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Abstract ▼ AI-Helper

The purification of myrosinase from radish roots was performed using Concannavalin A-Sepharose affinity chromatography and gel permeation HPLC, which gave a 22-fold-purification(S.P.A.=39,000 units/mg) with 50% recovery, SDS-polyacrylamide gel electrophoresis showed a single major band, suggestive o...

The purification of myrosinase from radish roots was performed using Concannavalin A-Sepharose affinity chromatography and gel permeation HPLC, which gave a 22-fold-purification(S.P.A.=39,000 units/mg) with 50% recovery, SDS-polyacrylamide gel electrophoresis showed a single major band, suggestive of a relatively pure myrosinase, and the M.W. of the enzyme determined on gel permeation HPLC was ca. 124K. The enzyme showed on optimum pH of 6.5 and was stable at pH 6 to 7 at room temperature, but unstable below pH 4. The enzyme possessed an optimum temperature of $37^{\circ}C$, and gave a Vmax value of $40\;{\mu}moles/mg{\cdot}min$ and a Km value of 0.12mM for sinigrin. The purified myrosinase was activated maximally by 0.6mM of ascorbic acid, but somewhat inhibited by more than 2 mM ascorbic acid. The activities of myrosinase present in the peelings and the peeled radish amounted to approximately 1,333 units/g and 140 units/g weight, respectively and the peelings contained much more myrosinase activity than the peeled radish.

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