RESUMEN
Generation of superoxide anion (O2-.) and peroxidase activity were significantly increased in bean leaves infected with incompatible and compatible pathogens: Botrytis fabae and Botrytis cinerea, respectively, but the induction was greater on direct inoculation with B. fabae, than with B. cinerea. A slightly higher O2-. level was also detected in the parts of leaves surrounding the inoculation side. Overproduction of O2-. was observed earlier than the increase in peroxidase activity. Pretreatment of the leaves with methyl jasmonate enhanced both O2-. production and peroxidase activity following inoculation with B. cinerea. Induction of superoxide dismutase activity after the infection was less pronounced than changes in O2-. level. The differences in the rate of NADH oxidation in the extracts from control and inoculated leaves, correlated with the differences in the rate of O2-. production. The results indicate that O2-. level is one of the essential factors responsible for the difference in the interactions between bean plant and compatible and incompatible pathogens.
Asunto(s)
Fabaceae/enzimología , Hongos Mitospóricos/aislamiento & purificación , Peroxidasa/biosíntesis , Hojas de la Planta/enzimología , Plantas Medicinales , Superóxido Dismutasa/biosíntesis , Superóxidos/metabolismo , Fabaceae/microbiología , Hongos Mitospóricos/patogenicidad , Hojas de la Planta/microbiologíaRESUMEN
It was found that the acid protease of Fusarium culmorum can hydrolyze various proteins of plant origin including polygalacturonase inhibitor from bean (BPI) and soybean trypsin inhibitor (STI). The highest hydrolysis extent of BPI and STI by the enzyme was only 5% and 3% respectively. The partially hydrolyzed BPI lost its inhibition ability to fungal polyglacturonases. Similarly, the partially hydrolyzed STI lost its inhibition ability to trypsin and fungal alkaline protease. The F. culmorum acid protease showed broad substrate specificity towards synthetic dipeptides.