Porous zirconium phosphate ( P-ZrP) and zirconium benzenephosphonate ( P-ZrBP) were prepared in the presence of an anionic surfactant acting as a template. Poorly crystalline materials with a P/Zr molar ratio equal to 2 and having a relatively high surface area and micro/mesoporosity have been obtained. The interaction of myoglobin with the two types of surfaces, the hydrophobic P-ZrBP and the hydrophilic P-ZrP, was investigated, and the adsorption isotherms were determined at different pH and temperature values. A model was proposed for the mechanism of the interaction of the protein with the surface based on the shape of the adsorption isotherm and the physical-chemical properties of myoglobin. The pH has been found to be an important parameter for determining the maximum adsorption capacity of P-ZrBP and P-ZrP for myoglobin molecules because of the changes that occur in the type and net charge of the protein surface as the pH of the medium changes. Protein binding affinity and capacity increase when the temperature is increased. This phenomenon occurs because myoglobin varies its conformation at high temperature with an increase in the exposed hydrophobic region. This process causes a stronger hydrophobic interaction between the protein and the adsorbent and reduces the repulsion between the adsorbed molecules. Studies on the activities of the obtained biocomposites are in progress.