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| Content Provider | Springer Nature Link |
|---|---|
| Author | Yoshida, Asami Bae, Inwoo Sonoda, Hiroko Masuo, Ryuichi Oda, Sachie Cao, Min Jie Osatomi, Kiyoshi Hara, Kenji |
| Copyright Year | 2009 |
| Abstract | Gelatinolytic enzymes were partially purified from the skeletal muscle of red sea bream Pagrus major and characterized to obtain information on post mortem tenderization of fish muscle. Four gelatinolytic activities, G1 (90 kDa), G2 (65 kDa), G3 (60 kDa), and G4 (100 kDa), were detected in the Q Sepharose column. G1, the major gelatinolytic enzyme, and G4 were identified as serine proteinases from results of inhibitor spectrum and substrate specificity. By contrast, G2 and G3 were found to be metalloproteinases since these were inhibited by ethylenediamine tetraacetic acid and o-phenanthroline, and activated by 4-aminophenylmercuric acetate. The optimum pH and temperature of these enzymes were in the ranges of 7–9 and 20–40°C, respectively. |
| Starting Page | 1317 |
| Ending Page | 1322 |
| Page Count | 6 |
| File Format | |
| ISSN | 09199268 |
| Journal | Fisheries Science |
| Volume Number | 75 |
| Issue Number | 5 |
| e-ISSN | 14442906 |
| Language | English |
| Publisher | Springer Japan |
| Publisher Date | 2009-07-29 |
| Publisher Place | Japan |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Gelatinolytic enzyme Metalloproteinase Muscle Red sea bream Serine proteinase Food Science Freshwater & Marine Ecology Fish & Wildlife Biology & Management |
| Content Type | Text |
| Resource Type | Article |
| Subject | Aquatic Science |
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