Glycosidic Enzyme Activity in Pea Tissue and Pea-Fusarium solani Interactions.

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]  L. Hadwiger,et al.  Nuclear changes associated with the host-parasite interaction between Fusarium solani and peas , 1978 .

[2]  L. Hadwiger.  An Evaluation of Pea Histones as Disease Resistance Factors , 1977 .

[3]  C. G. Goff.  Histones of Neurospora crassa. , 1976, The Journal of biological chemistry.

[4]  L. Hadwiger,et al.  Pisatin-inducing components in filtrates of virulent and avirulent Fusarium solani cultures , 1976 .

[5]  L. Hadwiger,et al.  Physiological and Cytological Similarities between Disease Resistance and Cellular Incompatibility Responses. , 1974, Plant physiology.

[6]  G. Pegg,et al.  Chitinase activity in Lycopersicon esculentum and its relationship to the in vivo lysis of Verticillium albo-atrum mycelium , 1973 .

[7]  F. B. Abeles,et al.  Temporal and Hormonal Control of β-1,3-Glucanase in Phaseolus vulgaris L , 1970 .

[8]  D. Smyth,et al.  The determination of glucosamine and galactosamine. , 1970, Analytical biochemistry.

[9]  G. Dixon,et al.  Hyphal lysis and tylose formation in tomato cultivars infected by Verticillium albo-atrum , 1969 .

[10]  J. Howard,et al.  Isolation and characterization of fig lysozyme. , 1969, The Journal of biological chemistry.

[11]  J. Howard,et al.  Studies of the physicochemical and enzymatic properties of papaya lysozyme. , 1967, The Journal of biological chemistry.

[12]  M. Mandels,et al.  β-(1→3) Glucanases from plant callus cultures , 1967 .

[13]  M. Alexander,et al.  Dissolution of fungal cell walls by a streptomycete chitinase and beta-(1-3) glucanase. , 1965, Archives of biochemistry and biophysics.

[14]  R. Powning,et al.  STUDIES ON THE CHITINASE SYSTEM IN BEAN AND OTHER SEEDS. , 1965, Comparative biochemistry and physiology.

[15]  L. Zechmeister,et al.  Über die Chitin‐Spaltung durch Emulsin‐Präparate (III. Mitteil. über enzymatische Spaltung von Polysacchariden) , 1934 .