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Abstract

Interaction between sepiolite and collagen has been studied using two different micronizing procedures for the sepiolite. Micronizing in the dry state yields shorter fibers than micronizing in the wet state. The adsorption of collagen was followed by ultraviolet-absorbance and measurement of the amino acid content of the protein-clay complexes. The interaction primarily involved the high molecular weight aggregates of the protein. A collagen-clay weight ratio of 0.4 was reached at pH ~4. The adsorption decreased with increasing ionic strength. A model is proposed wherein rod-shaped protein molecules are bound on the stepped surface of the sepiolite.

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