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http://dx.doi.org/10.18419/opus-820
| Autor(en): | Urlacher, Vlada B. Makhsumkhanov, Akhmadjan Schmid, Rolf D. |
| Titel: | Biotransformation of ionones by engineered cytochrome P450 BM-3 |
| Erscheinungsdatum: | 2005 |
| Dokumentart: | Preprint |
| Erschienen in: | Applied microbiology & biotechnology 70 (2006), S. 53-59. URL http://dx.doi.org./10.1007/s00253-005-0028-4 |
| URI: | http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26603 http://elib.uni-stuttgart.de/handle/11682/837 http://dx.doi.org/10.18419/opus-820 |
| Zusammenfassung: | 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. |
| Enthalten in den Sammlungen: | 03 Fakultät Chemie |
Dateien zu dieser Ressource:
| Datei | Beschreibung | Größe | Format | |
|---|---|---|---|---|
| Urlacher_2005.pdf | 113,96 kB | Adobe PDF | Öffnen/Anzeigen |
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