Abstract
Polyphenol oxidase (EC 1.10.3.1) was extracted from an acetone powder prepared from Koshu grapes. The enzyme was purified 172-fold by ammonium sulfate fractionation followed by three successive column chromatographies on O-(carboxymethyl) cellulose, O-(diethylaminoethyl) cellulose and hydroxylapatite. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis. The molecular weight of this enzyme was estimated to be 39 000 - 41 000 by gel filtration and sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the enzyme molecule had no subunit. The temperature and pH optima were 25°C and 6.0, respectively. The enzyme was stable in the alkaline pH range (between pH 7.0 and pH 11.0) and at temperatures up to 30°C. The enzyme exhibited high activity toward o-diphenolic compounds and showed no activity toward monophenols.
- Received August 1982.
- Copyright 1983 by the American Society for Enology and Viticulture
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