Process Biochemistry, cilt.131, ss.52-58, 2023 (SCI-Expanded)
Uricase suppresses the harmful effects of uric acid accumulation by the degradation of uric acid to allantoin. Maintaining enzyme stability is a major challenge. The stability issue can be avoided when using enzymes loaded into polymeric structures. For this purpose, uricase loaded into responsive nanopolymers (UO-RNPs) was synthesized. The characterizations such as SEM, FTIR, and zeta potential of UO-RNPs were performed. Maximum uricase loading to RNPs was investigated and the release performance of UO-RNPs also under variable conditions such as pH and temperature. On the other hand, loading yield (LY) and loading efficiency (LE) was founded 73.22 ± 3.62% and 71.24 ± 4.61%, while storage stability and reusability of the UO-RNPs were found to be about 68% and 51% of the original activity after 4 weeks and 10 cycles, respectively. From Lineweaver-Burk plot the Km was founded 0.192 and 0.327 mM for loaded and free uricase. While V max was founded 0.131 and 0.0714 μM/min for free uricase and UO-RNPs, respectively. UO-RNPs showed promising matrices for high catalytic efficiency and enhanced stability. Up until now, as far as we know, the present study of the loaded uricase into responsive nanopolymers is the first attempt of uricase enzyme in such an investigation.