Importance of frozen storage temperature in the type of aggregation of myofibrillar proteins in cod (Gadus morhua) fillets

• Published in: Journal of Agricultural and Food Chemistry
• Main Authors: Careche, Mercedes, Mazo, M. Luisa del, Torrejón, Purificación, Tejada Yábar, Margarita
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: American Chemical Society 1998
• Subjects: Aggregation; Actomyosin; Temperatures; Frozen storage; Cod fillets; Gadus morhua
• Online Access: http://hdl.handle.net/10261/93745; https://doi.org/10.1021/jf970841y

Cod fillets were examined to determine the effect of two frozen storage temperatures (-20 and -30 °C) on the formation of aggregates and if this relates to changes in texture and functionality. The evolution of apparent viscosity during frozen storage was similar at either storage temperature. Loss of extractability in 0.6 M NaCl was slightly greater at -20 °C. The aggregate which formed at -30 °C was extractable in solutions which cleave secondary interactions [2% sodium dodecyl sulfate (SDS)] whereas at -20 °C the role of non-disulfide covalent bonds was more important, so that this aggregate was not totally extracted in 2% SDS plus 5% β-mercaptoethanol. The aggregates consisted largely of myosin and actin, but myosin was the most important constituent, contributing more to the formation of covalent bonds, particularly at the higher temperature. This difference in aggregation was accompanied with a difference in the evolution over time of shear resistance, which was higher at-20 °C. Peer Reviewed