| Yazarlar (4) |
Canan Gülmez
Türkiye |
Prof. Dr. Onur ATAKİŞİ
Kafkas Üniversitesi, Türkiye |
Dr. Öğr. Üyesi Kezban YILDIZ DALGINLI
Kafkas Üniversitesi, Türkiye |
Prof. Dr. Emine ATAKİŞİ
Kafkas Üniversitesi, Türkiye |
| 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 … |
| Anahtar Kelimeler |
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale |
| Dergi Adı | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES |
| Dergi ISSN | 0141-8130 Wos Dergi Scopus Dergi |
| Dergi Tarandığı Indeksler | SCI |
| Makale Dili | İngilizce |
| Basım Tarihi | 01-2018 |
| Sayfalar | 436 / 443 |
| Doi Numarası | 10.1016/j.ijbiomac.2017.11.133 |
| Atıf Sayıları | |
| Google Scholar | 33 |
