Ppo

v2o2

also causes the oxidative degradation of carotene to volatile products, such as ionone and 5,6-epoxy-/?-ionone.

The polymerization of o-quinone to polyaromatic pigments requires water in the reaction components. The effort to stabilize the quinone for the purpose of regiospecific oxidation of the aromatic compounds has been attempted. Polyphenol oxidase has been found to function in chloroform whereby phenol substrates can be converted to stable quinone, which can be quantitatively reduced to catechols (47-49).

Glucose oxidase (EC1.1.3.4) is a food enzyme used for the removal of glucose to prevent the Maillard reaction in egg solids, dried meats, potatoes, and so on. When coupled with catalase, it is used for the removal of oxygen from the head space of packaged foods. The enzyme is also used in the production of gluconic acid, and for the quantitative determination of D-glucose in food, agricultural, and pharmaceutical products (50-52). The enzyme catalyzes the irreversible oxidation of a number of sugars to the corresponding lactones. Common substrates include glucose, deoxyglucose, mannose and galactose.

The enzyme is a dimer containing flavin adenine dinu-cleotide (FAD) as cofactor. In the reaction, the substrate is oxidized to the lactone while the FAD is reduced to FADH2 (Scheme 10). In a subsequent step, the lactone is nonen-zymatically hydrolyzed to gluconic acid, and the reduced enzyme is reoxidized (53).

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