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.

Extraction and Purification of Lipoxygenase From Peanut Seed Arachis hypogaea. L

The study included the selection of the best methods to extract the enzyme among nine methods. The protein content was concentrated and precipitated by cold acetone among other five methods of concentration (partial purification). The purification stages were achieved by using ion exchange column chromatography (DEAE – Sephadex A 50 column). Followed by gel filtration chromatography using sephacryl S-300. The active parts were lyophlizated (free drying) to obtain Lipoxygenase with 43.18% yield and 8.16 folds of purification and specific activity of 1162.9 unit / mg. The purity of enzyme was confirmed by poly acryl amide gel electrophoresis under non denaturing conditions, with the appearance a single band .