Data underlying the chapter and publication: Native amine dehydrogenases can catalyze the direct reduction of carbonyl compounds to alcohols in the absence of ammonia

doi:10.4121/60aff897-18b0-4dda-ad79-4a92597b90f9.v1
The doi above is for this specific version of this dataset, which is currently the latest. Newer versions may be published in the future. For a link that will always point to the latest version, please use
doi: 10.4121/60aff897-18b0-4dda-ad79-4a92597b90f9
Datacite citation style:
Fossey-Jouenne, Aurélie; Ducrot, Laurine; Jongkind, Ewald; Elisée, Eddy; Zaparucha, Anne et. al. (2024): Data underlying the chapter and publication: Native amine dehydrogenases can catalyze the direct reduction of carbonyl compounds to alcohols in the absence of ammonia. Version 1. 4TU.ResearchData. dataset. https://doi.org/10.4121/60aff897-18b0-4dda-ad79-4a92597b90f9.v1
Other citation styles (APA, Harvard, MLA, Vancouver, Chicago, IEEE) available at Datacite
Dataset

This dataset contains data collected during experiments at Delft University of Technology retrieved by Ewald Jongkind. This work is shown in the dissertation written by Ewald Jongkind. The aim of this work was to determine the activity of AmDHs in absence of ammonia. This was done by reaction screening and determining reaction activities in buffers with and without ammonia. Contributions as co-author include co-writing the publication, screening of cyclohexanone in different pH, and assessing enantiomeric excess of chiral alcohol products. Dataset consists of analyzed data in Excel by GC-FID regarding conversions to chiral alcohols, the raw table from screening AmDHs with and without ammonia, and the conversion to cyclohexanol in different buffer pH. More information can be found in the corresponding publication and the README-file

history
  • 2024-08-02 first online, published, posted
publisher
4TU.ResearchData
format
.xlsx, .txt
funding
  • (grant code ANR-19-CE07-0007)
organizations
TU Delft, Faculty of Applied Sciences, Department of Biotechnology;
François Jacob Institute of biology;
University of York, Department of Chemistry, York Structural Laboratory

DATA

files (4)