Partial purification of enzyme myrosinase from Brassica juncea
1998
Prakong Sakorn | Nuansri Rak-ariyatham (Huachiew Chalermprakiat Univ., Bangkok (Thailand). Faculty of Medical Technology. Dept. of Clinical Chemistry)
Myrosinases (EC 3.2.3.1) are a group of isoenzymes present in plants of the Cruciferae family which catalyze the hydrolysis of glucosinolates. Partial purification of myrosinases from defatted mustard powder (Brassica juncea) have been performed by 6 different extracting solvents for 10 minutes. The main component was then isolated by precipitating with 60-90 percent ammonium sulfate. After exttraction of B. juncea myrosinases with 0.01 M phosphate buffer, pH 8.0 at 4 deg C for 10 minutes following by adjustment the medium to pH 6.0 and then dialysis against 0.01 M phosphate buffer, pH 6.0, it was found that the myrosinase activity of the extract was found to be high (3.5 unit per 4 g of mustard powder). When the enzyme extract in phosphate buffer was precipitated by ammonium sulfate, the concentration of 70 percent gave the highest activity of the enzymes.
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