| Abstract: | The adsorption and desorption of proteins and polyamino acids on illite, montmorillonite, goethite, and marine sediments was investigated. Three 14C-labeled hydrophilic proteins, Rubisco from C. reinhardtii, and GroEL and GroES from genetically modified Escherichia coli, were synthesized and purified for this study. The proteins were strongly and rapidly adsorbed by the clay minerals and marine sediments, and much of the adsorbed protein was not readily desorbed. Sodium dodecyl sulfate (SDS) extraction and separation by SDS-polyacrylamide gel electrophoresis (PAGE) and sucrose density gradients showed that Rubisco and GroEL were adsorbed on illite and sediments in their original forms. The apparent adsorption partition coefficients of the proteins were on the order of 102 l/kg on illite, 103–104 l/kg on goethite and montmorillonite, and 200 and 75 l/kg on Skan Bay and Resurrection Bay (Alaska) sediments, respectively. These partition coefficients are sufficiently large to permit sedimentary protein preservation via an adsorptive mechanism. Generally, basic polyamino acids had greater adsorption partition coefficients than acidic polyamino acids. Molecular size did not affect the electrostatic interaction between polyamino acids and mineral surfaces. Adsorption of bovine serum albumin (BSA) and negatively charged polyamino acids inhibited Rubisco adsorption, while positively charged cytochrome c and polyamino acids increased Rubisco adsorption. These results indicate that electrostatic interactions dominated in protein adsorption. |
