Exploring the Impact of Taurine on the Biochemical Properties of Urate Oxidase: Response Surface Methodology and Molecular Dynamics Simulation

Abstract

Abstract This paper investigates the impact of taurine as an additive on the structural and functional stability of urate oxidase. First, the effect of the processing parameters for the stabilization of Urate Oxidase (UOX) using taurine was examined using the response surface methodology (RSM) and the central composite design (CCD) model. The maximum stabilization of UOX with taurine was examined under various experimental conditions, including taurine concentration, temperature, and incubation time. Also, the study examines thermodynamic and kinetic parameters as well as structural changes, including intrinsic and ANS fluorescence, of urate oxidase with and without taurine. The results indicate that taurine treatment enhances the thermostability of uricase, with a longer half-life (135.91 min) compared to untreated urate oxidase (38.08 min) at 40°C. Thermo-inactivation experiments conducted at 40, 55, and 60°C demonstrate that the taurine-treated uricase has lower inactivation rate constants (Kinact) than untreated uricase. The examination of the inactivation process reveals that the increased thermostability of UOX-Taurine can be attributed to elevated activation energy (Ea) as well as greater values of ΔG# and ΔH# at a specific temperature. Furthermore, molecular dynamics simulation is conducted in order to get insights into the alterations in the structure of urate oxidase in the absence and presence of taurine under optimal conditions.