INFLUENCE OF WASHING AND FROZEN STORAGE ON THE MYOFIBRILLAR PROTEIN FRACTION IN SARDINE MINCE FLESH.

Abstract

Frozen storage of fish species, such as sardine, result in detrimental changes in functional properties that determine storage life. Sardine meat is characterized by high fat content, dark meat, and sarcoplasmic proteins that inhibit gel formation. Washing mince flesh with solutions such as sodium bicarbonate is very effective for removing undesirable components. The objective of this research was to study the effects of frozen storage at -30°C in the myofibrillar protein fraction of sardine mince flesh washed with 0.5% sodium bicarbonate solution. Samples of sardine-minced flesh were washed three times with a 0.5% of sodium bicarbonate solution and centrifuged at 3000 rpm for 15 minutes. These samples were divided in lots of 100 g. packed in plastic bags and stored at -30°C, and analyzed every 30 days for 150 days. The myofibrillar proteins were extracted using a phosphate buffer (tris HCl, KCl, EDTA, pH 7.6), and evaluated by SDS-PAGE. The bands were analyzed and digitalized with a Gel Doc 2000 and Quality One 4.1.1 by Bio-Rad. The main bands of myofibrillar protein were identified by comparison of these against a prestained molecular weight standard. After 60 days there was deterioration of the myofibrillar protein fraction with apparent molecular weight between 220 and 65KD, and the formation of molecular aggregates at high molecular weight occurred. After 120 days due to myofibrillar protein deterioration, protein and peptides with low molecular weight were formed and increasing throughout frozen storage. Understanding the mechanism involved in the deterioration of the mince flesh during frozen storage we would enable to help the establishment of quality parameters and ability to predict storage life for that product.