In small-scale experiments Aureobasidium pullulans (isolate LS-30) displayed significant antagonistic activity against Botrytis cinerea, Penicillium expansum, Rhizopus stolonifer and Aspergillus niger on table grapes, and B. cinerea and P. expansum on apple fruit. To improve the performance of this yeast-like fungus, possible modes of action were investigated. Competition for nutrients appeared to play a role in the activity of this antagonist. Extracellular exochitinase [N-acetyl-beta -D-glucosaminidase (Nagase)] and beta -1-3-glucanase activities were also detected both in vitro and in apple wounds, which are the main sites of penetration of postharvest fungal pathogens, suggesting that these enzymes may actually be involved in the antagonistic activity of this microorganism. Neither antibiosis nor direct physical interaction of LS-30 cells with the hyphae of B. cinerea appeared to be involved in the activity of this antagonist. (C) 2001 Elsevier Science B.V. All rights reserved.
Aureobasidium pullulans (LS-30) an antagonist of postharvest pathogens of fruits: study on its modes of action
CASTORIA, Raffaello;DE CURTIS, Filippo;LIMA, Giuseppe;
2001-01-01
Abstract
In small-scale experiments Aureobasidium pullulans (isolate LS-30) displayed significant antagonistic activity against Botrytis cinerea, Penicillium expansum, Rhizopus stolonifer and Aspergillus niger on table grapes, and B. cinerea and P. expansum on apple fruit. To improve the performance of this yeast-like fungus, possible modes of action were investigated. Competition for nutrients appeared to play a role in the activity of this antagonist. Extracellular exochitinase [N-acetyl-beta -D-glucosaminidase (Nagase)] and beta -1-3-glucanase activities were also detected both in vitro and in apple wounds, which are the main sites of penetration of postharvest fungal pathogens, suggesting that these enzymes may actually be involved in the antagonistic activity of this microorganism. Neither antibiosis nor direct physical interaction of LS-30 cells with the hyphae of B. cinerea appeared to be involved in the activity of this antagonist. (C) 2001 Elsevier Science B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
