A new bacillolycin with serin-protease nature is inhibited by cupper
Yazarlar (2)
Prof. Dr. Bilge Hilal ÇADIRCI Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Mesut Tolan
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Biocatalysis and Biotransformation (Q4) | ||
| Dergi ISSN | 1024-2422 Dergi Bilgileri (2021) | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 02-2021 |
| Kabul Tarihi | 27-01-2021 | Yayınlanma Tarihi | 14-02-2021 |
| Cilt / Sayı / Sayfa | 39 / 4 / 275–282 | DOI | 10.1080/10242422.2021.1884231 |
| Makale Linki | http://dx.doi.org/10.1080/10242422.2021.1884231 | ||
| UAK Araştırma Alanları |
Biyoteknoloji
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| Özet |
| In this study, it is aimed to search for new proteases with novel properties from bacteria and to characterise the properties of the enzyme. The best protease producing microorganisms was isolated from soil and characterised by 16 s rDNA sequence analysis. A 33 kDa molecular weight bacillolycin metallo–serine protease from newly isolated Bacillus sp. BHC01 was purified 2.6–fold with a final 38,617.0 ± 1013.7 U/mg protein specific activity. Optimum reaction temperature and pH of the enzyme was found to be 50° C and pH 7.5, respectively. Fe2+, N+, Co2+ and Mg2+ ions were detected as activators, and Cu2+ metal ions was observed as inhibitors. The kinetic constants of the enzyme Km and Vmax is measured as 0.574 mg/mL, 338.1 mmol/ml.min, respectively. Because ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF), both inhibit the enzyme, it is concluded that this … |
| Anahtar Kelimeler |
| Bacillolycin | metallo-serine protease | organic solvent tolerant | protective effect of Cu +2 |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Google Scholar | 1 |