Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca2+-, EDTA-, Mg2+-, and Mg2+-Ca2+-ATPase activities of actomyosin decreased, whereas Mg2+-EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A signifcant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE.
|Number of pages||6|
|Journal||Journal of Food Science|
|Publication status||Published - 2002|
- Protein conformation
- Threadfin bream
ASJC Scopus subject areas
- Food Science