College of Food Science, South China Agricultural University, Guangzhou 510642, China.
College of Food Science, South China Agricultural University, Guangzhou 510642, China.
Food Chem. 2019 Sep 30;293:455-462. doi: 10.1016/j.foodchem.2019.05.016. Epub 2019 May 3.
To explore the protein surface properties treated by Pulsed Electric Field (PEF) with metal ions, we employed ovalbumin as the object and added three divalent metal ions (Ca, Cu and Ba), respectively. The changes in surface hydrophobicity and surface tension were evaluated. Raman, FTIR, and fluorescence were used to record their structure variations. The results show that the surface hydrophobicity and surface tension of ovalbumin increased with the adding of metal ions. It was caused by the burial of some hydrophobic residues and variation of hydrophobic interaction between molecules, which was consistent with the results of spectra. With the combination of metal ions and PEF, the surface hydrophobicity and surface tension of ovalbumin showed an enhanced trend at first and then reduced with pulse time. These results demonstrate that metal ions and PEF have crucial influences on surface properties, that might afford a theoretical basis for the production and application of ovalbumin.
为了研究脉冲电场（PEF）处理与金属离子相互作用的蛋白质表面特性，我们以卵清蛋白为对象，分别添加三种二价金属离子（Ca、Cu 和 Ba）。评估表面疏水性和表面张力的变化。使用拉曼、FTIR 和荧光记录它们的结构变化。结果表明，随着金属离子的加入，卵清蛋白的表面疏水性和表面张力增加。这是由于一些疏水性残基的埋藏和分子间疏水相互作用的变化所致，这与光谱结果一致。随着金属离子和 PEF 的结合，卵清蛋白的表面疏水性和表面张力先增加后随脉冲时间减少。这些结果表明，金属离子和 PEF 对表面性质有重要影响，这可能为卵清蛋白的生产和应用提供理论依据。
