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SEPARATION ,PURIFICATION AND PARTIAL CHARACTERIZATION OF LYSOZYME FROM CAULIFLOWER | ||
| The Iraqi Journal of Agricultural Science | ||
| Article 1, Volume 40, Issue 2, 2009, Pages 111-119 | ||
| Authors | ||
| S.M. Abdul; | ||
| Abstract | ||
| This study was aimed to separate cauliflower lysozyme by using different extraction solutions, after primry experiences it was found that 0.2 M phosphate buffer pH (6.5) is the best one for extraction because the specific activity for the enzyme reached 10.9 unit/mg comparison with other extraction solutions. primary purification of the enzyme was done by concentrating the crude extract using ammonium sulphate at 60% saturation, then dialyzed aginst phosphate buffer to remove the salts . followed by appling the dilayzed concentrate on ion exchange chromatography on the cation exchange column Duolite C-464 .The results of partial purification pointed out that the enzyme yield and purification folds and specific activity were 58.2% and 7.7 times and 43.3 unit/mg respectively. The results of enzyme partial characterization showed that the optimum pH for the enzyme activity was 6, and the enzyme was most stable at pH values ranged between 5.5 - 6 . At optimization the optimum temperature for activity the enzyme exhibited the maximum activity at 60 oC at temperature degrees ranged between 30 to 80 oC while the study of heat stability pointed out that the enzyme retained almost its entire activity over 15 min incubation at 50-65 oC at pH 6 and 92% from its original activity at 70 oC . | ||
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