Four types of polyphenol oxidase were isolated from the crude extract of a Ligularia fischeri by gel filtration on Sephadex G-150. Optimum pH and temperature for the activity of partially purified enzyme were 7.5 and 25¡É, respectively. It was stable at temperature 40¡Éwhen examined at pH 7.5 for ;i min, and lost 90% of its activity at 70¡É in 30 min at pH 7.5. The enzyme has good activity on catechol and chlorogenic acid but was inactive on dopamine(Received 3, March, 1992, accepted 6, May 1992).
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