Purification and partial characterization of exopolygalacturonase I from Penicillium frequentans.
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.
dos Santos Cunha Chellegatti
Maria Angélica
MA
Departamento de Ciências Farmacêuticas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Brazil.
Fonseca
Maria José Vieira
MJ
Said
Suraia
S
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
D005656:Fungal Proteins; D012987:Soil; D006026:Glycoside Hydrolases; C020136:exopolygalacturonase