| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1189958 | Food Chemistry | 2008 | 7 Pages |
Physicochemical characteristics of proteins extracted from muscles excised from four distinct regions of mackerel were examined. Three regions were identified based on their fin position; namely anterior muscle, median muscle, posterior muscle and red muscles from beneath the lateral line. The biochemical characteristics like reactive sulphydryl groups, surface hydrophobicity, Ca2+ ATPase activity, turbidity, proximate composition and the functional characteristics such as viscosity, emulsion activity index (EAI) and emulsion stability (ES) were studied in the samples, from different regions. Sarcoplasmic protein (SPP) solubility was found to be higher in red muscles compared to that of white muscles, whereas myofibrillar protein (MFP) solubility was higher in white muscles particularly in the posterior portion. The MFP from posterior white muscles showed better viscosity, surface hydrophobicity and Ca2+ ATPase activity, which in turn contributed to the higher EAI and ES of this muscle portion. Variations in composition, electrophoretic pattern of proteins and selected functional properties (EAI) were noticed between red and white muscles, which may be of significance from the utilization point of the fish.
