCG under alkaline conditions. SDS-PAGE analysis revealed that EGCG modification caused crosslinking of SPI proteins. Circular dichroism spectra demonstrated that the secondary structure of SPI proteins was changed by EGCG modification. In addition, the modifications resulted in the perturbation of the tertiary structure of SPI as evidenced by intrinsic fluorescence spectra and surface hydrophobicity measurements. Oil-in-water emulsions of modified SPI had smaller droplet sizes and better creaming stability compared to those from unmodified SPI.The covalent modification by EGCG improved the emulsifying property of SPI. This study therefore provided an innovative approach for improving the emulsifying properties of proteins. © 2018 Society of Chemical Industry.
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