静电场辅助冷冻对面筋蛋白品质及分子结构的影响

本文研究了静电场辅助冷冻对面筋蛋白流变特性和热特性的影响，并通过分析其分子结构及离子键、氢键、疏水相互作用和二硫键的结果，探究静电场辅助冷冻对面筋蛋白品质的改善作用。结果表明，与对照（传统冷冻方式）相比，静电场辅助冷冻提高了面筋蛋白的黏弹特性、变性温度（Tp）和变性焓（?H）。化学作用力的分析表明，氢键的含量呈先降低后增加的趋势，而离子键、氢键和疏水相互作用的变化则与之相反。600 V电压静电场处理后，面筋蛋白的二级结构及二硫键的构型分布更加均匀，且?-螺旋的含量增加，二硫键构型中g-g-g构型的含量增加。扫描电镜分析表明，施加300 V和600 V的静电场后，面筋蛋白的网络结构具有更小的孔隙且分布均匀。

The effect of electrostatic field-assisted freezing on the quality and molecular structure of gluten protein

The effect of electrostatic field-assisted freezing on the gluten protein rheological properties and thermal properties were investigated in this paper. And the molecular structure, the contents of disulfide bonds, ionic bonds, hydrogen bonds, and hydrophobic of the gluten protein was analyzed to explore the improvement effect of electrostatic field assisted freezing on the quality of gluten protein. The results showed that electrostatic field assisted freezing improved the viscoelasticity, the denaturation temperature (Tp) and denaturation enthalpy (?H) of gluten protein compared with the control (traditional freezing method). The analysis of chemical interaction revealed that the content of hydrogen bond decreased first and then increased, while the changes of ionic bond, hydrogen bond and hydrophobic interaction had an opposite tendency. The imaging results of the laser confocal micro-Raman spectrometer indicated that the distribution of secondary structure and the configurations of disulfide bond in the gluten protein became more uniform, and the content of ?-helix and g-g-g configuration increased with the 600 V voltage electrostatic field treatment. SEM image analysis showed that the network structure of gluten protein has smaller pores and distributed evenly under the 300 V and 600 V voltage electrostatic fields.