Noskov Boris, Loglio Giuseppe, Miller Reinhard, Milyaeva Olga, Panaeva Maria, Bykov Alexey
Institute of Chemistry, St. Petersburg State University, Universitetsky pr. 26, St. Petersburg 198504, Russia.
Institute of Condensed Matter Chemistry and Technologies for Energy, 16149 Genoa, Italy.
Polymers (Basel). 2023 Oct 2;15(19):3970. doi: 10.3390/polym15193970.
The dynamic surface properties of aqueous dispersions of α-lactalbumin (ALA) amyloid fibrils differ noticeably from the properties of the fibril dispersions of other globular proteins. As a result, the protocol of the application of ALA fibrils to form stable foams and emulsions has to be deviate from that of other protein fibrils. Unlike the fibrils of β-lactoglobulin and lysozyme, ALA fibrils can be easily purified from hydrolyzed peptides and native protein molecules. The application of the oscillating barrier method shows that the dynamic surface elasticity of ALA fibril dispersions exceeds the surface elasticity of native protein solutions at pH 2. ALA fibrils proved to be stable at this pH, but the stability breaks at higher pH levels when the fibrils start to release small peptides of high surface activity. As a result, the dynamic surface properties of ALA coincide with those of native protein solutions. The ionic strength strongly influences the adsorption kinetics of both fibril dispersions and native protein solutions but have almost no impact on the structure of the adsorption layers.
α-乳白蛋白（ALA）淀粉样原纤维水分散体的动态表面性质与其他球状蛋白质原纤维分散体的性质明显不同。因此，应用ALA原纤维形成稳定泡沫和乳液的方案必须不同于其他蛋白质原纤维的方案。与β-乳球蛋白和溶菌酶的原纤维不同，ALA原纤维可以很容易地从水解肽和天然蛋白质分子中纯化出来。振荡屏障法的应用表明，在pH 2时，ALA原纤维分散体的动态表面弹性超过天然蛋白质溶液的表面弹性。ALA原纤维在该pH值下被证明是稳定的，但在较高pH值时稳定性会被打破，此时原纤维开始释放具有高表面活性的小肽。结果，ALA的动态表面性质与天然蛋白质溶液的性质一致。离子强度强烈影响原纤维分散体和天然蛋白质溶液的吸附动力学，但对吸附层的结构几乎没有影响。
