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Isolation and partial characterization of trypsin from pancreas of small-spotted catshark (Scyliorhinus canicula)

AuthorsBlanco Comesaña, M. ; Simpson, B. K.; Pérez Martín, Ricardo Isaac CSIC ORCID; González Sotelo, Carmen CSIC ORCID
Issue Date2014
CitationJournal of Food Biochemistry 38(2): 196-206 (2014)
AbstractFish 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.
Description11 páginas, 3 tablas, 9 figuras
Publisher version (URL)http://dx.doi.org/10.1111/jfbc.12038
Appears in Collections:(IIM) Artículos
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