ABSTRACT
Lipase activity was assayed in mature Caesalpinia bonducella L. seeds using olive oil emulsion stabilized with 10% gum acacia as a substrate. The maximum lipase activity at pH 7.0 and at 30 EC and the pH stability was found in between 6-7.5. Lipase activity was fairly stable up to 60 EC and retaining 90% activity. Whereas lipase activity was completely lost at 90 EC within 10 minutes. C. bonducella L. seeds was found most specific towards coconut oil and lipase activity was slightly increased in the presence of calcium but enzyme activity was decreased by the addition of sodium deoxycholate, Tween 80 and Triton X-100.
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How to cite this article
Vajanti Mala Pahoja, M.Umar Dahot and Mumtaz Ali Sethar, 2001. Characteristic
Properties of Lipase from Crude Extract of Caesalpinia bonducella
L. Seeds. Journal of Biological Sciences, 1: 775-778.
DOI: 10.3923/jbs.2001.775.778
URL: https://scialert.net/abstract/?doi=jbs.2001.775.778
DOI: 10.3923/jbs.2001.775.778
URL: https://scialert.net/abstract/?doi=jbs.2001.775.778
REFERENCES
- Lowry, O.H., N.J. Rosebrough, A.L. Farr and R.J. Randall, 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem., 193: 265-275.
CrossRefPubMedDirect Link - Boland. W., C. Frobl and M. Lorenz, 1991. Estrolytic and lipolytic enzymes in organic synthesis. Synthesis, 12: 1049-1072.
Direct Link - Maschima, M. and H. Beevers, 1985. Purification and properties of glyoxysomal lipase from castor bean. Plant Physiol., 79: 489-493.
Direct Link - Savendsen, A., 2000. Lipase protein engineering. Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol., 1543: 223-238.
CrossRefPubMedDirect Link