Please use this identifier to cite or link to this item: http://dx.doi.org/10.18419/opus-813
Authors: Maurer, Steffen Christian
Schulze, Holger
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
Issue Date: 2003
metadata.ubs.publikation.typ: Preprint
metadata.ubs.publikation.source: Advanced synthesis & catalysis 345 (2003), S. 802-810. URL http://dx.doi.org./10.1002/adsc.200303021
URI: http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26527
http://elib.uni-stuttgart.de/handle/11682/830
http://dx.doi.org/10.18419/opus-813
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 1.2.1.2) 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

Files in This Item:
File Description SizeFormat 
Maurer_2003.pdf578,4 kBAdobe PDFView/Open


Items in OPUS are protected by copyright, with all rights reserved, unless otherwise indicated.