| Autor: |
Pimentel, M. C. B., Krieger, N., Coelho, L. C. C. B., Fontana, J. O., Melo, E. H. M., Ledingham, W. M., Lima Filho, J. L. |
| Zdroj: |
Applied Biochemistry and Biotechnology; October 1994, Vol. 49 Issue: 1 p59-74, 16p |
| Abstrakt: |
A lipases (glycerol ester hydrolases E. C. 3.1.1.3) from a brazilian strain ofPenicillium citrinumhas been investigated. When the microorganism was cultured in the simple medium (1.0% olive oil and 0.5% yeast extract), using olive oil in as carbon source in the inocula, the enzyme extracted showed maximum activity (409 IU/mL). In addition, decrease of yeast extract concentration also reduces the lipase activity. Nevertheless, when yeast extract was replaced by ammonium sulfate, no activity was detected. Purification by precipitation with ammonium sulfate showed best activity in the 40–60% fraction. The optimum temperature for enzyme activity was found in the range of 34–37°C. However, after 30 min at 60°C, the enzyme was completely inactivated. The enzyme showed optimum at pH 8.0. The dried concentrated fraction (after dialysis and lyophilization) maintained its lipase activity at room temperature (28°C) for 8 mo. This result in lipase stability suggests an application of lipases fromP. citrinumin detergents and other products that require a high stability at room temperature. |
| Databáze: |
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