Abstract
Botrytis cinerea Pers. added to fermenting musts or white wines alters the sensory characteristics of the product. Analysis of wines made in the presence of Botrytis preparations revealed higher residual sugar in addition to higher alcohol and acid. Extracts made from lyophilized B. cinerea were examined for oxidoreductase activity, Two enzymes surviving treatment with 10-20% alcohol were glucose 6-phosphate-NADP dehydrogenase and a NADH-sensitive phenol oxidase. The latter assayed for benzidine dimerase activity exhibited properties which implicated its participation in wine decoloration by freeze-dried B. cinerea powders. Investigation of the kinetic and electrophoretic behavior of benzidine dimerase indicated a response to several classical inhibitors, particularly sodium fluoride, and provided evidence that the enzyme exists in three molecular forms or isoenzymes. The advantages of using enzymes from B. cinerea grown separately from the grape for modifying bland white wines are discussed.
- Accepted October 1968.
- Published online January 1968
- Copyright 1968 by the American Society for Enology and Viticulture
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