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Physicochemical properties of protein-smectite and protein-Al(OH)x-smectite complexes

Published online by Cambridge University Press:  09 July 2018

A. Violante
Affiliation:
Dipartimento di Scienze Chimico-Agrarie, Università di Napoli, “Federico II”, 80055 Portici, Napoli, Italy
A. de Cristofaro
Affiliation:
Dipartimento di Scienze Chimico-Agrarie, Università di Napoli, “Federico II”, 80055 Portici, Napoli, Italy
M.A. Rao
Affiliation:
Dipartimento di Scienze Chimico-Agrarie, Università di Napoli, “Federico II”, 80055 Portici, Napoli, Italy
L. Gianfreda
Affiliation:
Dipartimento di Scienze Chimico-Agrarie, Università di Napoli, “Federico II”, 80055 Portici, Napoli, Italy

Abstract

Proteins (catalase, albumin, pepsin and lysozyme with different molecular weights and isoelectric points) were differently adsorbed at pH 7.0 on the clay fraction of three raw Na-saturated smectites (Crook and Uri montmorillonites and one hectorite). The adsorption isotherms of proteins on clay minerals showed typical Langmuir characteristics. Lysozyme was adsorbed under the effect of electrostatic interactions between the opposite charges of clay surfaces and protein molecules, whereas catalase and albumin were adsorbed under the effect of non-electrostatic forces. Pepsin was held in relatively high amounts only on the surfaces of hectorite. Proteins were intercalated in the interlayers spaces of smectites, usually undergoing extensive unfolding. Protein-smectite complexes showed different behaviour to heating treatment. Some complexes remained practically unchanged after heating at 200°C. Presence of ‘wrecks’ of interlayered materials was found after heating at 500°C for two hours. The amounts of proteins adsorbed on the external and interlamellar surfaces of clay minerals, partially coated with OH-Al species, were much lower than those fixed on the clean clays. Only lysozyme was intercalated in chlorite-like complexes.

Information

Type
Research Article
Copyright
Copyright © The Mineralogical Society of Great Britain and Ireland 1995

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