# Biomass‐Derived Diformylxylose as a Renewable Solvent for Biocatalysis Applications

**Authors:** Fatma Feyza Özgen, Peter Stockinger, Anastasia Komarova, Jeremy Luterbacher, Rebecca Buller

PMC · DOI: 10.1002/cssc.202502273 · Chemsuschem · 2026-02-25

## TL;DR

This paper shows that diformylxylose (DFX), a green solvent derived from biomass, can effectively support enzyme reactions, especially for ketoreductases and lipases, outperforming traditional solvents.

## Contribution

The study introduces DFX as a renewable solvent that enhances enzyme performance and substrate solubility in biocatalysis.

## Key findings

- KRED TeSADH W110A achieved full conversion in DFX at high substrate concentration, outperforming DMSO and DMF.
- Lipase CalB reached 95% conversion in DFX at high substrate loading.
- DFX supports high enzyme activity for KREDs and lipases but shows limited compatibility with transaminases and imine reductases.

## Abstract

Developing sustainable biocatalytic processes requires alternative solvents that support enzyme activity while reducing environmental impact. This study explores the potential to use diformylxylose (DFX), a xylose‐derived green solvent, as a cosolvent in enzymatic reactions, and compares its application to reaction outcomes in conventional solvents such as dimethyl sulfoxide (DMSO) and dimethylformamide (DMF). A comprehensive enzyme panel, including ketoreductases (KREDs), lipases as well as transaminases (TAs) and imine reductases (IREDs) was tested for activity and stability in DFX. In the green solvent, the selected KREDs and the immobilized lipase CalB retained high or even superior catalytic activity compared to conventional media, while the selected biocatalysts from other enzyme classes such as TAs, and IREDs exhibited limited compatibility under the tested conditions underscoring the enzyme‐specific nature of solvent effects. Notably, the KRED TeSADH W110A achieved full conversion when asymmetrically reducing phenyl‐ring‐containing ketones at 300 mM substrate concentration in DFX, significantly outperforming reaction conditions with DMSO and DMF (∼40% conversion). Lipase CalB also exhibited remarkable activity, reaching 95% conversion at 300 mM 4‐nitrophenyl butyrate loading. The findings highlight DFX as a promising alternative solvent for biocatalysis applications, particularly for KRED‐ and lipase‐mediated reactions.

It feels greener in diformylxylose (DFX)! The renewable solvent dissolves aromatic ketones at remarkable concentrations and sustains the performance of robust enzymes such as ketoreductases (KREDs) and lipases. By combining superior substrate dissolution with improved enzyme performance, DFX offers a green medium for selective, high‐load biotransformations.© 2026 WILEY‐VCH GmbH

## Linked entities

- **Proteins:** CALB1 (calbindin 1), THAS (thoracoabdominal syndrome)
- **Chemicals:** dimethyl sulfoxide (PubChem CID 679), DMSO (PubChem CID 679), dimethylformamide (PubChem CID 6228), DMF (PubChem CID 6228), 4-nitrophenyl butyrate (PubChem CID 75834)

## Full-text entities

- **Diseases:** toxicity (MESH:D064420)
- **Chemicals:** H2SO4 (MESH:C033158), DMSO (MESH:D004121), glucose (MESH:D005947), 4-nitrophenyl butyrate (MESH:C033592), hydrogen (MESH:D006859), PLP (MESH:D011732), (S)-alcohol (MESH:D000438), GC (MESH:C057580), NAD+ (MESH:D009243), D-xylose (MESH:D014994), DMF (MESH:D004126), paraformaldehyde (MESH:C003043), CO2 (MESH:D002245), fatty acids (MESH:D005227), carbohydrate (MESH:D002241), 2-Me-THF (MESH:C587233), amine (MESH:D000588), NADP+ (MESH:D009249), HEPES (MESH:D006531), glycerol (MESH:D005990), KREDs (-), ethyl acetate (MESH:C007650), aldehyde (MESH:D000447), NaOH (MESH:D012972), bmim]BF4 (MESH:C419324), EtOH (MESH:D000431), 2-propanol (MESH:D019840), water (MESH:D014867), carbon (MESH:D002244), ketone (MESH:D007659), ester (MESH:D004952), triglycerides (MESH:D014280), acetonitrile (MESH:C032159), N2 (MESH:D009584), 2-MeTHF (MESH:C550584), His (MESH:D006639), formic acid (MESH:C030544), acids (MESH:D000143), sugar (MESH:D000073893), methanol (MESH:D000432)
- **Species:** PX clade (clade) [taxon 569578], Lentilactobacillus kefiri (species) [taxon 33962], Thermoanaerobacter ethanolicus (species) [taxon 1757], Chryseobacterium sp. (species) [taxon 1871047], Pseudomonas putida (species) [taxon 303], Paracoccus pantotrophus (species) [taxon 82367], Thermoanaerobacter ethanolicus JW 200 (strain) [taxon 509192], Escherichia coli (E. coli, species) [taxon 562]
- **Mutations:** W110A, C for 16-20, W110A, C-55 C, C-70 C
- **Cell lines:** E. coli BL21(DE3) — Mus musculus (Mouse), Hybridoma (CVCL_B7HM), pET28b — Oryctolagus cuniculus (Rabbit), Transformed cell line (CVCL_6E94), ChKRED20 — Aedes aegypti (Yellowfever mosquito), Spontaneously immortalized cell line (CVCL_Z353), S2 — Drosophila melanogaster (Fruit fly), Spontaneously immortalized cell line (CVCL_Z232)

## Full text

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## Figures

4 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12934546/full.md

## References

46 references — full list in the complete paper: https://tomesphere.com/paper/PMC12934546/full.md

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Source: https://tomesphere.com/paper/PMC12934546