PREPARATION AND PROPERTIES OF HORSERADISH PEROXIDASE CROSS-LINKED IN NONAQUEOUS MEDIA

Horseradish peroxidase (hydrogen peroxide oxidoreductase [1.11.1.7]) has been cross‐linked in methylene chloride using N,N'‐carbonyldiimidazole to produce a water insoluble preparation which retains enzymatic activity. Relative to native enzyme, which was treated with methylene chloride but not N,N'‐carbonyldiimidazole, the cross‐linked product displayed significant stability toward denaturation in aqueous mixtures of ethanol, methanol, and 1,4‐dioxane. The cross‐linked product showed a a marked stability toward thermal denaturation relative to the native protein. Applications of the catalyst in chemical reactors for the preparation of synthetic quinones are discussed.