Adsorption kinetics and dilatational rheological properties of recombinant Pea Albumin-2 at the oil-water interface
Adsorption kinetics and dilatational rheological properties of recombinant Pea Albumin-2 at the oil-water interface
复制标题
重组豌豆白蛋白2在油水界面的吸附动力学和膨胀流变特性
DOI：
10.1016/j.foodhyd.2021.106866
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发表时间：
2021-05-29
影响因子：
10.7
通讯作者：
Chen, Yijie
中科院分区：
文献类型：
--
作者：
Luo, Yilun;Zheng, Wei;Chen, Yijie
为了研究豌豆白蛋白-2 (PA-2) 在油水界面的吸附动力学和膨胀流变特性，表达并纯化了重组 PA-2。我们的天然 PAGE、SDS-PAGE 和同源建模结果表明 PA-2（一种球状蛋白）可以通过非共价相互作用而不是二硫键形成二聚体。 TEM结果显示，部分PA-2蛋白可形成2-3μm左右的聚集体。与其他球状蛋白不同，PA-2 表现出动态粘弹性模量 (E) 的非单调动力学依赖性。此外，PA-2的重排率（kR）显着高于其他典型食品蛋白。我们的结果表明 PA-2 可以以聚集体的形式吸附到油水界面上。 2-ME（β-巯基乙醇）的添加会影响 PA-2 的膨胀流变特性，导致 PA-2 蛋白聚集体在油水界面发生解聚和更高程度的重排。我们的数据提供了有关球状蛋白界面动态特性的更多信息，并基于球状蛋白的动态粘弹性行为，为油水界面处球状蛋白的构象变化提供了新的见解。
To investigate the adsorption kinetics and dilatational rheological properties of Pea Albumin-2 (PA-2) at the oilwater interface, recombinant PA-2 was expressed and purified. Our native-PAGE, SDS-PAGE, and homology modeling results indicated that PA-2, a kind of globular protein, could form dimers by non-covalent interactions rather than disulfide bonds. The TEM results showed that some PA-2 proteins could form aggregates with the size of around 2-3 mu m. Unlike other globular proteins, PA-2 exhibited the non-monotonic kinetic dependency of the dynamic viscoelastic modulus (E). Besides, the rate of rearrangement (kR) of PA-2 was significantly higher than that of other typical food proteins. Our results demonstrated that PA-2 could adsorb to the oil-water interface in the form of aggregates. The addition of 2-ME (beta-mercaptoethanol) would impact dilatational rheological properties of PA-2, leading to disaggregation and higher rearrangement of PA-2 protein aggregates at the oil-water interface. Our data offered more information on the interfacial dynamic properties of globular proteins, and provided a new insight to the conformational changes of globular proteins at the oil-water interface, basing on their dynamic viscoelastic behaviors.