Abstract
Horseradish peroxidase was tested to determine if it catalysed any reaction between coal and hydrogen peroxide. Experiments were performed in aqueous buffers of pH 5.0, 6.5 or 8.0 and used either Wyodak, Beulah Zap, Texas lignite, Mississippi Wilcox lignite or solubilized Mississippi Wilcox lignite. Reactions were monitored by determining the amounts of hydrogen peroxide consumed at various points in time. All coals reacted rapidly with hydrogen peroxide in the absence of peroxidase and these reaction rates increased as pH increased. Horseradish peroxidase did not measurably increase the reaction rates even when present in large concentrations. These data suggest that coal is not a substrate for horseradish peroxidase.
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