Record Details
Salmon plasma protein to inhibit protease enzymes and enhance surimi gelation
ScholarsArchive at Oregon State University
| Field | Value |
|---|---|
| Title | Salmon plasma protein to inhibit protease enzymes and enhance surimi gelation |
| Names |
Fowler, Matthew (Matthew Ryan)
(creator) Park, Jae W. (advisor) |
| Date Issued | 2014-09-18 (iso8601) |
| Note | Graduation date: 2015 |
| Abstract | The ability of salmon plasma protein (SPP) obtained from Chinook salmon at the Klaskanine Fish Hatchery (Astoria, OR) to inhibit protease enzymes found in Pacific whiting (PW) surimi and salmon mince as well as the effect of SPP on the gelation properties of PW surimi under various heating conditions was investigated. The first study focused on the biochemical aspects of SPP, including enzyme and autolysis inhibition, stability, and molecular weight determination through inhibitor staining. The second study focused on the effects of SPP on PW surimi gelation using various heating treatments to isolate the activity of both protease enzymes and transglutaminase (TGASE) The results indicated that SPP contains both cysteine and serine protease inhibitors and effectively inhibits autolysis in both PW surimi and salmon mince. As little as 0.25% SPP inhibited PW surimi autolysis by about 90%, suggesting that low concentrations SPP could be effective when added to PW surimi. In addition, both cysteine and serine protease inhibitors in SPP exhibited good thermal, pH and salt stability. As little as 0.5% addition of SPP significantly improved the gel strength of PW surimi that was rapidly heated to 60°C and held at that temperature for 30 min before rapidly heating to 90°C in order to isolate protease enzyme activity. Analysis of TCA-soluble peptide analysis showed no significant proteolytic activity in this gel after SPP was added. One percent addition of SPP was shown to significantly improve the gel strength of PW surimi that was held at 25°C for 2 hr before being rapidly heated to 90°C in order to isolate TGASE activity. This suggests that SPP may contain its own TGASE activity in addition to endogenous TGASE present in PW surimi. These results were confirmed by SDS PAGE and scanning electron microscopy. |
| Genre | Thesis/Dissertation |
| Access Condition | http://creativecommons.org/licenses/by-nc-sa/3.0/us/ |
| Topic | surimi |
| Identifier | http://hdl.handle.net/1957/52384 |
