Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis
Metadatos
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Recio Muñoz, María Isabel; de la Torre, Jesús; Daddaoua, Abdelali; Udaondo, Zulema; Duque, Estrella; Gavira Gallardo, José Antonio; López Sánchez, Carmen; Ramos, Juan LuisEditorial
John Wiley & Sons
Fecha
2024-04-08Referencia bibliográfica
Recio, M.-I., de la Torre, J., Daddaoua, A., Udaondo, Z., Duque, E., Gavira, J.A. et al. (2024) Characterization of an extremophile bacterial acid phosphatase derived from metagenomics analysis. Microbial Biotechnology, 17, e14404. Available from: https://doi.org/10.1111/1751-7915.14404
Patrocinador
Grants from the Ministry of Science through grants from the Plan Nacional 2021 (PID2021-123469OBI00) and Transición Ecológica (TED2021129632BI00) and European Commission projects EJP soils (EJPSOIL862695) and PREPSOIL (HE/CL5SOILM/0102)Resumen
Acid phosphatases are enzymes that play a crucial role in the hydrolysis of various organophosphorous molecules. A putative acid phosphatase called FS6 was identified using genetic profiles and sequences from different environments. FS6 showed high sequence similarity to type C acid phosphatases and retained more than 30% of consensus residues in its protein sequence. A histidine-tagged recombinant FS6 produced in Escherichia coli exhibited extremophile properties, functioning effectively in a broad pH range between 3.5 and 8.5. The enzyme demonstrated optimal activity at temperatures between 25 and 50°C, with a melting temperature of 51.6°C. Kinetic parameters were determined using various substrates, and the reaction catalysed by FS6 with physiological substrates was at least 100-fold more efficient than with p-nitrophenyl
phosphate. Furthermore, FS6 was found to be a decamer in solution, unlike the dimeric forms of crystallized proteins in its family.