Abstract

Objective: To investigate the presence of industrial enzymes (trypsin and chymotrypsin) as well as collagenolytic and fibrinolytic activities of the neglected processing waste of greater amberjack Seriola dumerili (S. dumerili). Methods: The investigations on trypsin, chymotrypsin, collagenolytic and fibrinolytic activities in residues in digestive viscera were performed. The enzymes trypsin and chymotrypsin were physicochemically characterized (including pH- and thermo-stabilities and sensitivity to metal ions and inhibitors). The kinetic parameters were also determined. Collagenolytic and fibrinolytic activities of the crude extract were also investigated. Results: The crude extract of S. dumerili showed enzymatic activity of (1.460 0 ± 0.001 1 and (0.710 0 ± 0.007 9) IU/mg protein for trypsin and chymotrypsin, respectively. The optimal temperature and pH was 60 °C and 9 for trypsin and 40 °C and 8 for chymotrypsin. The main inhibitory ions were in the following order: Fe3+ > Cu2+ > Zn2+ > Cd2+ > Hg2+ (trypsin) and Hg2+ > Fe3+ > Zn2+ > Cd2+ > Mn2+ (chymotrypsin). TLCK and benzamidine were the strongest inhibitors for both enzymes. The crude extract also presented collagenolytic activity [(42.44 ± 0.01) IU/mg] and fibrinolytic activity [(26.70 ± 0.05) IU/mL]. Conclusions: The crude extract of S. dumerili showed potential for reuse of its residues and to provide biomolecules of industrial interest like trypsin and to be a source of fibrinolytic enzymes.

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