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https://doi.org/10.21256/zhaw-19537Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Aregger, David | - |
| dc.contributor.author | Peters, Christin | - |
| dc.contributor.author | Buller, Rebecca | - |
| dc.date.accessioned | 2020-02-20T16:00:13Z | - |
| dc.date.available | 2020-02-20T16:00:13Z | - |
| dc.date.issued | 2020-02 | - |
| dc.identifier.issn | 2073-4344 | de_CH |
| dc.identifier.uri | https://digitalcollection.zhaw.ch/handle/11475/19537 | - |
| dc.description.abstract | 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. | de_CH |
| dc.language.iso | en | de_CH |
| dc.publisher | MDPI | de_CH |
| dc.relation.ispartof | Catalysts | de_CH |
| dc.rights | http://creativecommons.org/licenses/by/4.0/ | de_CH |
| dc.subject.ddc | 660.6: Biotechnologie | de_CH |
| dc.title | Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa | de_CH |
| dc.type | Beitrag in wissenschaftlicher Zeitschrift | de_CH |
| dcterms.type | Text | de_CH |
| zhaw.departement | Life Sciences und Facility Management | de_CH |
| zhaw.organisationalunit | Institut für Chemie und Biotechnologie (ICBT) | de_CH |
| dc.identifier.doi | 10.3390/catal10020254 | de_CH |
| dc.identifier.doi | 10.21256/zhaw-19537 | - |
| zhaw.funding.eu | No | de_CH |
| zhaw.issue | 2 | de_CH |
| zhaw.originated.zhaw | Yes | de_CH |
| zhaw.publication.status | publishedVersion | de_CH |
| zhaw.volume | 10 | de_CH |
| zhaw.publication.review | Peer review (Publikation) | de_CH |
| zhaw.author.additional | No | de_CH |
| Appears in collections: | Publikationen Life Sciences und Facility Management | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| 2020_Aregger_Characterization_of_the_Novel_Ene_Reductase_MDPI.pdf | 1.23 MB | Adobe PDF |  View/Open |
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Aregger, D., Peters, C., & Buller, R. (2020). Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa. Catalysts, 10(2). https://doi.org/10.3390/catal10020254
Aregger, D., Peters, C. and Buller, R. (2020) ‘Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa’, Catalysts, 10(2). Available at: https://doi.org/10.3390/catal10020254.
D. Aregger, C. Peters, and R. Buller, “Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa,” Catalysts, vol. 10, no. 2, Feb. 2020, doi: 10.3390/catal10020254.
AREGGER, David, Christin PETERS und Rebecca BULLER, 2020. Characterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxa. Catalysts. Februar 2020. Bd. 10, Nr. 2. DOI 10.3390/catal10020254
Aregger, David, Christin Peters, and Rebecca Buller. 2020. “Characterization of the Novel Ene Reductase Ppo-Er1 from Paenibacillus Polymyxa.” Catalysts 10 (2). https://doi.org/10.3390/catal10020254.
Aregger, David, et al. “Characterization of the Novel Ene Reductase Ppo-Er1 from Paenibacillus Polymyxa.” Catalysts, vol. 10, no. 2, Feb. 2020, https://doi.org/10.3390/catal10020254.
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