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Enhancement of Dissolution Rates of Amorphous Silica by Interaction with Bovine Serum Albumin at Different pH Conditions

Published online by Cambridge University Press:  01 January 2024

Motoharu Kawano  and
Jinyeon Hwang
Motoharu Kawano*
Affiliation:
Graduate School of Science and Engineering, Kagoshima University, 1-21-35 Korimoto, Kagoshima 890-0065, Japan
Jinyeon Hwang
Affiliation:
Division of Earth Environmental System, Pusan National University, Busan 609-735, Korea
*
* E-mail address of corresponding author: kawano@sci.kagoshima-u.ac.jp
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Abstract

Proteins and protein-like molecules are abundant in various geochemical environments; they form complexes with mineral surfaces and with dissolved organic matter. To evaluate the effect of proteins on rates of dissolution of minerals, experiments on the dissolution of amorphous silica in solutions containing various concentrations of bovine serum albumin (BSA) were performed in this study. The dissolution experiments were carried out by a batch method using solutions of 0.1 mM NaCl with 0.00, 0.05, 0.1, 0.2, 0.5, and 1.0 mg/mL of BSA at three different pH conditions, 6, 5, and 4. The results of the experiments demonstrated that BSA exhibited strong rate-enhancement effects on the dissolution of amorphous silica and were dependent on BSA concentration and the solution pH. At pH 6, the dissolution rates of amorphous silica appeared to increase successively by ~1.6, 2.2, 2.4, 2.5, and 2.9 times with increasing BSA concentrations of 0.05, 0.1, 0.2, 0.5, and 1.0 mg/mL, respectively. The rates of dissolution increased by greater degrees, ~3.1–5.8 and 4.9–13.0 times at pH 5 and 4, respectively. According to the calculated charge distributions of amino acid residues of the BSA molecule, the dissolution rates of amorphous silica were likely to be enhanced by attractive electrostatic interactions of the positively charged side chains of lysine, arginine, and histidine residues with the negatively charged >SiO− sites on the amorphous silica surface. The negatively charged side chains such as glutamic acid and aspartic acid residues may inhibit the attractive interaction, depending on the degree of deprotonation.

Keywords

Amorphous SilicaBovine Serum AlbuminDissolution RatesProteinSide Chain
Type
Article
Information
Clays and Clay Minerals , Volume 58 , Issue 2 , April 2010 , pp. 272 - 279
Copyright
Copyright © Clays and Clay Minerals 2010

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