title: Purification and partial characterization of exopolygalacturonase I from Penicillium frequentans.
abstract: A polygalacturonase with a molecular mass of 74 kDa, an isoelectric point around pH 4.2 and pH--and temperature optima of 3.9 and 50 degrees C, respectively, was purified from a culture fluid of Penicillium frequentans. The enzyme was characterized as an exo-alpha-1,4-polygalacturonase (exo-PG I). Km and Vmax for sodium polypectate hydrolysis were 0.68 g/l and 596.8 U x mg(-1), respectively. The enzyme, a glycoprotein with a carbohydrate content of 81%, is probably the main pectinase of Penicillium frequentans responsible for cleaving monomer units from the non-reducing end of pectin.
authors.affiliation: Departamento de Ciências Farmacêuticas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Brazil.
authors.forename: Maria Angélica
authors.initials: MA
authors.lastname: dos Santos Cunha Chellegatti
authors.forename: Maria José Vieira
authors.initials: MJ
authors.lastname: Fonseca
authors.forename: Suraia
authors.initials: S
authors.lastname: Said
mesh_terms: D001938:Brazil; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D012987:Soil / Q000032:analysis; D012988:Soil Microbiology
chemical_list: D005656:Fungal Proteins; D012987:Soil; D006026:Glycoside Hydrolases; C020136:exopolygalacturonase