CHARACTERIZATION OF ANIONIC SOYBEAN (GLYCINE-MAX) SEED COAT PEROXIDASE

Soybean (Glycine max) seed coats may contain large amounts of peroxida se 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 see ds 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 ca talytic activity towards phenolic substrates including eugenol, caffei c acid, and ferulic acid. Both leaf and stem cationic peroxidases beha ved similarly to seed coat peroxidase in their substrate specificity. Furthermore, using guaiacol as a substrate at various pH levels and te mperatures, soybean seed coat peroxidase had a greater enzyme stabilit y and a wider range of action than other peroxidase enzymes. Polyclona l antibodies raised against cationic peanut peroxidase cross-reacted w ith soybean peroxidase in the presence and the absence of its glycosid ic chains. This suggests homology in epitopes between the soybean and peanut polypeptide and (Or) glycan chains.