| Autor: |
Krieger, N., Taipa, M. A., Melo, E. H. M., Lima-Filho, J. L., Aires-Barros, M. R., Cabral, J. M. S. |
| Zdroj: |
Applied Biochemistry and Biotechnology; July 1997, Vol. 67 Issue: 1-2 p87-95, 9p |
| Abstrakt: |
A lipase from a wild strain ofPenicillium citrinumwas encapsulated in AOT/isooctane-reversed micelles, and the kinetic parameters were studied relative to triolein hydrolysis. Lipolytic activity was strongly dependent on the water amount in the system (Wo) and presented a bell-shaped curve for this parameter, with a maximum in the range of Wo10–15. Optimum conditions for enzyme activity were pH 8.0 and 45‡C. The influence of substrate concentration was also studied. The enzyme showed a Michaelis-Menten behavior and the apparent kinetics constants were calculated as beingVmax.app.- 120 U/mg and Kmapp= 49.2 mM. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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