This work was partially supported by Grant No. NA36RG0451 (Project No. R/SF-1) from the National Oceanic and Atmospheric Administration to the Oregon State University Sea Grant College Program and by appropriation made by the Oregon State legislature and by Grant No. 96–35500-3340 from the U.S. Dept. of Agriculture-Cooperative State Research, Education, and Extension Service. The views expressed herein are those of the authors and do not necessarily reflect the views of NOAA or any of its subagencies.
Physicochemical Changes in Pacific Whiting Muscle Proteins during Iced Storage
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 62, Issue 4, pages 729–733, July 1997
How to Cite
BENJAKUL, S., SEYMOUR, T. A., MORRISSEY, M. T. and AN, H. (1997), Physicochemical Changes in Pacific Whiting Muscle Proteins during Iced Storage. Journal of Food Science, 62: 729–733. doi: 10.1111/j.1365-2621.1997.tb15445.x
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- Ms received 10/21/96; revised 2/3/97; accepted 2/12/97.
- Pacific whiting;
- muscle proteins;
No changes in actomyosin Ca2+-, Mg2+-, or Mg2+-Ca2+-ATPase activities were observed during iced storage of Pacific whiting fillets, but Mg2+-EGTA-ATPase increased with a loss of Ca2+-sensitivity. Surface hydrophobicity of actomyosin increased substantially within 2 days, but not total sulfhydryl (SH) content. During longer storage, the SH content decreased gradually, but surface hydrophobicity remained constant. Autolytic degradation products increased in fish muscle with storage time. Myosin heavy chain (MHC) was degraded by 45% within 8 days, but no noticeable difference was observed in actin. Results indicated that autolysis may be the main cause of physicochemical changes in Pacific whiting muscle proteins during iced storage.