Surface chemistry and spectroscopic studies of the native phenylalanine dehydrogenase Langmuir monolayer at the air/aqueous NaCl interface
Surface chemistry and spectroscopic studies of the native phenylalanine dehydrogenase Langmuir monolayer at the air/aqueous NaCl interface
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DOI：
10.1016/j.jcis.2019.10.086
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发表时间：
2020-02-15
影响因子：
9.9
通讯作者：
Leblanc, Roger M.
中科院分区：
文献类型：
--
作者：
Cruz Gomes da Silva, Rafael Leonardo;Sharma, Shiv K.;Leblanc, Roger M.
本研究考察了天然苯丙氨酸脱氢酶(PheDH)在空气/水界面的主要表面行为，采用盐水亚相诱导该酶的表面活性。表面化学实验是为了确定形成层的表面堆积和稳定性，而光谱实验提供了关于其二级结构构象的信息。研究发现，PheDH酶在整个压缩过程中形成一种流体膜，在整个压缩过程中相当均匀，在很长一段时间内都是稳定的，在界面压缩/减压过程中没有明显的聚集体或不可逆的结构域。通过原位反射-吸收红外光谱分析了PheDH膜的主要二级结构，表明在膜转移到固体白云母载体后，Oc-螺旋的存在是主要的。固定化薄膜沉积均匀、规则，粗糙度可控，平均厚度在8~10 nm之间。(C)2019 Elsevier Inc.保留所有权利。
This study investigates the main aspects of the surface behavior of the native phenylalanine dehydrogenase (PheDH) enzyme at the air/aqueous interface employing a saline subphase to induce the enzyme surface activity. Surface chemistry experiments were performed in order to determine the surface packing and stability of the formed layer, while spectroscopic experiments provided information regarding its secondary structure conformation. It was found that the PheDH enzyme forms a fluid film, which is quite homogeneous throughout its entire compression, being stable for long periods of time with no significant evidence of aggregates or irreversible domains during interfacial compression/decompression processes. The main secondary structures of the interfacial PheDH film were accessed via in situ reflectance-absorbance infrared spectroscopy, indicating a majority presence of oc-helices, which were maintained after the film transfer to solid muscovite supports. The immobilized films presented a homogeneous and regular deposition, with controlled roughness and a mean thickness in the range of 8-10 nm. (C) 2019 Elsevier Inc. All rights reserved.