Biocatalytic Oxidative CC Bond Formation Catalysed by the Berberine Bridge Enzyme: Optimal Reaction Conditions
✍ Scribed by Verena Resch; Joerg H. Schrittwieser; Silvia Wallner; Peter Macheroux; Wolfgang Kroutil
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 458 KB
- Volume
- 353
- Category
- Article
- ISSN
- 1615-4150
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✦ Synopsis
Abstract
Berberine bridge enzyme (BBE) catalyses the oxidative formation of an intramolecular CC bond using (S)‐reticuline as the natural substrate to form (S)‐scoulerine as the product. To allow application of the enzyme on a preparative scale for the synthesis of novel optically pure berbine and isoquinoline derivatives, an organic solvent is required to solubilise the barely soluble substrates. It was shown that BBE tolerates a broad variety of organic co‐solvents. Ideally the enzymatic enantioselective oxidative CC bond formation can be performed in 70% v v^−1^ toluene concentration, which allowed a soluble substrate concentration of at least 20 g L^−1^. In addition, the enzyme works in a broad operational window concerning pH and temperature. High conversions can be reached between pH 8 and 11 and from 30 to 50 °C, respectively. The enantioselective oxidative CC bond formation was demonstrated on a preparative scale (500 mg) in a kinetic resolution leading to optically pure products (>97% ee).