Purification and properties of an alkaline protease of <Emphasis Type="Italic">Aspergillus clavatus</Emphasis> |
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| Authors: | C R Tremacoldi R Monti H S Selistre-De-Araújo E C Carmona |
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| Institution: | 1.Phytopathology Laboratory,Embrapa Amaz?nia Oriental,Belém,Brazil;2.Food and Nutrition Department,Faculdade de Ciências Farmacêuticas,Araraquara,Brazil;3.Physiology Department,S?o Carlos,Brazil;4.Biochemistry and Microbiology Department,Universidade Estadual Paulista “Júlio deMesquita Filho”-UNESP,Rio Claro,Brazil |
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| Abstract: | An extracellular alkaline serine protease has been purified from a strain of Aspergillus clavatus, to apparent homogeneity, by ammonium sulfate precipitation and chromatography on Sephadex G-75. Its molar mass, estimated
by SDS-PAGE, was 35 kDa. Maximum protease activity was observed at pH 9.5 and 40°C. The enzyme was active between pH 6.0 and
11.0 and was found to be unstable up to 50°C. Calcium at 5 mM increased its thermal stability. The protease was strongly inhibited
by PMSF and chymostatin as well as by SDS, Tween 80 and carbonate ion. Substrate specificity was observed with N-p-Tos-Gly-Pro-Arg-p-nitroanilide and N-Suc-Ala-Ala-Ala-p-nitroanilide being active substates. Parts of the amino acid sequence were up to 81% homologous with those of several fungal
alkaline serine proteases. |
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| Keywords: | Alkaline protease Aspergillus clavatus Characterization Enzyme purification Sequence |
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