S-构型转化对卵白蛋白微观结构的影响

采用圆二色谱(CD)、X射线衍射(XRD)、ANS荧光探针和紫外光谱(UV)研究了S-构型转化对卵白蛋白微观结构的影响.结果显示,不同诱导时间处理的卵白蛋白二级结构的α-螺旋,β-折叠,β-转角和无规卷曲之间相互转化,α-螺旋略有减少,β-折叠相应增加,分子有序性提高;S-构型转化后卵白蛋白晶体结构增加,72 h处理后...

Effect of S-configuration transformation on the microstructure of ovalbumin

The effect of S-configuration transformation on the microstructure of ovalbumin was studied by CD spectra, XRD spectra, ANS fluorescence probe emission spectra and UV absorption spectra. CD spectra was used to examine the changes in the secondary structure of the ovalbumin during S-ovalbumin information process. When the induction time was prolonged, the mutual transformation between alpha-helix, beta-sheet, beta-turn and the random coil was observed, and the orderliness of the secondary structure was increased with alpha-helix decreasing slightly and beta-sheet increasing correspondingly. XRD spectra analysis showed that the crystal structure content of the ovalbumin increased with prolonging the induction time and the largest data was observed at 72 h, indicating that the orderliness of the secondary structure was increased. The results were similar to CD spectra analysis. The ANS fluorescence probe emission spectra analysis demonstrated that S-configuration transformation induced an increase in surface hydrophobicity with prolonging the induction time, and the largest data was also observed at 72 h. In addition, UV absorption spectra analysis indicated that S-configuration transformation resulted in a decrease in the UV-absorption maximum value with prolonging the induction time, indicating that the aromatic amino acid was buried in the molecular interior. The results indicated that the changes in the microstructure of ovalbumin were relevant to S-configuration transformation.