Proteases hydrolyze polypeptides to release peptides and/or amino acids. This subclass of
enzymes is among those with the most sales worldwide, particularly those produced by microorganisms.
Proteases may be applied in the several industries, including the food industry, leather, detergents, and bioremediation.
Myceliophthora thermophila protease was produced by a submerged bioprocess and then purified 185-fold by anion
exchange and hydrophobic chromatography with a 37% yield. The molecular mass was estimated at 36.2 kDa, and mass
spectrometry identified two sequences: GVVANMSLGGSYSASINNAAAALVR and STGNAAITGVPSGTTNR. The
isolated protein was characterized biochemically, showed an optimum pH of 6.5 and optimum temperature of 45 °C, and
stability at wide range of pH and temperatures and in the presence of reducing agents and some surfactants. Kinetic assays
for this enzyme showed a greater catalytic efficiency when the substrate had alanine at position P'2. The protease presented
characteristics that may be of interest to many industrial areas.
Keywords: FRET substrates, neutral protease, mass spectrometry, Myceliophthora thermophila, purification, stability.
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