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Plant Physiology 66:199-204 (1980)
© 1980 American Society of Plant Biologists

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Articles

Glycosidic Enzyme Activity in Pea Tissue and Pea-Fusarium solani Interactions 1,2

Everett J. Nichols, Jean M. Beckman and Lee A. Hadwiger

Department of Plant Pathology, Washington State University, Pullman, Washington 99164

Membrane barriers which prevent direct contact between Fusarium solani and pea endocarp tissue prevent fungal spores from inducing phytoalexin production. Conversely, preinduced host resistance responses are not readily transported from the plant across the membrane barrier to Fusarium macroconidia.

Crude enzyme extracts from pea endocarp tissues partially degrade Fusarium solani f. sp. phaseoli cell walls. Activities of the glycosidic enzymes, chitinase, {beta}-1,3-glucanase, chitosanase, {beta}-D-N-acetylglucosaminidase, {beta}-D-N-acetylgalactosaminidase, {beta}-D-glucosidase, {alpha}-D-glucosidase, and {alpha}-D-mannosidase, were detected in pea endocarp tissue. If pods are challenged with Fusarium spores or chitosan, the chitinase activity of the infected tissue remains higher than water-treated pods 0.5 to 6 hours after treatment. The {beta}-1,3-glucanase activity increases within 6 hours in both inoculated and control tissue. Chitosanase activity was lower in tissue treated with Fusarium solani f. sp. pisi, f. sp. phaseoli or chitosan than in water-treated control tissue. Thus, the pea tissue contains glycosidic enzymes with the potential to degrade the major compounds of the Fusarium cell walls.

1 This research was supported in part by National Science Foundation Grant PCM-7712924.

2 Scientific Paper No. 5439, College of Agriculture Research Center, Washington State University, Pullman, Washington.






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Copyright © 1980 by the American Society of Plant Biologists