This title appears in the Scientific Report :
2020
Please use the identifier:
http://dx.doi.org/10.1021/acscatal.0c01789 in citations.
Please use the identifier: http://hdl.handle.net/2128/26105 in citations.
Engineered PQQ-Dependent Alcohol Dehydrogenase for the Oxidation of 5-(Hydroxymethyl)furoic Acid
Engineered PQQ-Dependent Alcohol Dehydrogenase for the Oxidation of 5-(Hydroxymethyl)furoic Acid
Furan-2,5-dicarboxylic acid (FDCA) is a bio-based platform chemical with the potential to replace terephthalic acid in the production of polymers. A critical step for enzymatic and whole-cell production of FDCA from 5-(hydroxymethyl)furfural (HMF) is the transformation of 5-(hydroxymethyl)furoic aci...
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Personal Name(s): | Wehrmann, Matthias |
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Elsayed, Eslam M. / Köbbing, Sebastian / Bendz, Laura / Lepak, Alexander / Schwabe, Johannes / Wierckx, Nick / Bange, Gert (Corresponding author) / Klebensberger, Janosch (Corresponding author) | |
Contributing Institute: |
Biotechnologie; IBG-1 |
Published in: | ACS catalysis, 10 (2020) 14, S. 7836 - 7842 |
Imprint: |
Washington, DC
ACS
2020
|
DOI: |
10.1021/acscatal.0c01789 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology |
Link: |
Published on 2020-06-09. Available in OpenAccess from 2021-06-09. Restricted Published on 2020-06-09. Available in OpenAccess from 2021-06-09. Restricted |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/26105 in citations.
Furan-2,5-dicarboxylic acid (FDCA) is a bio-based platform chemical with the potential to replace terephthalic acid in the production of polymers. A critical step for enzymatic and whole-cell production of FDCA from 5-(hydroxymethyl)furfural (HMF) is the transformation of 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA). Here, we establish periplasmic pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenases (ADHs) as biocatalytic tools for the oxidation of HMFA, HMF, and 5-formylfurfural (FFF). Further, we identify several amino acid residues including the “lid loop” of the substrate channel as promising targets for future engineering steps toward a fully periplasmic oxidation pathway to FDCA. |