Fish viscera have been documented to be an important source for obtaining enzymes that can be used for several industrial applications. In this study, trypsin was purified from the pancreas of Scyliorhinus canicula by ammonium sulfate precipitation and soybean trypsin inhibitor (SBTI) sepharose 4B affinity chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the isolated trypsin showed a single band with a molecular weight of approximately 28 kDa and an approximate isoelectric point value of 5.5. The optimum pH and temperature for activity were 8.0 and 55C, respectively. SBTI and phenylmethylsulfonyl fluoride were inhibitors of the isolated fraction, supporting its serine proteinase nature. Stability results with detergents and surfactants suggest that this enzyme can be incorporated as an ingredient in detergent formulations.

The authors would like to acknowledge the financial support of DG Environment for the project “Benign and environmentally friendly fish processing practices to provide added value and innovative solutions for a respon- sible and sustainable management of fisheries” and the Atlantic Area Transnational Programme with the project “Biotechnological exploitation of marine products and by-products” (BIOTECMAR)

11 páginas, 3 tablas, 9 figuras

Peer reviewed