EC Number   |
General Stability |
Reference |
|---|
   1.1.99.28 | enzyme activity loss in pineapple juice is even stronger (18%) than in 0.5 M sugar solution |
724873 |
| 1.1.99.28 | glucose-fructose oxidoreductase (GFOR)/glucono-delta-lactonase (GL) enzyme complex immobilized on Ca-alginate is stable for at least 23 cycles |
762807 |
| 1.1.99.28 | guanidinium hydrochloride inactivates by induction of structural transitions that are comparable to that observed during substrate turnover. This leads to time-dependent formation of high-order associates and consequently inactivation |
10909 |
| 1.1.99.28 | in absence of substrates or in presence of only one substrate, either fructose or glucose, the enzyme is fully stable |
10908 |
| 1.1.99.28 | inactivation during substrate conversion |
10911, 10912 |
| 1.1.99.28 | inactivation during substrate turnover. The process of inactivation is triggered by structural transitions that are induced by the lactone product and involves aggregation as the ultimate cause of irreversible inactivation |
10909 |
| 1.1.99.28 | the interaction of the enzyme with the aldonolactone product triggers a sequential process that affects the protein structure conformationally and chemically and, ultimately, results in an irreversible loss of activity |
10903 |
| 1.1.99.28 | thiol reagents stabilize. Dithiothreitol is the most efficient, 5-15 mM |
10908, 10911, 10912 |
| 1.1.99.28 | urea, 1.0 M, prevents the formation of high-order associates and increases the half-life under operational conditions 10fold |
10909 |
