Título: Screening mutant libraries of versatile peroxidase from Pleurotus eryngii to enhance oxidative stability
Autor: González-Pérez, David; Roman, Alina; García-Ruiz, Eva; Ruiz-Dueñas, F. J.; Martínez, Ángel T.; Alcalde Galeote, Miguel
Resumen: Versatile peroxidases (VPs) are promiscuous high-redox potential biocatalysts with broad substrate specificity. VPs are strongly inhibited by modest concentrations of hydrogen peroxide which hampers their application in
different industrial settings. In the current work, a VP mutant evolved in our laboratory for functional expression was used as departure point to tailor oxidative stability. A high-throughput assay based on the analysis of the apparent half-life using different H2O2:enzyme molar ratios was designed and employed to explore mutant libraries. After only one round of directed evolution two variants were selected showing apparent half-life of 10- 23 min with a 3,000-fold H2O2:enzyme molar excess.
Descripción: Trabajo presentado en el 13th European Workshop on Lignocellulosics and Pulp, celebrado en Sevilla (España) del 24 al 27 de junio de 2014
↧