Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus

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Abstract

An elastinolytic proteinase of Aspergillus flavus has been isolated to homogeneity, and its physical and biochemical properties have been characterized. Two purification protocols were compared; an initial step of ion-exchange chromatography was found to be equivalent to ammonium sulfate precipitation at neutral pH. A combination of gel filtration and adsorption chromatographies on the resultant crude enzyme produced highly purified elastase with yields of 5 to 10%. The enzyme is a 23-kilodalton protein with a pI of 7.6. The enzyme activity is markedly inhibited by numerous metal ions. Aspergillus elastase appears to be a metalloproteinase (EC 3.4.24.X), as determined by its sensitivity to 1,10-phenanthroline.

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Rhodes, J. C., Amlung, T. W., & Miller, M. S. (1990). Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus. Infection and Immunity, 58(8), 2529–2534. https://doi.org/10.1128/iai.58.8.2529-2534.1990

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