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This study explores the potential to use diformylxylose (DFX), a xylose\u2010derived 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\u2010specific nature of solvent effects. Notably, the KRED TeSADH W110A achieved full conversion when asymmetrically reducing phenyl\u2010ring\u2010containing ketones at 300\u2009mM substrate concentration in DFX, significantly outperforming reaction conditions with DMSO and DMF (\u223c40% conversion). Lipase CalB also exhibited remarkable activity, reaching 95% conversion at 300\u2009mM 4\u2010nitrophenyl butyrate loading. The findings highlight DFX as a promising alternative solvent for biocatalysis applications, particularly for KRED\u2010 and lipase\u2010mediated reactions.<\/jats:p>","DOI":"10.1002\/cssc.202502273","type":"journal-article","created":{"date-parts":[[2026,3,8]],"date-time":"2026-03-08T16:54:03Z","timestamp":1772988843000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Biomass\u2010Derived Diformylxylose as a Renewable Solvent for Biocatalysis Applications"],"prefix":"10.1002","volume":"19","author":[{"given":"Fatma Feyza","family":"\u00d6zgen","sequence":"first","affiliation":[{"name":"Competence Center for Biocatalysis Zurich University of Applied Sciences  W\u00e4denswil Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter","family":"Stockinger","sequence":"additional","affiliation":[{"name":"Competence Center for Biocatalysis Zurich University of Applied Sciences  W\u00e4denswil Switzerland"},{"name":"Department of Chemistry Biochemistry and Pharmaceutical Sciences University of Bern  Bern Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anastasia","family":"Komarova","sequence":"additional","affiliation":[{"name":"Laboratory of Sustainable and Catalytic Processing Institute of Chemical Sciences and Engineering \u00c9cole Polytechnique F\u00e9d\u00e9rale de Lausanne (EPFL)  Lausanne Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeremy","family":"Luterbacher","sequence":"additional","affiliation":[{"name":"Laboratory of Sustainable and Catalytic Processing Institute of Chemical Sciences and Engineering \u00c9cole Polytechnique F\u00e9d\u00e9rale de Lausanne (EPFL)  Lausanne Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5997-1616","authenticated-orcid":false,"given":"Rebecca","family":"Buller","sequence":"additional","affiliation":[{"name":"Competence Center for Biocatalysis Zurich University of Applied Sciences  W\u00e4denswil Switzerland"},{"name":"Department of Chemistry Biochemistry and Pharmaceutical Sciences University of Bern  Bern Switzerland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2026,2,25]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.adh8615"},{"key":"e_1_2_9_3_1","first-page":"1","article-title":"Effective Engineering of Ketoreductase for Biocatalytic Synthesis of Ipatasertib Precursor","volume":"7","author":"Malca S. 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