Influence of chilled and frozen storage on the stability of trout and herring fillet

Effects of chilled and frozen storage on specific enthalpy (ΔH) and transition temperature (Td) of protein denaturation as well as on selected functional properties of muscle tissue of rainbow trout and herring were investigated. The Td of myosin shifted from 39 to 33 °C during chilling of trout post mortem, but was also influenced by pH. Toughening during frozen storage of trout fillet was characterized by an increased storage modulus of a gel made from the raw fillet. Differences between long term and short term frozen stored, cooked trout fillet were identified by a compression test and a consumer panel. These changes did not affect the Td and ΔH of heat denaturation during one year of frozen storage at –20 °C. In contrast the Td of two myosin peaks of herring shifted during frozen storage at –20 °C to a significant lower value and overlaid finally. Myosin was aggregated by hydrophobic protein-protein interactions. Both thermal properties of myosin and chemical composition were sample specific for wild herring, but were relative constant for farmed trout samples over one year. Determination of Td was very precise (standard deviation <2 %) at a low scanning rate (≤ 0.25 K·min-1) and is useful for monitoring the quality of chilled and frozen stored trout and herring.

Einfluss von Reifung und technologischen Behandlungen auf die Proteine des Rogens von Regenbogenforellen (Oncorhynchus mykiss)

The use of differential scanning calorimetry for investigating the yolk proteins of the roe of rainbow trout allows to monitor the influence of maturation and vitellogenesis which modifies the DSC curves with regard to transition temperature and enthalpy. Two endothermic peaks become more and more pronounced with increasing maturation of the roe. However, it is still not known which protein fraction is represented by each of the peaks. DSC curves of yolk protein depend on fish species. They are also influenced by technological treatments. Further investigation is necessary to discover whether or not yolk proteins of other fish species are influenced in the same manner by maturation and vitellogenesis and which protein fraction represent the individual peaks.