Abstract
Protein adsorption is a natural phenomenon in terrestrial and aquatic ecosystems. Bacteria and fungi secrete enzymes which cleave high molecular weight polymers of organic matter allowing soluble monomers to cross the membranes of the plant cells [1]. In soils, clays have large surface area and high adsorptive properties. Hydrophobic, hydrophilic and electrostatic interactions have not been fully elucidated for protein adsorption. We identify pH-dependent structural changes for Bovine Serum Albumin (BSA) adsorbed on montmorillonite and talc, which are electronegative and hydrophobic phyllosilicates respectively.
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References
Quiquampoix H., Abadie J., Baron M.H., Leprince F., Marumoto-Pintro P.T., Ratcliffe R.G. and Staunton S., in T.H. Horbett and J.L. Brash (eds) Proteins at Interfaces, ACS Symposium, Series 602, (1995), pp 321–333.
Boulkanz, L., Balcar N., Baron M. H., Applied Spectrosc. 49, (1995) 1737.
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© 1999 Springer Science+Business Media Dordrecht
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Servagent-Noinville, S., Revault, M., Quiquampoix, H., Baron, MH. (1999). Protein adsorption on soil mineral surfaces. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_26
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DOI: https://doi.org/10.1007/978-94-011-4479-7_26
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-5919-0
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