Characterization of anionic soybean (Glycine max) seed coat peroxidase

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.

Purification and characterization of cell wall-bound peroxidase from vanilla bean

“…POD separated from vanilla bean showed 15 g/100 g carbohydrate content. Compared to other studies, the carbohydrate content of POD was similar to that of turnip roots (9.1 g/100 g) (Duarte-Vazquez et al, 2001), Korean radish (9-14 g/100 g) (Lee & Kim, 1994), soybean (15%) (Schmitz, Gijzen, & Van Huystee, 1997), acidic turnip roots (18 g/100 g) (Duarte-Vazquez, Whitaker, Rojo-Domı´nguez, Garcia-Almenda´rez, & Regalado, 2003), but different from that of the peanut (22 g/100 g) (Hu & Van-Huystee, 1989) and palm leaf (37 g/100 g) (Deepa & Arumughan, 2002).…”

Effects of ageing on peroxidase activity and localization in radish (Raphanus sativus L.) seeds

“…In artificially aged peanut seeds, peroxidase activity has been measured separately in cotyledons and embryo axis, the latter being found to have most of the activity Sung and Jeng, 1994). Some POD activity has been detected in the husk and in the transparent or green layer of the pericarp of barley (Cochrane et al, 2000) and in the integument of Brassica juncea (Le Beller et al, 1986) and soybean (Schmitz et al, 1997). In imbibed Brassica oleracea seeds, enzyme activity measured in the integument and in the cotyledons was higher than in the embryo axis at the start of imbibition (Bellani et al, 2002).…”

Lignin content and peroxidase activity in soybean seed coat susceptible and resistant to mechanical damage

“…Soy bean peroxidase is a 37 kD glycoprotein ex pressed in the seed coat approx i mately 20 days af ter anthesis (Gillikin and Gra ham 1991). Seed coat tis sues may ac cu mu late large amounts of peroxidase in the hour glass cells of the sub-epi der mis and may rep re sent at least 5 % of the pro tein in the dry seed coat (Schmitz et al 1997). This ac cu mu la tion is de pend ent upon the pres ence of a sin gle dom i nant gene Ep (Buzzel and But tery 1969).…”