Purification and Characterization of a Trypsin-Like Protease from Flatfish (Paralichthys olivaceus) Intestine
Version of Record online: 6 JUL 2012
© 2012 Wiley Periodicals, Inc
Journal of Food Biochemistry
Volume 37, Issue 6, pages 732–741, December 2013
How to Cite
Kim, M. and Jeong, Y. (2013), Purification and Characterization of a Trypsin-Like Protease from Flatfish (Paralichthys olivaceus) Intestine. Journal of Food Biochemistry, 37: 732–741. doi: 10.1111/j.1745-4514.2012.00672.x
- Issue online: 4 DEC 2013
- Version of Record online: 6 JUL 2012
- Manuscript Accepted: 29 MAY 2012
- Manuscript Received: 19 MAR 2011
A trypsin-like protease was purified from the intestine of flatfish (Paralichthys olivaceus) by gel filtration and anion-exchange chromatography. The molecular weight was estimated to be 29.6 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Flatfish protease had maximal activity at 70C and pH 7.5 using N-α-benzoyl-dl-arginine-ρ-nitroanilide as substrate. It was stable to heat treatment up to 50C and to pH ranges between 7.0 and 10.0. It was activated by calcium ion and completely inhibited by mercury ion and known serine-protease inhibitors, such as phenylmethylsulfonyl fluoride, tosyl lysine chloromethyl ketone and benzamidine.
Flatfish trypsin could be an alternative to commercial trypsins in a wide variety of applications in the food, detergent and pharmaceutical industries. In the food industry, trypsin is used to produce protein hydrolysates, extract flavor, tenderize meat and improve oil extractions. It is also used in detergent, bating of leather and in diabetes diagnosis and therapy. Moreover, it can break down tumors and cancer cells in cancer therapy.