Abstract
Two myrosinase isoenzymes ( EC 3. 2. 3. 1 ) were extracted and purified by (NH 4) 2SO 4 precipitation and DEAE-cellulose and Sephadex G-200 chromatography from radish root tissues with M r s 28 800 and 58 900. The most active one (120 U mg −1) was identified and characterized. The yield of the purified myrosinases was 21 mg (2398 U) of pure enzymes from 100 g of dry root tissues. The purity was ascertained by obtaining a single sharp band by disc electrophoresis. Optimal myrosinase activity on sinigrin was recorded in phosphate buffer, pH 6 – 6.5 at 37°. The K m for myrosinase with sinigrin as substrate was 0.47 mM at pH 6. The enzyme was stable for 45 min at 30 and 40° (18% denaturation).
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