Immobilisation of P450 BM-3 and an NADP+ Cofactor Recycling System: Towards a Technical Application of Heme-Containing Monooxygenases in Fine Chemical Synthesis
✍ Scribed by Steffen C. Maurer; Holger Schulze; Rolf D. Schmid; Vlada Urlacher
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 123 KB
- Volume
- 345
- Category
- Article
- ISSN
- 1615-4150
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✦ Synopsis
Abstract
Abstract: Cytochrome P450 monooxygenases are potentially a very useful class of hydroxylation catalysts; they are able to introduce oxygen at activated and non‐activated carbon‐hydrogen bonds and thus lead to regio‐ and/or stereochemically pure compounds. However, this potential is lowered by their intrinsic low activity and inherent instability. P450‐catalysed biotransformations require a constant supply of NAD(P)H, making the process an expensive one. To render these catalysts more suitable for industrial biocatalysis, the immobilisation of P450 BM‐3 (CYP 102A1) from Bacillus megaterium in a sol‐gel matrix was combined with a cofactor recycling system based on NADP^+^‐dependent formate dehydrogenase (EC 1.2.1.2) from Pseudomonas sp. 101 and tested for practical applicability. This approach was used for the conversion of β‐ionone, octane and naphthalene to the respective hydroxy compounds with DMSO as cosolvent using sol‐gel immobilised P450 BM‐3 mutants.