Purification and partial characterization of an elastinolytic proteinase from Aspergillus flavus culture filtrates |
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Authors: | J E Mellon P J Cotty |
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Institution: | (1) USDA, ARS, Southern Regional Research Center, P.O. Box 19687, New Orleans, Louisiana 70179, USA. Fax: 504–286–4419, e-mail: jmellon@nola.srrc.usda.gov, US |
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Abstract: | A 23-kDa protein with elastinolytic activity was purified from Aspergillus flavus (NRRL 18543) culture filtrates by gel-filtration chromatography. Severe inhibition of the elastinolytic activity by 1,10-phenanthrolene
(5 mM) and EDTA (0.8 mM) indicated that the protein belongs to the metallo class of proteases. The isoelectric point was 9.0.
Natural substrates susceptible to cleavage by this protease, in addition to elastin, included cottonseed storage protein,
collagen, ovalbumin and bovine serum albumin. The 23-kDa protein was thermostable to 70°C and retained its elastinolytic activity
in concentrated form at 4°C for 6 months. Elastinolytic activity was initially secreted into the culture medium as a 35-kDa
protein, which was subsequently converted to a 23-kDa protein, presumably through autolysis. This putative proteolytic degradation
product appears to be identical to the 23-kDa protein recovered from the gel-filtration column. The 23-kDa protease may confer
selective advantage to the fungus in the extracellular environment because of its temperature and pH stability and wide range
of potential natural protein substrates.
Received: 24 October 1995/Received last revision: 27 March 1996/Accepted: 30 March 1996 |
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