食品科学 ›› 2020, Vol. 41 ›› Issue (19): 146-153.doi: 10.7506/spkx1002-6630-20190929-344

• 食品工程 • 上一篇    下一篇

高压均质对大豆分离蛋白-大豆异黄酮相互作用及其复合物功能性质的影响

王娜,吴长玲,陈凡凡,李杨,滕飞   

  1. (东北农业大学食品学院,黑龙江?哈尔滨 150030)
  • 出版日期:2020-10-15 发布日期:2020-10-23
  • 基金资助:
    黑龙江省创新人才项目(UNPYSCT-2017015);黑龙江省自然科学基金联合引导项目(LH2020C028); 黑龙江省自然科学基金杰出青年基金项目(JC2018009);“十三五”国家重点研发计划重点专项(2017YFD0400200)

Effect of High Pressure Homogenization on Soybean Protein Isolate-Soybean Isoflavone Interaction and Functional Properties of Their Complex

WANG Na, WU Changling, CHEN Fanfan, LI Yang, TENG Fei   

  1. (School of Food Science, Northeast Agricultural University, Harbin 150030, China)
  • Online:2020-10-15 Published:2020-10-23

摘要: 为探明高压均质处理对大豆分离蛋白(soybean protein isolate,SPI)和大豆异黄酮(soy isoflavone,SI)之间相互作用及其复合物功能性质的影响,并确定最佳处理条件,本实验研究10 mg/mL SPI分别与0、0.2、2 mg/mL SI所形成复合物的结构和功能特性随均质压力条件变化的规律。采用紫外光谱、荧光光谱和傅里叶变换红外光谱(Fourier transform infrared spectrometer,FTIR)分析不同均质条件下复合物构象变化,以粒径、Zeta电位、溶解度和疏水性表征不同均质条件下复合物的流体动力学半径和功能特性。荧光光谱结果表明SI对SPI的荧光猝灭机制为静态猝灭。在压力为80 MPa、SI质量浓度为0.2 mg/mL时,粒径分布稳定,Zeta电位绝对值、溶解度、疏水性均显著提高(P<0.05)。紫外光谱和FTIR结果表明SPI中色氨酸残基附近的微环境亲水性增强,SPI二级结构发生改变。

关键词: 大豆分离蛋白;大豆异黄酮;高压均质;结构性质;功能性质

Abstract: In order to find out the effect of high pressure homogenization on the interaction between soybean protein isolate (SPI) and soybean isoflavone (SI) and the functional properties of their complexes and to determine the best treatment conditions, complexation between 10 mg/mL SPI and 0, 0.2 or 2 mg/mL SI was triggered using different homogenization pressures. The conformational differences among the resulting composites were analyzed by ultraviolet spectroscopy (UVS), fluorescence spectroscopy (FS) and Fourier transform infrared spectroscopy (FTIR). Their hydrodynamic radius and functional properties were characterized by their particle size, zeta potential, solubility and hydrophobicity. The results showed that the fluorescence quenching of SPI by SI was static as evaluated by FTIR. When the pressure was 80 MPa and the SI concentration was 0.2 mg/mL, the particle size distribution was stable, and the absolute value of zeta potential, solubility, and hydrophobicity were remarkably improved (P < 0.05). UVS and FTIR indicated that the microenvironment near tryptophan residues in SPI was more hydrophilic and the secondary structure of SPI was changed.

Key words: soybean protein isolate; soybean isoflavone; high pressure homogenization; structural properties; functional properties

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