pH对水酶法大豆乳状液稳定性影响的机理研究
Mechanism of effect of pH on stability of aqueous enzyme soybean emulsion
  
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中文关键词:  乳状液  水酶法  pH  稳定性  机理
英文关键词:emulsion  aqueous enzymatic method  pH  stability  mechanism
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HU Miao, QI Baokun, XIE Fengying,etc  
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中文摘要:
      以水酶法大豆乳状液为研究对象,通过激光共聚焦、红外光谱、荧光光谱等手段研究pH对水酶法乳状液粒径、Zeta电位、微观结构及其中蛋白质性质的影响,研究pH对乳状液稳定性影响的机理。结果表明:随着乳状液pH的增加(2~10),乳状液的Zeta电位显著降低,且当pH为4.5~4.7范围内时乳状液的Zeta电位接近0;当pH在蛋白质等电点附近,乳状液的粒径最大,乳状液中蛋白质的表面疏水性最低,相对分子质量最大,荧光强度最低,三级结构更加松散,二级结构中有序的α-螺旋含量最低,而无规卷曲含量最高。表明pH在蛋白质等电点附近时,乳状液是最不稳定的,在此环境下更容易破除乳状液。
英文摘要:
      With aqueous enzymatic soybean emulsion as material, the effects of pH on the particle size, Zeta potential and microstructure of emulsion and properties of protein in emulsion were studied by laser confocal microscopy, infrared spectroscopy and fluorescence spectroscopy to explore the mechanism of effect of pH on stability of emulsion. The results showed that with the increase of emulsion pH from 2 to 10, the Zeta potential of the emulsion significantly reduced, and approached to zero when the pH was in the range of 4.5-4.7. When the pH was near the isoelectric point of the protein, the particle size of emulsion was the largest, and the surface hydrophobicity of the protein in the emulsion was the lowest with the largest relative molecular weight, the lowest fluorescence intensity, more loose tertiary structure, the lowest ordered α-helix content and the highest random coil content in the secondary structure. So when pH was near the isoelectric point, the emulsion was the most unstable and easier to be broken.
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