SUMO-G5C23-D208G@ZIF-F: A Novel Immobilized Enzyme with Enhanced Stability and Reusability for Organophosphorus Hydrolysis.

ABSTRACT: Organophosphorus hydrolase (OPH) is a highly effective bioscavenger for detoxifying hazardous organophosphorus compounds. However, its practical application is hindered by low yield and poor stability. In this study, we employed Small Ubiquitin-like Modifier (SUMO) fusion expression to enhance the solubility of the OPH mutant G5C23-D208G and, for the first time, immobilized the enzyme on a zeolitic imidazolate framework-F (ZIF-F) carrier to improve its stability. The SUMO-G5C23-D208G fusion protein was successfully expressed in Escherichia coli, resulting in a yield that was 2.4 times higher than that of native OPH and an 11-fold increase in solubility. The purified protein achieved a purity of 95%. The immobilized enzyme, SU-MO-G5C23-D208G@ZIF-F, exhibited a farfalle-shaped structu

SUBMITTER: Wang S 

PROVIDER: S-EPMC11942619 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature