Plant and fungal invertases in grape berries infected with Botrytis cinerea
1992
Ruffner, H.P. | Geissmann, M. | Rast, D.M.
Acid invertases (beta-fructofuranosidases) from berries of Vitis vinifera and from axenically grown Botrytis cinerea were found to differ substantially in their chromatographic behaviour on Concanavalin A-Sepharose. While the partially purified plant enzyme showed low affinity for the lectin and desorbed readily in 0.1 M methylmannoside solution, the interaction of fungal invertase was stable and desorption slow even at 1 M eluant concentrations. Based on this criterion, samples from both organisms were mixed, extracted, and the enzymes re-separated to the point where individual assessments of invertase activities were possible. The recovery factors were subsequently used to quantitate the in vivo contributions of plant and fungal enzyme to sucrose cleavage in immature diseased grapes, extracted 1 week after infection with B. cinerea. Total invertase activities were determined in 20 g (fresh weight) material at the presporulating stage of infection. They amounted to approximately 400 nkat of the grape enzyme and to about 150 nkat of fungal invertase. The role of relative invertase activities attributed to host or pathogen is discussed in relation to the type of phytopathogenic association at hand.
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