Resumen

MARCIAL, J. et al. Characterization of an aspartic protease produced by Amylomyces rouxii. Rev. Mex. Ing. Quím [online]. 2011, vol.10, n.1, pp.9-16. ISSN 1665-2738.

The zigomycete Amylomyces rouxii was isolated, in our laboratory, from effluents of paper industries, it was showed that this fungus produces extracellular tyrosinase. In this work, we show that this fungus produces also an extracellular protease. The extracellular protease was partially purified using two-step purification, by (NH₄)₂SO₄ fractionation and DEAE-sepharose anion exchange chromatography with 4.25-fold factor purification. The optimal pH for protease activity, using hemoglobin as substrate, was 3.5. Results from protein purification revealed that this protease is an aspartic protease. Protease activity was inhibited 73% by pepstatin A, a specific inhibitor of acid proteases. Results allow conclude that A. rouxii produce an extracellular aspartic protease that has similar characteristics to aspartic proteases produced by fungi as Mucor and Rhizopus.

Palabras llave : Amylomyces rouxii; aspartic protease; inhibitor protease.

        · resumen en Español     · texto en Inglés     · Inglés ( pdf )