Purification and properties of a chitinase from Penicillium oxalicum autolysates |
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Authors: | J Rodríguez JL Copa-Patiño MI Pérez-Leblic |
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Institution: | Departamento de Microbiologia y Parasitología, Universidad de Alcaláde Henares, Alcaláde Henares, Madrid, Spain |
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Abstract: | 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°C, respectively. The enzyme was stable at temperatures up to 45°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. |
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