Please use this identifier to cite or link to this item: http://dx.doi.org/10.18419/opus-813
|Authors:||Maurer, Steffen Christian|
Schmid, Rolf D.
Urlacher, Vlada B.
|Title:||Immobilisation of P450 BM-3 and an NADP+ cofactor recycling system : towards a technical application of heme-containing monooxygenases in fine chemical synthesis|
|metadata.ubs.publikation.source:||Advanced synthesis & catalysis 345 (2003), S. 802-810. URL http://dx.doi.org./10.1002/adsc.200303021|
|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 NADPƒy-dependent formate dehydrogenase (EC 22.214.171.124) from Pseudomonas sp. 101 and tested for practical applicability. This approach was used for the conversion of £]-ionone, octane and naphthalene to the respective hydroxy-compounds with DMSO as cosolvent using sol-gel immobilised P450 BM-3 mutants.|
|Appears in Collections:||03 Fakultät Chemie|
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