Aggregation of minced hake during frozen storage

Abstract

Aggregation in minced hake muscle (Merluccius merluccius) during storage at -20 °C was studied in conditions where there is progressive deterioration of functionality and texture as measured by apparent viscosity and shear resistance. Natural actomyosin was extracted with 0.6 M NaCl over a period of 49 weeks. Insoluble residue was extracted successively with 2% sodium dodecyl sulphate (SDS) and 2% SDS plus 5% β-mercaptoethanol (ME) solutions. SDS-polyacrylamide gel electrophoresis was performed on the extracted fractions. The results showed a 75% decrease in 0.6 M NaCl extractability by the end of the storage period. Initially the remaining precipitate was all extracted in 2% SDS and although the amount extracted in this solution increased as storage time progressed, its proportion decreased, accounting for as little as 40-50% of the protein aggregate by the end of storage. The proteins most involved in formation of the aggregate not extracted in 0.6 M NaCl were myosin and actin. Neither of these proteins was fully recovered in the fractions extracted with 0.6 M NaCl, 2% SDS, or 2% SDS plus 5% ME, and therefore it was inferred that they were forming part of the aggregates, bound by covalent bonds.