A novel exopolygalacturonase (EC 188.8.131.52) was purified to apparent homogeneity from cultures of Fusarium oxysporum f. sp, lycopersici on synthetic medium supplemented with polygalacturonic acid, using two, steps of purification preparative isoelectric focusing and cationic exchange chromatography. The enzyme designated PG3 had an apparent M(r) of 63 000 ± 3000 Da upon SDS-PAGE and a p1 of 7.0. PG3 was active with n a broad range of pH from 3 5 to 9. The temperature opt mum was 55°C PG3 hydrolyzed polygalacturonic acid in an exo-manner as demonstrated by analysis of degradation products. The enzyme was N-glycosylated The production of PG3 was constitutive at low levels and synthesis was increased following induction by PGA and partially repressed by glucose.
García Maceira, F. I., Di Pietro, A., & Roncero, M. I. G. (1997). Purification and characterization of a novel exopolygalacturonase from Fusarium oxysporum f.sp. lycopersici. FEMS Microbiology Letters, 154(1), 37–43. https://doi.org/10.1016/S0378-1097(97)00298-X