PECTIN METHYLESTERASE FROM BOTRYTIS-CINEREA - PHYSIOLOGICAL, BIOCHEMICAL AND IMMUNOCHEMICAL STUDIES

Pectin methylesterase (PME) was purified from the supernatant of Botry tis cinerea strain Bd90. SDS-PAGE showed a single band at 42 kDa, but this band corresponded to two distinct isoforms observed by IEF-PAGE a t pI values of 7.0 and 7.4. PME was produced during the exponential ph ase of fungal growth and independently of the carbon source. Unlike ot her pectinases of B. cinerea, which are polymorphic, no differences we re observed between the PME profiles of 25 strains of different origin s, Polyclonal antibodies were raised against purified PME from B. cine rea, and immunochemical comparisons with PMEs from Erwinia chrysanthem i, Vigna radiata and Glycine max showed the presence of common epitope s between these different enzymes.