A novel detergent additive: Organic solvent- and thermo-alkaline-stable recombinant subtilisin
Yazarlar (4)
Canan Gülmez
Prof. Dr. Onur ATAKİŞİ Kafkas Üniversitesi, Türkiye
Doç. Dr. Kezban YILDIZ DALGINLI Kafkas Üniversitesi, Türkiye
Prof. Dr. Emine ATAKİŞİ Kafkas Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES (Q1) | ||
| Dergi ISSN | 0141-8130 Dergi Bilgileri (2018) | ||
| Dergi Tarandığı Indeksler | SCI | ||
| Makale Dili | İngilizce | Basım Tarihi | 01-2018 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 01-03-2018 |
| Cilt / Sayı / Sayfa | – / 0 / 436–443 | DOI | 10.1016/j.ijbiomac.2017.11.133 |
| Makale Linki | https://linkinghub.elsevier.com/retrieve/pii/S0141813017333421 | ||
| UAK Araştırma Alanları |
Veteriner Biyokimyası
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| Özet |
| In the present work, subtilisin gene from Bacillus subtilis PTTC 1023 was synthesized, cloned into the vector pD441-NH and expressed in E. coli BL21 (DE3). Recombinant subtilisin was purified in a single-step procedure by affinity chromatography. The molecular mass of the purified protein was determined to be about 40 kDa by SDS-PAGE. The optimum pH and temperature values of its proteolytic activity were 10.5 and 50 °C, respectively and retained more than 70% and 89% of its activity in pH range of 7–12 and 30–60 °C, respectively. Enzyme purity was estimated to be about 200- fold greater than that of the crude extract and subtilisin had a specific activity of 56.16 U/mg, with a yield of about 87.9%. It was completely inhibited by phenylmethanesulfonyl fluoride, which strongly suggests its belonging to serine protease family. Interestingly, subtilisin protease displayed a significant compatibility with commercial … |
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BM Sürdürülebilir Kalkınma Amaçları
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| Google Scholar | 35 |