Isolation and characterization of a trypsin fraction from the pyloric ceca of chinook salmon (Oncorhynchus tshawytscha) |
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Authors: | Kurtovic I Marshall S N Simpson B K |
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Institution: | aSeafoods and Marine Extracts Group, Crop and Food Research Limited, P.O. Box 5114, Port Nelson, Nelson, New Zealand;bFood Science Department, McGill University (Macdonald Campus) 21,111 Lakeshore Road, Ste. Anne de Bellevue (QC) Canada H9X 3V9 |
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Abstract: | A trypsin fraction was isolated from the pyloric ceca of New Zealand farmed chinook salmon (Oncorhynchus tshawytscha) by ammonium sulfate fractionation, acetone precipitation and affinity chromatography. The chinook salmon enzyme hydrolyzed the trypsin-specific synthetic substrate benzoyl-dl-arginine-p-nitroanilide (dl-BAPNA), and was inhibited by the general serine protease inhibitor phenyl methyl sulfonyl fluoride (PMSF), and also by the specific trypsin inhibitors — soybean trypsin inhibitor (SBTI) and benzamidine. The enzyme was active over a broad pH range (from 7.5 to at least pH 10.0) at 25 °C and was stable from pH 4.0 to pH 10.0 when incubated at 20 °C, with a maximum at pH 8.0. The optimum temperature for the hydrolysis of dl-BAPNA by the chinook salmon enzyme was 60 °C, however, the enzyme was unstable at temperatures above 40 °C. The molecular mass of the chinook salmon trypsin was estimated as 28 kDa by SDS–PAGE. |
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Keywords: | Affinity chromatography Chinook salmon Farmed fish Fish viscera Oncorhynchus tshawytscha Proteolytic enzymes Serine protease Trypsin |
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