Mono and bi-cationic influence on the enzymatic activity of many oxidoreductaze enzymes

This research aims to study the effects of some oxidoreductase enzymes activity in the seedlings of maize plant stem cells, which Cultured in the present of the following cations: Na+, K+, Mg2+, and Ca2+. (GHOTA 82) yallow corn seeds were used, and cultured for six days in water and in solution of cations with different concentrations. In brief, preparation and titration processes consist of extraction of enzymatic solutions from plant stem cells seedlings by buffer solutions (at appropriate PH for each enzyme). The results show that the activity of used enzymes increases with the increasing concentrations of the used cations from 1 to 6 g/l by comparison with those of cultured samples in water. Besides the difference in the effect of cations was limited by the concentrations range between 6-9 g/ l.

Characterization of β-galactosidase which was Isolated from New Born Goat Brain

Some characteristics of β-galactosidase enzyme that was isolated from a new born goat brain were studied. This study concluded that the enzyme is glucoenzyme in which the carbohydrate part constitutes 22.1% in accordance with phenol –sulfate acid method. The optimum pH for the enzyme activity is 5.5. The enzyme lost its activity completely at pH8.5, and showed great stability at the range of pH 4-6. The results indicated that the optimum temperature for the enzyme activity is 55Co at the optimum pH. The stability temperature for the enzyme is 35-60Co. The analytical results of 5%lactose solution hydrolyzed by the enzyme have indicated that the hydrolysis rate is between 40% after 60 minutes, to 95% after 270 minutes.

Isolation and Purification of β-galactosidase From New Born Goat Brain

β-galactosidase enzyme was isolated from the new born goat brain by nine methods, It was found that the sodium acetate 0.2 Mole/Liter +0.2Mole/Liter NaCl PH5 method have given the highest specific activity of crude enzyme in comparison with the other methods. Also, this enzyme was purified by using four methods, the second one (cold acetone) was the butter. As a result the purification fold was about 135.46 times and the yield about 77.14% by using Sephacryl S200 (second step). This enzyme is 187.437 KDa as a molecular weight.