Tokur B., Polat A.

JOURNAL OF MUSCLE FOODS, vol.21, no.1, pp.102-118, 2010 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 21 Issue: 1
  • Publication Date: 2010
  • Doi Number: 10.1111/j.1745-4573.2009.00170.x
  • Title of Journal : JOURNAL OF MUSCLE FOODS
  • Page Numbers: pp.102-118


The oxidation of myofibrillar and sarcoplasmic proteins of thin-lipped mullet (Liza ramada) in different ages during refrigerated storage (4C), and in vitro oxidation of muscle after 2 and 24 h incubation with Fe+2/H2O2 at 4C were evaluated by means of protein carbonyl content. Changes in myofibrillar and sarcoplasmic proteins were estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The carbonyl content of myofibrillar proteins exhibited a regular increase at 2 years of age during the refrigerated storage for 10 days (P < 0.05), and increased at 4 and 6 years of age after 5 days of cold storage (P > 0.05), and then did not significantly change between 5 and 10 days of storage (P > 0.05). Sarcoplasmic proteins showed a decrease in the carbonyl content at 2 years of age during 10 days of storage. However, no significant changes were observed in carbonyl content of sarcoplasmic proteins at 4 and 6 years of age (P > 0.05). An increase in carbonyl content of whole muscle, but not statistically significant, was found at 2, 4 and 6 years of age during 10 days of cold storage. There were no significant differences in oxidation of thin-lipped gray mullet proteins in all ages between 2 and 24 h of incubation with Fenton-like oxidation system (Fe+2SO(4)/H2O2) at 4C (P < 0.05). However, there was a tendency to find an increase in carbonyl content in all ages after 24 h of incubation. Electrophoretic studies in the presence and absence of beta-mercaptoethanol showed that high-molecular weight polymers via disulfide cross-linking and/or degradation/digestion by proteolysis could be formed in the myofibrillar proteins in different ages. Slight changes were observed in sarcoplasmic proteins of thin-lipped gray mullet both in the absence and presence of a disulfide-splitting agent. These results suggest that there is a probable link between protein oxidation and protelytic degradation of myofibrillar proteins during postmortem storage, and the effects of cold storage on oxidation and possible changes in myofibrillar and sarcoplasmic proteins could be changed depending on ages in same species.