| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 70137 | Journal of Molecular Catalysis B: Enzymatic | 2012 | 7 Pages |
The endo-inulinase gene (EnIA) from Arthrobacter sp. S37 was ligated into the expression vector pINA1317 and over-expressed in Yarrowia lipolytica Po1h. It was found that the endo-inulinase activity and specific endo-inulinase activity produced by the transformant 1317-EnIA were 16.7 U/mL and 93.4 U/mg, respectively. The recombinant EnIA was purified and characterized. The molecular weight of the purified rEnIA was 78.9 kDa. The optimal pH and temperature of the purified rEnIA were 4 and 50 °C, respectively. The purified rEnIA was stable in the temperature range of 4–40 °C and in the pH range of 2–8. The activity of rEnIA was greatly stimulated in the presence of Li+. The purified rEnIA could actively convert inulin into disaccharides.
Graphical abstractThe purified recombinant endo-inulinase (A) and oligosaccharides produced from inulin by the purified recombinant endo-inulinase (B).Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The endo-inulinase gene (EnIA) from Arthrobacter sp. S37 was over-expressed in Yarrowia lipolytica Po1h. ► The molecular weight of the purified rEnIA was 78.9 kDa. The optimal pH and temperature of the purified rEnIA were 4 and 50 °C, respectively. ► The activity of rEnIA was greatly stimulated in the presence of Li+. ► The purified rEnIA could actively convert inulin into disaccharides.
