食品科学

• 基础研究 • 上一篇    下一篇

水牛奶酪蛋白胶束结构的荧光光谱研究

杨同香1,2,陈俊亮1,吴孔阳3,李全阳2,李智丽1,康怀彬1   

  1. 1.河南科技大学食品与生物工程学院,河南 洛阳 471023;2.广西大学轻工与食品工程学院,广西 南宁 530004;
    3.洛阳师范学院生命科学学院,河南 洛阳 471022
  • 发布日期:2014-12-15

Structure of Casein Micelles from Buffalo Milk Determined by Fluorescence Spectroscopy

YANG Tong-xiang1,2, CHEN Jun-liang1, WU Kong-yang3, LI Quan-yang2, LI Zhi-li1, KANG Huai-bin1   

  1. 1. College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471023, China;
    2. Institute of Light Industry and Food Engineering, Guangxi University, Nanning 530004, China;
    3. College of Life Science, Luoyang Normal University, Luoyang 471022, China
  • Published:2014-12-15

摘要:

利用内源荧光团色氨酸(Trp)和外源荧光探针8-苯胺基-1-萘磺酸(8-anilino-1-naphthalenesulfonic acid,ANS)的荧光特性对水牛奶酪蛋白胶束结构进行研究。结果表明:当蛋白质质量浓度较低时,酪蛋白胶束结构变化不明显,而较高的蛋白质质量浓度会破坏其胶束结构,使其疏水基团暴露;此外,在离子强度较大、pH值较低条件下,对酪蛋白胶束结构影响较大,使酪蛋白疏水基团暴露,酪蛋白微球先膨胀后聚集并形成酪蛋白胶束。

关键词: 酪蛋白, 胶束结构, 荧光光谱

Abstract:

The structure of casein micelles from buffalo milk was analyzed by fluorescence spectroscopy with the extrinsic
fluorescent probe 8-anilino-1-naphthalenesulfonic acid (ANS) and the intrinsic fluorophore tryptophan (Trp). The results
showed that the effect of buffalo milk protein at low concentration on the structure of casein micelles was obvious. As the
structure of casein micelles was broken, the hydrophobic groups were exposed to the solvent with high protein concentration.
In addition, the structure of casein micelles was influenced evidently at higher ionic strength and lower pH level, which could
cause exposure of hydrophobic groups of casein to the solvent so that the casein micelles could be formed by the expansion
and aggregation of casein microspheres.

Key words: casein, micelles structure, fluorescence spectroscopy

中图分类号: