Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization

• Kishimura, Hideki

• Tokuda, Yusuke

• Yabe, Mamoru

• Klomklao, Sappasith

• Benjakul, Soottawat

• Ando, Seiichi

Abstract

Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii), TR-J, and elkhorn sculpin (Alcichthys alcicornis), TR-E, were purified by gel filtration on Sephacryl S-200 and Sephadex G-50. The molecular weights of TR-J and TR-E were estimated to be 24,000 Da by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. TR-J and TR-E revealed optimum temperatures of 60 and 50 °C, respectively, and showed the same optimum pH (pH 8.0) for hydrolysis of Nα-p-tosyl-l-arginine methyl ester. TR-J and TR-E were unstable at above 50 and 40 °C, respectively, and were more stable at alkaline pH than at acidic pH. Thermal stabilities of TR-J and TR-E were highly calcium dependent. These purified trypsin enzymes were inhibited by serine protease inhibitors, such as TLCK and soybean trypsin inhibitor. The N-terminal amino acid sequences of TR-J and TR-E were also investigated. The N-terminal amino acid sequences of TR-J, IVGGYECKPYSQPHQVSLNS, and TR-E, IVGGYECTPHSQAHQVSLNS, were found, and these sequences showed highly homology to other fish trypsins.

Journal

• Food Chemistry

  Food Chemistry 100 (4), 1490-1495, 2007

  Elsevier B.V.

Keywords

• Jacopever
• Sebastes schlegelii
• Elkhorn sculpin
• Alcichthys alcicornis
• Pyloric ceca
• Trypsin
• Characteristics

Details

• CRID: 1050845763910217216
• NII Article ID: 120000964273
• HANDLE: 2115/14904
• ISSN: 03088146
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles