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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences >
Peer-reviewed Journal Articles, etc >
Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization
| Title: | Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization |
| Authors: | Kishimura, Hideki Browse this author →KAKEN DB | | Tokuda, Yusuke Browse this author | | Yabe, Mamoru Browse this author →KAKEN DB | | Klomklao, Sappasith Browse this author | | Benjakul, Soottawat Browse this author | | Ando, Seiichi Browse this author |
| Keywords: | Jacopever | | Sebastes schlegelii | | Elkhorn sculpin | | Alcichthys alcicornis | | Pyloric ceca | | Trypsin | | Characteristics |
| Issue Date: | 2007 |
| Publisher: | Elsevier B.V. |
| Journal Title: | Food Chemistry |
| Volume: | 100 |
| Issue: | 4 |
| Start Page: | 1490 |
| End Page: | 1495 |
| Publisher DOI: | 10.1016/j.foodchem.2005.11.040 |
| 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. |
| Relation: | http://www.sciencedirect.com/science/journal/03088146 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/14904 |
| Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 岸村 栄毅
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