Abstract

A glucose oxidase-catalase enzyme system was tested thoroughly for an extended period with a number of samples. Oxygen was rapidly scavenged in white table and rosé wines with residual glucose. Evidence indicates that most of the hydrogen peroxide formed by the glucose oxidase is reduced by the sulfur dioxide rather than the catalase. If the sulfur dioxide is low, however, the catalase is necessary to prevent browning. Conditions which appear to optimize effective maintenance of wine quality by the enzyme treatment are lower pH and medium sulfur dioxide content. The color and aldehyde content are not affected by the enzyme treatment under usual conditions. Ethanol does not affect rate of oxygen removal by the enzyme system. The lower pH9s will reduce the rate slightly.

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