Cloning, Expression and Characterization of Xylanase (xyn-akky1) from Bacillus subtilis in Escherichia coli
Yazarlar (4)
Doç. Dr. Sema BİLGİN
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Karamanoğlu Mehmetbey Üniversitesi, Türkiye
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Prof. Dr. İsa GÖKÇE
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
| Makale Türü |
Özgün Makale
|
| Makale Alt Türü | Ulusal alan endekslerinde (TR Dizin, ULAKBİM) yayınlanan tam makale |
| Dergi Adı | Sakarya Üniversitesi Fen Bilimleri Enstitüsü Dergisi |
| Dergi ISSN | 1301-4048 Scopus Dergi |
| Dergi Tarandığı Indeksler | TR DİZİN |
| Makale Dili | İngilizce |
| Basım Tarihi | 12-2018 |
| Cilt No | 22 |
| Sayı | 6 |
| Sayfalar | 1508 / 1517 |
| DOI Numarası | 10.16984/saufenbilder.327153 |
| Makale Linki | http://dx.doi.org/10.16984/saufenbilder.327153 |
| Özet |
| In this study, Bacillus subtilis akky1 strain was isolated from the soil of beech forest in Akkuş City, OrduProvince, Turkey. akky1 strain was identified by 16S rRNA analysis. The full-length 16S rRNA sequenceof akky1 strain showed the 100% similarity with Bacillus subtilis strain B7 (KC310823.1) . A 642 bp DNAfragment was obtained from genomic DNA using primers designed based on the gene sequence of Bacillussubtilis xylanase given in GenBank. The gene encoding xylanase was cloned into pET28b (+) plasmidvector, sequenced and expressed in Escherichia coli BL21 (DE3). The hexahistidine (6xHis) tagged fusionprotein was purified using nickel affinity chromatography and the xylanase activity was measured. Themolecular mass of the purified xylanase was approximately 26 kDa as estimated by SDS-PAGE. Thexylanase had optimal activity at pH 6.0 and 60°C. The Km values of the recombinant enzyme towardsbeechwood was 3.33 mg/ml. |
| Anahtar Kelimeler |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| TRDizin | 1 |
| Google Scholar | 17 |