EXTRACTION, PARTIAL PURIFICATION AND CHARACTERIZATION OF SOME  PROPERTIES OF  CARROT  INVERTASE

	EXTRACTION, PARTIAL PURIFICATION AND CHARACTERIZATION OF SOME PROPERTIES OF CARROT INVERTASE
AL-TAQANI
Article 1, Volume 24, Issue 5, 2011, Pages 0-0
Abstract
This research aimed at extraction, purification and determination of some properties of Iraqi carrot (Daucus carota) invertase . Partial purification of the enzyme was done by two steps including concentrating the crude extract by precipitation with acetone at the ratio 1:2 . To complete the purification process separation was made using gel filtration chromatography through Sephadex G-100.The results of partially purified invertase revealed that the enzyme yield ,purification folds and specific activity at the last step were 8.6% and 2.125 times and 1.186 unit/mg , respectively. The results of characterization of partially purified enzyme pointed out that the optimum pH for the enzyme activity was 6 , and it was most stable and retained its full activity for 15 min incubation at pH range of 5-7, which means that the enzyme was stable at the neutral and acid near neutral medium . The optimum temperature for maximum invertase activity was 45 C. The determination of heat stability showed that the enzyme retained almost its entire activity for 15 min incubation at 15 to 50 C , which means that it is stable at a broad range of temperature . Upon examining the effects of some chemical compounds on invertase activity a complete inhibiton was observed upon the addition of HgCl2 to the reaction medium and the enzyme activity was reduced obviously due to the addition of CuSO4 , while addition of CaCl2 did not show any effect on the enzyme activity.

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