Abstract
By using two columns, DEAE-cellulose and phenyl sepharose CL-4B resins, a homogeneous grape peroxidase could be isolated. The specific activity was increased to nearly 16-fold, and the enzyme gave a single band on gel electrophoresis. The temperature and pH optima of the purified enzyme were 47°C and 6.0, respectively. The apparent Km for guaiacol as a substrate was 1.2 mM at optimum hydrogen peroxide concentration.
- Received September 1982.
- Copyright 1983 by the American Society for Enology and Viticulture
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