Abstract
Soybean (Glycine max) seed coats may contain large amounts of peroxidase enzyme. The release of peroxidase from whole seeds upon imbibition and the catalytic and antigenic properties of this enzyme were studied. Comparisons between high (Ep) and low (epep) peroxidase activity seeds demonstrated a lengthy (336 h) release of anionic peroxidase by Ep (Harovinton) cultivars following incubation in an aqueous environment. In its purified state, soybean seed coat peroxidase exhibited good catalytic activity towards phenolic substrates including eugenol, caffeic acid, and ferulic acid. Both leaf and stem cationic peroxidases behaved similarly to seed coat peroxidase in their substrate specificity. Furthermore, using guaiacol as a substrate at various pH levels and temperatures, soybean seed coat peroxidase had a greater enzyme stability and a wider range of action than other peroxidase enzymes. Polyclonal antibodies raised against cationic peanut peroxidase cross-reacted with soybean peroxidase in the presence and the absence of its glycosidic chains. This suggests homology in epitopes between the soybean and peanut polypeptide and (or) glycan chains. Key words: cross-reactivity, enzyme activity, peroxidase, polymerization, substrate.
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