FISH AS A POTENTIAL SOURCE OF COLLAGENOLYTIC AND FIBRINOLYTIC ENZYMES OF INTEREST TO THE PHARMACEUTICAL AND BIOMEDICALINDUSTRY

Neglected fish processing wastes are promising sources of biomolecules with potential for industrial application. This work aimed to perform a sorting of discarded fish residues (Rachycentron canadum, Caranx crysos, Lutjanus synagris, Scomberomorus mackerel, Parachromis managuensis, Colossoma macropomum, Oreochromis niloticus, Pseudoplatystoma corruscans, Cichla ocellaris, Cynoscion leiarchus) and shrimp hydrolyzate (Litopenaeus vannamei) investigating the presence of collagenolytic and fibrinolytic enzymes. The collagenolytic activities varied according to the species, between 15.95 ± 0.07 U/mg (P. corruscans) and 94.35 ± 0.02 U/mg (C. ocellaris). After sorting by collagenolytic activity, the species selected was Cichla ocellaris, having the biochemical properties defined. Optimal pH and temperature of collagenolytic activity were 7.5 and 55°C, respectively, showing stability at pH range from 6.5 to 11.5 and temperatures ranging from 25 to 60°C. The enzyme was sensitive to Cu, Hg and Pb, being partially inhibited by PMSF, TLCK and Benzamidine. The fibrinolytic activities varied between 5.51 ± 0.02 and 56.16 ± 0.42 U/ml, indicating another possibility of reuse of these byproducts. The results suggest intestinal fish viscera as a promising source of collagenolytic enzymes and shrimp hydrolyzate as well as fibrinolytic, both of which have palpitations in the pharmaceutical and biomedical industry after purification processes.