Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-19537
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dc.contributor.authorAregger, David-
dc.contributor.authorPeters, Christin-
dc.contributor.authorBuller, Rebecca-
dc.date.accessioned2020-02-20T16:00:13Z-
dc.date.available2020-02-20T16:00:13Z-
dc.date.issued2020-02-
dc.identifier.issn2073-4344de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/19537-
dc.description.abstractEne 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.isoende_CH
dc.publisherMDPIde_CH
dc.relation.ispartofCatalystsde_CH
dc.rightshttp://creativecommons.org/licenses/by/4.0/de_CH
dc.subject.ddc660.6: Biotechnologiede_CH
dc.titleCharacterization of the novel ene reductase Ppo-Er1 from paenibacillus polymyxade_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.3390/catal10020254de_CH
dc.identifier.doi10.21256/zhaw-19537-
zhaw.funding.euNode_CH
zhaw.issue2de_CH
zhaw.originated.zhawYesde_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume10de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.author.additionalNode_CH
Appears in collections:Publikationen Life Sciences und Facility Management

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