Journal
FOOD CHEMISTRY
Volume 115, Issue 1, Pages 155-162Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2008.11.087
Keywords
Trypsin; Serine proteinase; Tuna; Purification; Isolation; Viscera; N-terminal amino acid sequence
Funding
- International Foundation for Science, Sweden [E/4413-1]
- Thai government, Thailand
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Two trypsins (A and B) from the intestine of skipjack tuna (Katsuwonus pelamis) were purified by Sephacryl S-200, Sephadex G-50 and DEAE-cellulose with a 177- and 257-fold increase in specific activity and 23% and 21% recovery for trypsin A and B, respectively. Purified trypsins revealed a single band on native-PAGE. The Molecular weights of both trypsins were 24 kDa as estimated by size exclusion chromatography and SDS-PAGE. Trypsin A and B exhibited the maximal activity at 55 degrees C and 60 degrees C, respectively, and had the same opt inial pH at 9.0. Both trypsins were stable up to 50 degrees C and in the pH range from 6.0 to 11.0. Both trypsin A and B were stabilised by calcium ion. Activity of both trypsins continuously decreased with increasing NaCl concentration (0-30%) and were inhibited by the specific trypsin inhibitors - soybean trypsin inhibitor and N-p-tosyl-L-lysine chloromethyl ketone. Apparent K., and K,,, of trypsin A and B were 0.22-0.31 mM and 69.5-82.5 S-1, respectively. The N-terminal amino acid sequences of the first 20 amino acids of trypsin A and B were IVGGYECQAHSQPPQVSLNA and IVGGYECQAHSQPPQVSLNS. respectively. (C) 2008 Elsevier Ltd. All rights reserved.
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