Exfoliation of montmorillonite in protein solutions

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• 作者：Krzysztof Kolman^a ; ^b ; Werner Steffen^a ; Gabriela Bugla-P艂osko艅ska^c ; Aleksandra Skwara^c ; Jacek Pig艂owski^b ; Hans-Jü ; rgen Butt^a ; Adam Kiersnowski^a ; ^b ; ^{kiersnow@mpip-mainz.mpg.de} ; ^{adam.kiersnowski@pwr.wroc.pl}
• 关键词：Montmorillonite ; Exfoliation ; Nanoparticles ; Proteins ; Adsorption ; TEM ; DLS ; Bionanocomposites
• 刊名：Journal of Colloid and Interface Science
• 出版年：2012
• 期刊代码：125_00219797
• 类别：ch
• 出版时间：15 May, 2012
• 卷：374
• 期：1
• 页码：135-140
• 文件大小：717 K

摘要

In the study we demonstrate a method to obtain stable, exfoliated montmorillonite-protein complexes by adsorption of the proteins extracted from hen-egg albumen. Analysis of the process by means of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) revealed that the complexes are formed by sequential adsorption of ovotransferrin, ovalbumins, ovomucoid and lysozyme on the surface of the silicate. Structural studies performed by X-ray diffraction (XRD) and transmission electron microscopy (TEM) indicated that the adsorption of ovotransferrin and albumins is accompanied by disintegration of clay stacks into discrete platelets. Further analysis by dynamic light scattering (DLS) revealed that at protein to silicate weight ratios exceeding 20, the synergistic adsorption of albumen components leads to reaggregation of silicate platelets into disordered, microgel-like particles. By means of DLS it was found that exfoliation predominantly leads to formation of particles with average hydrodynamic radii (R_h) of 0.19 渭m while their aggregation causes formation of particles having R_h in of approx. 0.5 渭m and larger.