Abstract
Abstract Endopolygalacturonic acid lyase, purified from the phytopathogenic bacterium, Erwinia carotovora, induces phytoalexin accumulation in soybean (Glycine max L.) cotyledons. This pectin-degrading enzyme releases heat-stable elicitors of phytoalexin accumulation from soybean cell walls, citrus pectin, and citrus sodium polypectate. The most elicitor-active molecules obtained by treating soybean cell walls with endopolygalacturonic acid lyase have been purified and characterized. The cell-wall-derived elicitors are α-1,4-linked oligogalacturonides with degrees of polymerization of eight to twelve residues. The molecules with the highest specific elicitor activity were identified as α-1,4 -linked deca- and undecagalacturonides that contained 4,5-unsaturated galactosyluronic acid at the nonreducing termini.
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