Abstract
The addition of 10-2 to 10-3M L-ascorbic acid to the reaction medium was found to greatly promote the white mustard myrosinase activity under the condition (pH 6.4), producing neither white turbidity nor hydrogen sulfide. The amount of the white turbidity and hydrogen sulfide produced on addition of ascorbic acid to the reaction mixture of myrosinase and sinigrin increased with the decrease of the pH value of the medium. Any of those materials was produced in a larger amount in the case of white mustard enzyme than in the case of mold enzyme. The material producing white turbidity was found to be composed mainly of protein. It may be concluded that ascobic acid is a specific activator of myrosinase.
