Fibrinolytic proteases operate directly on fibrin clot and are able to maintain blood flow. Fungi show up as viable sources for obtaining this enzyme. The purpose of this systematic review is to is to unveil all the information concerning production, purification and characterization of fibrinolytic proteases by fungi. The search was conducted in ScienceDirect, PubMed and Scopus databases, using as keywords “(Fibrinolytic enzyme) OR (Fibrinolytic protease) AND (Fungal or Fungus or Fungi)”. Delimiting period of 10 years (2011-2021). The results obtained were filtered by selection criteria, and review articles or articles outside the scope of this work were excluded. The articles were evaluated and scored (0-10) according to pre-established criteria. None of the studies obtained the score 10, however the study with the highest score (9) presented relevant data in all criteria analyzed, obtaining fibrinolytic enzyme from Xylaria curta. Among the 21 selected articles, 12 different genera appear and Submerged Fermentation and purification of Serino-proteases were more described. This work also observed a greater representation of purification and characterization steps, indicating the need for attention to cultivation process and enzymatic application. It is clear that the production of these enzymes by fungi is pertinent towards the high recovery observed even after purification and its tendency for pharmaceutical application.

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Solid state fermentation is a promising technology largely used in biotechnology process and is a suitable strategy for producing low-cost enzymatic products. At the present study, a novel enzyme obtained through solid state fermentation using Aspergillus sydowii was herein purifi ed and characterized. The fermentations used coffee ground residue as substrate and the crude enzyme was submitted through further purifi cation steps of: acetonic precipitation, DEAE-Sephadex and Superdex G-75 column.Both crude and purifi ed enzymes were submitted to biochemical characterization of their thermostability, optimal temperature and pH, effects of inhibitors and metal ions.A purifi ed protease was obtained with yield of 5.9-fold and 53% recovery, with maximal proteolytic activity of 352.0 U/mL. SDS-PAGE revealed a band of protein at 47.0 kDa. The enzyme activity was abolished in the presence of phenyl-methyl sulfonyl fl uoride and partially inhibited against Triton X-100 (78.0%). The optimal activity was found in pH 8.0 at 45°C of temperature. Besides, the enzyme showed stability between 35°C and 50°C.It was possible to determine appropriate conditions to the obtainment of thermostable proteases with biotechnological interest associated with a method that concomitantly shows excellent production levels and recovery waste raw material in a very profi table process.

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