Expression and Characterization of a New Self‐Sufficient P450 Monooxygenase (P450 AZC1) from Azorhizobium caulinodans
Yazarlar (3)
Didem Yıldırım
Kafkas Üniversitesi, Türkiye
Dr. Öğr. Üyesi Cem ÖZİÇ
Kafkas Üniversitesi, Türkiye
Dr. Öğr. Üyesi Yunus ENSARİ
Kafkas Üniversitesi, Türkiye
| Makale Türü |
Özgün Makale
(SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
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| Dergi Adı | Chembiochem (Q3) | ||
| Dergi ISSN | 1439-4227 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | Türkçe | Basım Tarihi | 06-2023 |
| Cilt / Sayı / Sayfa | 24 / 12 / – | DOI | 10.1002/cbic.202300065 |
| Makale Linki | http://dx.doi.org/10.1002/cbic.202300065 | ||
| Özet |
| Oxyfunctionalization of non-activated carbon bonds by P450 monooxygenases has drawn great industrial attraction. Self-sufficient P450s containing catalytic heme and reductase domains in a single polypeptide chain offer many advantages since they do not require external electron transfer partners. Here, we report the first P450 enzyme identified and expressed from Azorhizobium caulinodans. Firstly, expression conditions of P450 AZC1 were optimized for enhanced expression in E.coli. The highest P450 content was obtained in E.coli Rosetta DE3 plysS when it was incubated in TB media supplemented with 0.75 mM IPTG, 0.5 mM ALA, and 0.75 mM FeCl3 at 25 °C for 24 hours. Subsequently, the purified enzyme showed a broad substrate spectrum including fatty acids, linear and cyclic alkanes, aromatics, and pharmaceuticals. Finally, P450 AZC1 showed optimal activity at pH 6.0 and 40 °C and a broad pH and temperature profile, making it a promising candidate for industrial applications. |
| Anahtar Kelimeler |
| Azorhizobium caulinodans | cytochrome P450 | CYPs | heterologous expression | self-sufficient monooxygenase |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| WoS | 2 |
| SCOPUS | 3 |
| Google Scholar | 2 |