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摘要
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 Scyliorhinuscanicula 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 28kDa 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. Practical ApplicationsCharacterization of a protease from low-value viscera and discarded fish species, and utilization of the enzyme may add value to this discarded species. Furthermore, the thermolability of the purified trypsin makes it potentially useful in food processing operations because it can be readily inactivated by mild heat treatment. The stability at acidic pH may also find use in operations where low pH is required, such as in the production of fish silage, or in the fish fillet industry. Finally, the stability of the enzyme in commercial detergents suggests that it can be used as an additive in laundry detergents.
- 出版日期2014-4
