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 amberjackSeriola dumerili(S. du...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 amberjackSeriola 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 ofS. dumerili showed enzymatic activity of (1.4600 ± 0.0011 and (0.7100 ± 0.0079) 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 ofS. 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.展开更多
文摘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 amberjackSeriola 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 ofS. dumerili showed enzymatic activity of (1.4600 ± 0.0011 and (0.7100 ± 0.0079) 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 ofS. 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.
