Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 24, 2018
Previous Article Next Article

Enzymatic reduction of levoglucosenone by an alkene reductase (OYE 2.6): a sustainable metal- and dihydrogen-free access to the bio-based solvent Cyrene®

Author affiliations

Abstract

Levoglucosenone (LGO) has been successfully converted into the green polar aprotic solvent 2H-LGO (aka Cyrene®) through an enzymatic process involving alkene reductases: wild-type Old Yellow Enzyme 2.6 (OYE 2.6 wt.) from Pichia stipitis and its mutant (OYE 2.6 Tyr78Trp) present the best conversion rates. This enzymatic process has been optimized in order to avoid the formation of the side-product (1R,2S)-2-hydroxy-6,8-dioxabicyclo[3.2.1]octan-4-one (OH-LGO) and reach total conversion (99%). Cyrene® was then successfully isolated by continuous extraction in quantitative yield (99%).

Graphical abstract: Enzymatic reduction of levoglucosenone by an alkene reductase (OYE 2.6): a sustainable metal- and dihydrogen-free access to the bio-based solvent Cyrene®

Back to tab navigation

Supplementary files

Article information


Submitted
08 Oct 2018
Accepted
09 Nov 2018
First published
09 Nov 2018

Green Chem., 2018,20, 5528-5532
Article type
Paper
Author version available

Enzymatic reduction of levoglucosenone by an alkene reductase (OYE 2.6): a sustainable metal- and dihydrogen-free access to the bio-based solvent Cyrene®

L. M. M. Mouterde, F. Allais and J. D. Stewart, Green Chem., 2018, 20, 5528
DOI: 10.1039/C8GC03146K

Social activity

Search articles by author

Spotlight

Advertisements