| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 71210 | Journal of Molecular Catalysis B: Enzymatic | 2006 | 6 Pages |
Abstract
Regioselective oxidations of the primary OH's of natural glycosides (thiocolchicoside, colchicoside, amygdalin, asiaticoside, ginsenoside RE) have been performed on a preparative scale by exploiting the laccase–2,2,6,6-tetramethyl-1-piperidinyloxy (TEMPO) methodology. The influence of water-miscible organic cosolvents on the stability and activity of a laccase from Trametes pubescens has been investigated. The enzyme has been covalently linked to Eupergit C250L and its performances evaluated. The recovered immobilized enzyme catalyzed several oxidative cycles of thiocolchicoside, without showing significant loss of activity.
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Physical Sciences and Engineering
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Catalysis
Authors
Lara Baratto, Andrea Candido, Mattia Marzorati, Francesca Sagui, Sergio Riva, Bruno Danieli,