ISOLATION, PURIFICATION AND PARTIAL CHARACTERIZATION OF LYSOZYME FROM CALOTROPIS PROCERA

M. Abdul-Rahman, S.; A . Shaker, K.; K Dalaly, B.

	ISOLATION, PURIFICATION AND PARTIAL CHARACTERIZATION OF LYSOZYME FROM CALOTROPIS PROCERA
The Iraqi Journal of Agricultural Science
Article 1, Volume 37, Issue 2, 2006, Pages 97-104
Authors
S. M. Abdul-Rahman; K. A . Shaker; B. K Dalaly
Abstract
Lysozyme of Calotropis procera latex was isolated and purified by using ion exchange chromatography on the cation exchange column Duolite-C464, followed by gel fdtration on Sephadex G-75 column. Purification folds and the enzyme yield were 4.054 and 38.89% , respectively. Purity of obtained enzyme was tested by polyacrylamide gel electrophoresis in the absence of sodium dodecyl sulfate and indicated that it has been purified to homogensity by giving a single band. The results of enzyme characterization showed that the molecular weights were 23000, 26302 dalton as determined by gel electrophoresis in the presence of SDS filtration . The optimum pH for the enzyme activity was 4.5 and it was most stable at pH values ranged between 3.5 and 5.5. The enzyme exhibited the maximum activity at 50 °C. . The study of heat stability pointed out that the enzyme retained its entire activity over 15 min incubation at 25-35 °C, and it remained active even when incubated at 20-80 °C.

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