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ResearchPaper zugänglich unter
URN: urn:nbn:de:bsz:93-opus-26603
URL: http://elib.uni-stuttgart.de/opus/volltexte/2006/2660/
Biotransformation of ionones by engineered cytochrome P450 BM-3
Urlacher, Vlada B. ;
Makhsumkhanov, Akhmadjan ;
Schmid, Rolf D.
Originalveröffentlichung:
(2005) Applied Microbiology & Biotechnology (2005), Jul 7, 1-7 Medline
pdf-Format:
Dokument 1.pdf (114 KB)
SWD-Schlagwörter:
Cytochrom P-450 , Monooxygenasen , Biokatalyse , Biokonversion , Biotransformation , Hydroxylierung , Mutagenese , Genbibliothek
Freie Schlagwörter (Englisch):
P450 BM-3 , beta-ionone , regioselectivity , mutagenesis , gene library
Institut:
Institut für Technische Biochemie
DDC-Sachgruppe:
Chemie
Dokumentart:
ResearchPaper
Sprache:
Englisch
Erstellungsjahr:
2005
Publikationsdatum:
01.06.2006
Kurzfassung auf Englisch:
Wild type cytochrome P450 monooxygenase from Bacillus megaterium (P450 BM-3) has low activity for the hydroxylation of beta-ionone (>1 min-1). Substitution of phenylalanine by valine at position 87 increased the beta-ionone hydroxylation activity up to 100-fold (115 min-1). For further activity improvement methods of site-directed and random mutagenesis were applied. The R47L Y51F F87V mutant, designed by site-directed mutagenesis and the A74E F87V P386S mutant, obtained after two rounds of error-prone PCR, exhibit an increase in activity up to 300-fold compared to the wild type enzyme. All mutants converted -ionone regioselectively to 4-hydroxy-beta-ionone.
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