Interfacial behavior of Proteinase K enzyme at air-saline subphase
Interfacial behavior of Proteinase K enzyme at air-saline subphase
复制标题
蛋白酶 K 在空气-盐水亚相的界面行为
DOI：
10.1016/j.jcis.2022.02.084
复制
发表时间：
2022
影响因子：
9.9
通讯作者：
Leblanc, Roger M.
中科院分区：
文献类型：
--
作者：
Paudyal, Suraj;Sigdel, Ganesh;Shah, Sujit K;Sharma, Shiv K.;Grubb, John D.;Micic, Miodrag;Caseli, Luciano;Leblanc, Roger M.
研究了蛋白酶K酶在空气-水界面的界面行为。用生理盐水亚相诱导酶在表面吸附。采用表面压力-面积π-A和表面电位-面积ΔV-A等温线考察了酶的表面堆积和稳定性。蛋白酶K酶在气-水界面形成膜，并通过压缩-减压循环实验显示出良好的稳定性。为了表征界面酶的表面组装形态，采用了紫外-可见和荧光光谱技术。结果表明，Langmuir酶单分子层具有良好的均匀性，压缩过程中无聚集现象。利用p偏振红外反射吸收光谱测定了酶在界面处的二级结构为α-螺旋结构。通过Langmuir-Blodgett （LB）膜的圆二色光谱证实了这一点，表明存在的主要构象是α-螺旋。
This study investigates the interfacial behavior of the proteinase K enzyme at air–water interface. Adsorption of enzyme on the surface was induced using saline subphase. The surface packing and stability of the enzyme was investigated using of surface pressure-area (π-A) and surface potential-area (ΔV-A) isotherms. Proteinase K enzyme forms film at air-aqueous interface and demonstrates good stability as shown through compression-decompression cycle experiments. To characterize the surface assembly morphology of the interfacial enzymes UV–vis and fluorescence spectroscopic techniques were used. The data revealed that the enzyme Langmuir monolayer has good homogeneity with no evidence of aggregates during compression. The secondary structure of the enzyme at interface was determined to be α-helix using p-polarized infrared-reflection absorption spectroscopy. This was confirmed through Circular dichroism spectra of the enzyme Langmuir-Blodgett (LB) film which showed that the major conformation present were α-helices.