Details
| Original language | English |
|---|---|
| Article number | e202402075 |
| Journal | CHEMSUSCHEM |
| Volume | 18 |
| Issue number | 6 |
| Early online date | 29 Oct 2024 |
| Publication status | Published - 17 Mar 2025 |
Abstract
Redox biocatalysis is an essential pillar of the chemical industry. Yet, the enzymes’ nature restricts most reactions to aqueous conditions, where the limited substrate solubility leads to unsustainable diluted biotranformations. Non-aqueous media represent a strategic solution to conduct intensified biocatalytic routes. Deep eutectic solvents (DESs) are designable solvents that can be customized to meet specific application needs. Within the large design space of combining DES components (and ratios), hydrophobic DESs hold the potential to be both enzyme-compatible – keeping the enzymes’ hydration –, and solubilizers for hydrophobic reactants. We explored two hydrophobic DESs, lidocaine/oleic acid, and lidocaine/decanoic acid, as reaction media for carbonyl reduction catalyzed by horse liver alcohol dehydrogenase, focusing on the effect of water contents and on maximizing substrate loadings. Enzymes remained highly active and stable in the DESs with 20 wt % buffer, whereas the reaction performance in DESs outperformed the pure buffer system with hydrophobic substrates (e. g., cinnamaldehyde to form the industrially relevant cinnamyl alcohol), with a 3-fold specific activity. Notably, the cinnamaldehyde reduction was for the first time performed at 800 mM (~100 g L −1) with full conversion, which opens up new avenues to industrial applications of hydrophobic DESs for enzyme catalysis.
Keywords
- Alcohol dehydrogenase, Hydrophobic deep eutectic solvents, Redox biocatalysis
ASJC Scopus subject areas
- Energy(all)
- General Energy
- Chemical Engineering(all)
- General Chemical Engineering
- Materials Science(all)
- General Materials Science
- Environmental Science(all)
- Environmental Chemistry
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In: CHEMSUSCHEM, Vol. 18, No. 6, e202402075, 17.03.2025.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Redox Biocatalysis in Lidocaine‐Based Hydrophobic Deep Eutectic Solvents
T2 - Non‐Conventional Media Outperform Aqueous Conditions
AU - Zhang, Ningning
AU - Lahmann, Viktoria
AU - Bittner, Jan Philipp
AU - María, Pablo Domínguez de
AU - Jakobtorweihen, Sven
AU - Smirnova, Irina
AU - Kara, Selin
N1 - Publisher Copyright: © 2024 The Author(s). ChemSusChem published by Wiley-VCH GmbH.
PY - 2025/3/17
Y1 - 2025/3/17
N2 - Redox biocatalysis is an essential pillar of the chemical industry. Yet, the enzymes’ nature restricts most reactions to aqueous conditions, where the limited substrate solubility leads to unsustainable diluted biotranformations. Non-aqueous media represent a strategic solution to conduct intensified biocatalytic routes. Deep eutectic solvents (DESs) are designable solvents that can be customized to meet specific application needs. Within the large design space of combining DES components (and ratios), hydrophobic DESs hold the potential to be both enzyme-compatible – keeping the enzymes’ hydration –, and solubilizers for hydrophobic reactants. We explored two hydrophobic DESs, lidocaine/oleic acid, and lidocaine/decanoic acid, as reaction media for carbonyl reduction catalyzed by horse liver alcohol dehydrogenase, focusing on the effect of water contents and on maximizing substrate loadings. Enzymes remained highly active and stable in the DESs with 20 wt % buffer, whereas the reaction performance in DESs outperformed the pure buffer system with hydrophobic substrates (e. g., cinnamaldehyde to form the industrially relevant cinnamyl alcohol), with a 3-fold specific activity. Notably, the cinnamaldehyde reduction was for the first time performed at 800 mM (~100 g L −1) with full conversion, which opens up new avenues to industrial applications of hydrophobic DESs for enzyme catalysis.
AB - Redox biocatalysis is an essential pillar of the chemical industry. Yet, the enzymes’ nature restricts most reactions to aqueous conditions, where the limited substrate solubility leads to unsustainable diluted biotranformations. Non-aqueous media represent a strategic solution to conduct intensified biocatalytic routes. Deep eutectic solvents (DESs) are designable solvents that can be customized to meet specific application needs. Within the large design space of combining DES components (and ratios), hydrophobic DESs hold the potential to be both enzyme-compatible – keeping the enzymes’ hydration –, and solubilizers for hydrophobic reactants. We explored two hydrophobic DESs, lidocaine/oleic acid, and lidocaine/decanoic acid, as reaction media for carbonyl reduction catalyzed by horse liver alcohol dehydrogenase, focusing on the effect of water contents and on maximizing substrate loadings. Enzymes remained highly active and stable in the DESs with 20 wt % buffer, whereas the reaction performance in DESs outperformed the pure buffer system with hydrophobic substrates (e. g., cinnamaldehyde to form the industrially relevant cinnamyl alcohol), with a 3-fold specific activity. Notably, the cinnamaldehyde reduction was for the first time performed at 800 mM (~100 g L −1) with full conversion, which opens up new avenues to industrial applications of hydrophobic DESs for enzyme catalysis.
KW - Alcohol dehydrogenase
KW - Hydrophobic deep eutectic solvents
KW - Redox biocatalysis
UR - http://www.scopus.com/inward/record.url?scp=85209804589&partnerID=8YFLogxK
U2 - 10.1002/cssc.202402075
DO - 10.1002/cssc.202402075
M3 - Article
VL - 18
JO - CHEMSUSCHEM
JF - CHEMSUSCHEM
SN - 1864-5631
IS - 6
M1 - e202402075
ER -