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Purification and properties of a chitinase from Penicillium oxalicum autolysates
Author(s) -
Rodríguez J.,
CopaPatiño J.L.,
PérezLeblic M.I.
Publication year - 1995
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1995.tb00404.x
Subject(s) - chitinase , chromatography , size exclusion chromatography , chitin , chemistry , substrate (aquarium) , ammonium sulfate precipitation , enzyme , ammonium , gel electrophoresis , enzyme assay , polyacrylamide gel electrophoresis , electrophoresis , biochemistry , biology , chitosan , ecology , organic chemistry
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 K m was 2.5 mg ml ‐1 for colloidal chitin, Hg 2+ and Ag + were effective inhibitors. The viscosimetric study carried out using carboxymethyl chitin as substrate revealed the endotype action of this enzyme.