• Vagne de Melo Oliveira Universidade Federal Rural de Pernambuco -  UFRPE, Laboratório de Tecnologia de Produtos Bioativos -  LABTECBIO, Departamento de Morfologia e Fisiologia Animal -  DMFA / Universidade Federal de Pernambuco -  UFPE, Laboratório de Enzimologia -  LABENZ, Departamento de Bioquí­­mica
  • Caio Rodrigo Dias Assis Universidade Federal de Pernambuco -  UFPE, Laboratório de Enzimologia -  LABENZ, Departamento de Bioquí­­mica
  • Jéssica Costa Silva Universidade Federal Rural de Pernambuco -  UFRPE, Laboratório de Tecnologia de Produtos Bioativos -  LABTECBIO, Departamento de Morfologia e Fisiologia Animal -  DMFA
  • Quesia Jemima Silva Universidade Federal Rural de Pernambuco -  UFRPE, Laboratório de Tecnologia de Produtos Bioativos -  LABTECBIO, Departamento de Morfologia e Fisiologia Animal -  DMFA
  • Ranilson de Souza Bezerra Universidade Federal de Pernambuco -  UFPE, Laboratório de Enzimologia -  LABENZ, Departamento de Bioquí­­mica
  • Ana Lúcia Figueiredo Porto Universidade Federal Rural de Pernambuco -  UFRPE, Laboratório de Tecnologia de Produtos Bioativos -  LABTECBIO, Departamento de Morfologia e Fisiologia Animal -  DMFA



byproducts, collagenase, thrombolytic


Fish and shrimp industries generate a significant amount of by-products. These by-products can be used for the extraction of enzymes of biomedical interest, such as fibrinolytic and collagenolytic. Thus, this work aimed to perform a screening of fish and shrimp byproducts as sources of enzymes with fibrinolytic and collagenolytic activities and to characterize the biochemical properties of crude extracts with collagenolytic activity from Cichla ocellaris residues. Fibrinolytic enzymes were recovered with activities between 5.51 ± 0.02 U.mL-1 (Caranx crysos) and 56.16 ± 0.42 U.mL-1 (Litopenaeus vannamei), while collagenolytic enzymes were detected in a range between 6.79 ± 0.00 (Trachurus lathami) and 94.35 ± 0.02 (C. ocellaris). After collagenolytic screening, the selected species was C. ocellaris, being subjected to a preheating, which culminated with an increase of enzymatic activity of 35.07% (up to 127.44 ± 0.09 The optimal collagenolytic activity recovered from C. ocellaris byproducts was 55 °C (thermostable between 25 and 60 °C) and 7.5 (stable between 6.5 and 11.5) for temperature and pH evaluations, respectively. The kinetic parameters were determined, obtaining Km of 5.92 mM and Vmax of 294.40 The recovered enzyme was sensitive to the Cu2+, Hg2 and Pb2+ ions, being partially inhibited by phenylmethylsulphonyl fluoride (PMSF), N-p-tosyl-L-lysin chloromethyl ketone (TLCK) and Benzamidine. Furthermore, it was able to cleave native type I collagen, the most important type for industry. Thus, the recovery of biomolecules, besides offering to the industry an alternative source of active molecules, contributes to the reduction of the environmental impact, adding value to the fish product and providing a new source of income.


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