Abstract
Pacific whiting protein solubility was significantly affected as the pH shifted away from the isoelectric point (pH 5.5). The highest breaking force of gels was measured for fish proteins treated at pH 11, while high deformation values were obtained at pH 2 and 11. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed that fish proteins were highly degraded by acid or alkali treatment. High activity of cathepsin B-like enzyme was detected from acid-aided fish proteins. Strong cathepsin L-like activity was found in fish proteins treated at pH 10.5, corresponding well to the lower breaking force and deformation. Disulfide bonds were thought to contribute to the high texture value of fish proteins treated at pH 11.
Original language | English |
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Pages (from-to) | 1231-1239 |
Number of pages | 9 |
Journal | Fisheries Science |
Volume | 69 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2003 Dec |
Keywords
- Acid-aided processing
- Alkali-aided processing
- Fish proteins
- pH
ASJC Scopus subject areas
- Aquatic Science