Effect of Urease Enzyme Immobilized to Particle Surface with Glyoxal Molecule on Storage Stability
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https://doi.org/10.5281/zenodo.10001636Keywords:
Urease, immobilization, nanoparticle, stabilityAbstract
Immobilization is the immobilization of a biological catalyst in an analytical system. The synthesized complex has the catalytic feature of the free biochemical enzyme. Nowadays, it is tried to benefit from the advantages of immobilized enzymes instead of rapidly inactivated enzymes. Its advantages over free enzymes, such as reusability and ease of removal from the reaction medium, are developing day by day. In this study, it was planned to provide urease enzyme stabilization by using the advantages of nanoparticles (Çukurova University Project Unit, TYD-2015-3765). For this purpose, after the urease enzyme was bound to the produced nanoparticles and reshaped, the catalytic property of the enzyme activity was evaluated at different temperatures. Superparamagnetic nanoparticles (SPIONs) were synthesized. Surface modifications were provided by using glyoxal molecule and urease enzyme immobilization was performed for enzyme stability. The activity properties were investigated under the optimum temperature limits and under variable (25oC-4oC- 37oC) conditions. Statistically, it was determined that the study groups did not show a statistically significant difference between the control groups and groups. The results of the study showed that the immobilized enzyme improved the storage stability and shelf life (p>0.05).
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