Production and partial characterization of a new fibrinolytic protease from salmon oyster mushroom from Amazonia.

Abstract

Edible mushrooms are excellent sources of enzymes, especially fibrinolytic proteases, which work to dissolve blood clots and can be obtained through different fermentative processes. This research evaluated the production of fibrinolytic protease from a specie of edible mushroom in different formulations of liquid cultures. Pleurotus ostreatoroseus was provided by the DPUA culture collection at the Federal University of Amazonas and cultivated on PDA agar supplemented with 0.5% (w/v) yeast extract. Liquid fermentation was carried out in an Erlenmeyer flask in 50 mL of GYP, MGYP, or Malt medium under stirring at 150 rpm at 30 °C, eight days. The extracts were recovered and dialyzed, and the liquid culture medium was selected based on the activity of fibrinolytic enzymes. In the recovered extracts, qualitative activity (fibrin plate) and quantitative activity of fibrinolytic proteases were determined, and the effect of pH, temperature, stability, ions, and inhibitors on enzymatic activity was evaluated. Pleurotus ostreatoroseus excreted proteases in all culture media tested. However, the translucent halo (12.59 ± 0.7 mm) and significant activity of fibrinolytic enzymes (449.32 ± 0.01 U/mL) was determined in GYP. In the dialyzed extract, P. ostreatoroseus had an increase in the excretion of fibrinolytic proteases (1,361.73 ± 0.09). Results indicated that in GYP extracts, proteases showed optimal activity at pH 8.0 and at 30 °C of the serine and metallo protease types. Thus, these biocatalysts have strong potential for use in the pharmaceutical, detergent sectors and food industries.