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  • Author: Eric Grulke x
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Urease catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. The increase in pH from the urease reaction causes a broad range of deleterious effects. Nanoceria (cerium oxide) possesses unique chemical properties under a redox reaction. This study investigated the synthesis of nanoceria via a hydrothermal method and determined its interaction with urease enzyme.

Transmission electron microscopy results showed a cubic-figured nanoceria with a size of ~15 nm. Urease was immobilized on nanoceria through adsorption. The maximum velocity (V max) and Michaelis constant (K m) of the free urease and urease immobilized on nanoceria decreased after interaction with nanoceria, and the Lineweaver-Burk plot showed an uncompetitive inhibition. The thermodynamic study of the adsorption process showed an endothermic reaction. The interaction changed the secondary and tertiary structures of urease as demonstrated by the circular dichroism study (the decrease in both α- and β-structure percentages). The fluorescence study revealed a change in the tertiary structure. The FTIR for the nanoceria—urease complex showed no changes in the covalent bonds, which indicated the involvement of physical forces in the interaction between urease and nanoceria.


Calcium phosphate nanoparticles (CaPNP) have good biocompatibility and bioactivity inside human body. In this study, the interaction between CaPNP and human chorionic gonadotropin (hCG) was analyzed to determine the changes in the protein structure in the presence of CaPNP and the quantity of protein adsorbed on the CaPNP surface. The results showed a significant adsorption of hCG on the CaPNP nanoparticle surface. The optimal fit was achieved using the Sips isotherm equation with a maximum adsorption capacity of 68.23 µg/mg. The thermodynamic parameters, including ∆H° and ∆G°, of the adsorption process are positive, whereas ∆S° is negative. The circular dichroism results of the adsorption of hCG on CaPNP showed the changes in its secondary structure; such changes include the decomposition of α-helix strand and the increase in β-pleated sheet and random coil percentages. Fluorescence study indicated minimal changes in the tertiary structure near the microenvironment of the aromatic amino acids such as tyrosine and phenyl alanine caused by the interaction forces between the CaPNP and hCG protein. The desorption process showed that the quantity of the hCG desorbed significantly increases as temperature increases, which indicates the weak forces between hCG and the surface.