| Yazarlar |
Didem Yıldırım
Türkiye |
Dr. Öğr. Üyesi Cem ÖZİÇ
Türkiye |
Dr. Öğr. Üyesi Yunus ENSARİ
Kafkas Üniversitesi, Türkiye |
| 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 |
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale |
| Dergi Adı | CHEMBIOCHEM |
| Dergi ISSN | 1439-4227 |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Dergi Grubu | Q3 |
| Makale Dili | Türkçe |
| Basım Tarihi | 06-2023 |
| Cilt No | 24 |
| Sayı | 12 |
| Doi Numarası | 10.1002/cbic.202300065 |
| Makale Linki | http://dx.doi.org/10.1002/cbic.202300065 |
| Atıf Sayıları | |
| WoS | 1 |
| SCOPUS | 1 |
| Google Scholar | 1 |
