Optimization of immobilized urease enzyme on porous polymer for enhancing the stability, reusability and enzymatic kinetics using response surface methodology.

Autor: Sahin B; Department of Biotechnology, Gebze Technical University, Gebze 41400, Turkey., Ozbey-Unal B; Department of Environmental Engineering, Gebze Technical University, Gebze 41400, Turkey; Institute of Earth and Marine Sciences, Gebze Technical University, Gebze 41400, Turkey., Dizge N; Department of Environmental Engineering, Mersin University, Mersin 33343, Turkey., Keskinler B; Department of Environmental Engineering, Gebze Technical University, Gebze 41400, Turkey., Balcik C; Department of Environmental Engineering, Gebze Technical University, Gebze 41400, Turkey. Electronic address: cigdembalcik@gtu.edu.tr.
Jazyk: angličtina
Zdroj: Colloids and surfaces. B, Biointerfaces [Colloids Surf B Biointerfaces] 2024 Aug; Vol. 240, pp. 113986. Date of Electronic Publication: 2024 May 23.
DOI: 10.1016/j.colsurfb.2024.113986
Abstrakt: The study examines the immobilization of the urease enzyme on a range of High Internal Phase Emulsion (polyHIPE) materials, assessing characteristics, efficiency, and performance. It also investigates the impact of polyHIPE type, quantity, incubation time, and various parameters on the process and enzyme activity. Surface morphology and functional groups of polyHIPE materials were determined through scanning electron microscopy (SEM) and fourier transform infrared spectroscopy (FT-IR) analyses, revealing significant alterations after modification with polyglutaraldehyde (PGA). The maximum immobilization efficiency of 95% was achieved by adding PGA to polyHIPE materials with an incubation period of 15 h. The optimized conditions for immobilized enzyme using a Box-Behnken design (BBD) of response surface methodology (RSM) were as follows: temperature (40.8 °C), pH (7.1) and NaCl concentration (0.007 g/L). Furthermore, the immobilized enzyme demonstrated remarkable reusability, retaining 75% of its initial activity after six cycles, and sustained shelf-life stability, retaining over 40% activity after 10 days at room temperature. Kinetic analyses revealed that immobilized urease exhibited higher affinity for the substrate, but lower rate of substrate conversion compared to the free enzyme. These findings offer valuable insights into optimizing urease immobilization processes and enhancing urease stability and activity, with potential applications in various fields, including biotechnology and biocatalysis.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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