| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6531348 | Journal of Molecular Catalysis B: Enzymatic | 2013 | 6 Pages |
Abstract
- Biochemical properties of Streptomyces sp. SK glucose isomerase SKGI and its two recombinant forms were compared.
- Native SKGI was the most thermostable compared to the two recombinant enzymes.
- His tagged SKGI is less thermostable/thermoactive than untagged recombinant SKGI.
- Possible O-glycosylation of native SKGI (8%) at position Thr6 and/or Thr30.
- The His tag is located at the dimerization interface promoting the dimer dissociation.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Hajer Ben Hlima, Dorra Ayadi, Nushin Aghajari, Samir Bejar,