This research was partially funded by the Natl. Sea Grant College Program of the U.S. Dept. of Commerce's Natl. Oceanic and Atmospheric Administration under NOAA grant number NA76RG0476 (project nr R/SF-24) and by appropriations made by the Oregon State Legislature. The views expressed herein do not necessarily reflect the views of any of those organizations.
Frozen Stability of Fish Protein Isolate Under Various Storage Conditions
Article first published online: 30 JUN 2006
Journal of Food Science
Volume 71, Issue 3, pages C227–C232, April 2006
How to Cite
Thawornchinsombut, S. and Park, J. W. (2006), Frozen Stability of Fish Protein Isolate Under Various Storage Conditions. Journal of Food Science, 71: C227–C232. doi: 10.1111/j.1365-2621.2006.tb15622.x
- Issue published online: 30 JUN 2006
- Article first published online: 30 JUN 2006
- MS 20050675 Submitted 11/11/05, Revised 12/15/05, Accepted 1/25/06.
- alkali-treated protein isolates;
- frozen storage;
- surface hydrophobicity;
ABSTRACT: A novel process using pH-shift to recover fish proteins has been intensively studied. However, little information of its frozen stability has been revealed. The highest gel texture was found for samples frozen at pH 5.5 (5) and 7.0 (7) with cryoprotectants (C) and without freeze/thaw (F), whereas the lowest gel texture was obtained from frozen/thawed samples without cryoprotectants (NC). 5NC-F and 7NC-F demonstrated the lowest surface hydrophobicity and total sulfhydryl (SH), perhaps suggesting more protein aggregation through hydrophobic interactions and disulfide bonds. A slightly less stability of alkali-treated protein isolates (AKPI) kept at pH 5.5 than at pH 7 was noticed. AKPI, whether kept at pH 5.5 or 7.0, requires cryoprotectants to maintain frozen stability for longer shelf life.