Thermal Effects on Fast Skeletal Myosins from Alaska Pollock, White Croaker, and Rabbit in Relation to Gel Formation

Abstract

Thermodynamic properties in differential scanning calorimetry (DSC) and changes in viscoelasticity upon heating of myosins from white croaker, Alaska pollock, and rabbit fast muscles were investigated in relation to their thermal gel formation abilities. Alaska pollock myosin unfolded in a wide temperature range of 19 to 69 °C as revealed by DSC, whereas rabbit myosin unfolded in very narrow range of 32 to 56 °C. Thermal unfolding of white croaker myosin occurred in an intermediate temperature range of 30 to 60 °C. Viscoelastic properties determined as storage modulus, GЈ Ј Ј Ј Ј, and loss modulus, GЉ Љ Љ Љ Љ, reflected differences observed in DSC for the 3 myosins.

Rheological properties of selected fish paste at selected temperature pertaining to shaping of surimi-based products

“…Actomyosin of threadfin bream is also much higher in thermostability than those of cold water species (Yongsawatdigul & Park, 2003). Meanwhile, the increase of G 0 is related to the effects of temperature on the unfolding of proteins (Egelandsdal et al, 1995;Fukushima, Satoh et al, 2003;Hamann, 1991). Thereby, it is reasonable that walleye pollack and white croaker meat pastes showed relatively high G 0 at 5°C, whereas G 0 of threadfin bream meat paste showed lower value at this temperature and markedly increased upon thermal treatment.…”

“…Typical gels exhibit constant G 0 on frequency sweep analysis, whereas G 0 of typical sol is dependent on a frequency (Almdal, Dyre, Hvidt, & Kramer, 1992). It has been reported that walleye pollack and white croaker myosins heated at 80°C showed a constant G 0 (Fukushima, Satoh et al, 2003). The three meat pastes treated at 37°C for 1 h showed almost constant G 0 on frequency sweep analysis in a range of 0.1-10 Hz (Fig.…”

“…Temperature sweep analysis to measure the changes in dynamic rheological parameters including storage moduli (G 0 ), loss moduli (G 00 ) and tangent of phase angle (tan d) during heating were performed according to Fukushima, Satoh, Nakaya, Ishizaki, and Watabe (2003) at a constant frequency of 1.0 Hz and amplitude strain of 1%, which was within the linear viscoelastic region, from 5 to 30°C at an increasing rate of 1°C/min. Frequency sweep analysis for G 0 was also performed according to Fukushima, Satoh et al (2003) at a constant amplitude strain of 1% and in a frequency range of 0.1-10 Hz at 5, 10, 15, 20, 25 and 30°C. Frequency sweep analysis for G 0 was also carried out at 37°C for samples heated at this temperature for 1 h under the same conditions expect for measuring temperature.…”

Differential Scanning Calorimetry

“…Rabbit myosin showed T max at 45.4, 50.9 and 54.6 °C. According to circular dichroism investigations of these myosins upon heating, it appeared that a close relationship of endothermic peaks in DSC with unfolding of α-helical structure existed (Fukushima et al 2003a). Light meromyosins (LMMs) of white croaker and walleye pollack were prepared in an expression system using Escherichia coli and determined for their thermodynamic properties by using microDSC.…”

Rheological behavior of heat-induced actomyosin gels from yellowcheek carp and grass carp

“…GAM at a concentration of 10 mg/mL hardly formed a strong network structure, since its d value was higher than 45°in the temperature range of 47.3-78.5°C. It was previously demonstrated that species-specific differences in thermal unfolding and aggregation process of the myosin molecule resulted in differences of dynamic viscoelasticity and thus heat-induced gel forming ability [27][28][29]. Therefore, differences in thermal gelation profiles between YAM and GAM may be due to the different thermal stability of myosin from these two fish species.…”