ArticleChemSusChem2026
Biomass-Derived Diformylxylose as a Renewable Solvent for Biocatalysis Applications.
Article in ChemSusChem, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
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.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.