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• W2344604799 abstract "Lysine adsorption at clay/aqueous interfaces plays an important role in the mobility, bioavailability, and degradation of amino acids in the environment. Knowledge of these interfacial interactions facilitates our full understanding of the fate and transport of amino acids. Here, X-ray diffraction (XRD) and attenuated total reflectance Fourier-transform infrared spectroscopy (ATR-FTIR) measurements were used to explore the dynamic process of lysine adsorption on montmorillonite and the competition with Ca2+ at the molecular level. Density functional theory (DFT) calculations were employed to determine the peak assignments of dissolved lysine in the solution phase. Three surface complexes, including dicationic, cationic, and zwitterionic structures, were observed to attach to the clay edge sites and penetrate the interlayer space. The increased surface coverage and Ca2+ competition did not affect the interfacial lysine structures at a certain pH, whereas an elevated lysine concentration contributed to zwitterionic-type coordination at pH 10. Moreover, clay dissolution at pH 4 could be inhibited at a higher surface coverage with 5 and 10 mM lysine, whereas the inhibition effect was inconspicuous or undetected at pH 7 and 10. The presence of Ca2+ not only could remove a part of the adsorbed lysine but also could facilitate the readsorption of dissolved Si4+ and Al3+ and surface protonation. Our results provide new insights into the process of lysine adsorption and its effects on montmorillonite surface sites." @default.
• W2344604799 created "2016-06-24" @default.
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• W2344604799 date "2016-05-04" @default.
• W2344604799 modified "2023-10-02" @default.
• W2344604799 title "Adsorption of Lysine on Na-Montmorillonite and Competition with Ca²⁺: A Combined XRD and ATR-FTIR Study" @default.
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• W2344604799 doi "https://doi.org/10.1021/acs.langmuir.6b00563" @default.
• W2344604799 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27118104" @default.
• W2344604799 hasPublicationYear "2016" @default.
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