倍半硅氧烷
谷胱甘肽
吸附
化学
蛋白质吸附
傅里叶变换红外光谱
氧化物
朗缪尔吸附模型
石墨烯
核化学
有机化学
材料科学
化学工程
酶
聚合物
纳米技术
工程类
作者
Jingqi Sun,Limin Jia,Xuwei Chen
出处
期刊:Molecules
[MDPI AG]
日期:2023-01-01
卷期号:28 (1): 340-340
被引量:1
标识
DOI:10.3390/molecules28010340
摘要
Glutathione S-transferases (GSTs) are important type-II detoxification enzymes that protect DNA and proteins from damage and are often used as protein tags for the expression of fusion proteins. In the present work, octa-aminopropyl caged polyhedral oligomeric silsesquioxane (OA–POSS) was prepared via acid-catalyzed hydrolysis of 3-aminopropyltriethoxysilane and polymerized on the surface of graphene oxide (GO) through an amidation reaction. Glutathione (GSH) was then modified to GO–POSS through a Michael addition reaction to obtain a GSH-functionalized GO–POSS composite (GPG). The structure and characteristics of the as-prepared GPG composite were characterized using scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (FT-IR), thermogravity analysis, and surface charge analysis. The specific binding interactions between glutathione and GST gave GPG favorable adsorption selectivity towards GST, and other proteins did not affect GST adsorption. The adsorption behavior of GST on the GPG composite conformed to the Langmuir isotherm model, and the adsorption capacity of GST was high up to 364.94 mg g−1 under optimal conditions. The GPG-based solid-phase adsorption process was applied to the extraction of GST from a crude enzyme solution of pig liver, and high-purity GST was obtained via SDS-PAGE identification.
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