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https://doi.org/10.21256/zhaw-19537| Publikationstyp: | Beitrag in wissenschaftlicher Zeitschrift |
| Art der Begutachtung: | Peer review (Publikation) |
| Titel: | Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa |
| Autor/-in: | Aregger, David Peters, Christin Buller, Rebecca |
| et. al: | No |
| DOI: | 10.3390/catal10020254 10.21256/zhaw-19537 |
| Erschienen in: | Catalysts |
| Band(Heft): | 10 |
| Heft: | 2 |
| Erscheinungsdatum: | Feb-2020 |
| Verlag / Hrsg. Institution: | MDPI |
| ISSN: | 2073-4344 |
| Sprache: | Englisch |
| Fachgebiet (DDC): | 660.6: Biotechnologie |
| Zusammenfassung: | Ene reductases enable the asymmetric hydrogenation of activated alkenes allowing the manufacture of valuable chiral products. The enzymes complement existing metal- and organocatalytic approaches for the stereoselective reduction of activated C=C double bonds, and efforts to expand the biocatalytic toolbox with additional ene reductases are of high academic and industrial interest. Here, we present the characterization of a novel ene reductase from Paenibacillus polymyxa, named Ppo-Er1, belonging to the recently identified subgroup III of the old yellow enzyme family. The determination of substrate scope, solvent stability, temperature, and pH range of Ppo-Er1 is one of the first examples of a detailed biophysical characterization of a subgroup III enzyme. Notably, Ppo-Er1 possesses a wide temperature optimum (Topt: 20–45 °C) and retains high conversion rates of at least 70% even at 10 °C reaction temperature making it an interesting biocatalyst for the conversion of temperature-labile substrates. When assaying a set of different organic solvents to determine Ppo-Er1′s solvent tolerance, the ene reductase exhibited good performance in up to 40% cyclohexane as well as 20 vol% DMSO and ethanol. In summary, Ppo-Er1 exhibited activity for thirteen out of the nineteen investigated compounds, for ten of which Michaelis–Menten kinetics could be determined. The enzyme exhibited the highest specificity constant for maleimide with a kcat/KM value of 287 mM−1 s−1. In addition, Ppo-Er1 proved to be highly enantioselective for selected substrates with measured enantiomeric excess values of 92% or higher for 2-methyl-2-cyclohexenone, citral, and carvone. |
| URI: | https://digitalcollection.zhaw.ch/handle/11475/19537 |
| Volltext Version: | Publizierte Version |
| Lizenz (gemäss Verlagsvertrag): | CC BY 4.0: Namensnennung 4.0 International |
| Departement: | Life Sciences und Facility Management |
| Organisationseinheit: | Institut für Chemie und Biotechnologie (ICBT) |
| Enthalten in den Sammlungen: | Publikationen Life Sciences und Facility Management |
Dateien zu dieser Ressource:
| Datei | Beschreibung | Größe | Format | |
|---|---|---|---|---|
| 2020_Aregger_Characterization_of_the_Novel_Ene_Reductase_MDPI.pdf | 1.23 MB | Adobe PDF |  Öffnen/Anzeigen |
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