Purification and properties of a chitinase from Penicillium oxalicum autolysates.
A chitinase (EC. 3.2.1.14) from autolysed culture filtrate of Penicillium oxalicum was purified by precipitation with ammonium sulphate, gel filtration and ion exchange chromatographies. The purified enzyme showed a single protein band in SDS gel electrophoresis. The enzyme is an acidic protein with a pI of 4.5 and has a molecular weight of 54,900 as estimated from SDS gel electrophoresis and 21,500 from gel filtration. The optimum pH and temperature were 5.0 and 35 degrees C, respectively. The enzyme was stable at temperatures up to 45 degrees C and in a pH range between 4.0 and 6.0. The Km was 2.5 mg ml-1 for colloidal chitin, Hg2+ and Ag+ were effective inhibitors. The viscosimetric study carried out using carboxymethyl chitin as substrate revealed the endotype action of this enzyme.
Rodríguez
J
J
Departamento de Microbiología y Parasitología, Universidad de Alcalá de Henares, Madrid, Spain.
Copa-Patiño
J L
JL
Pérez-Leblic
M I
MI
D001329:Autolysis / Q000201:enzymology; D002688:Chitinases / Q000737:chemistry* / Q000302:isolation & purification*; D007526:Isoelectric Point; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*
D002688:Chitinases