Myosin thermal stability in fish muscle

Davies, Jennifer R.; Bardsley, R. G.; Ledward, D.A.; Poulter, R. G.

doi:10.1002/jsfa.2740450108

Cited by 39 publications

(27 citation statements)

References 15 publications

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“…In addition, the results would also indicate that the native muscle has higher thermal stability than the isolated myofibrillar proteins. These results agree with those reported by other authors (1,28,29). In addition, the results shown in Figures 1, 2, and 3 would indicate that the paramyosin content does not have a direct influence on the thermal stability of proteins.…”

Section: Thermal Behavior Of Both Striated and Smooth Wholesupporting

confidence: 95%

Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamyspatagonica). A Differential Scanning Calorimetric Study

Paredi

Tomás

Crupkin

2002

J. Agric. Food Chem.

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Denaturation of proteins from striated and smooth muscles of scallop (Zygochlamys patagonica) was studied with differential scanning calorimetry (DSC) by monitoring maximum temperatures of transition and denaturation enthalpies. DSC thermograms of both striated and smooth whole muscles showed two transitions: Tmax 55.0, 79.2 degrees C; and Tmax 54.7, 78.7 degrees C, respectively. The DSC thermograms of myofibrils and actomyosin were similar to those corresponding to their respective whole muscles. As pH and ionic strength increased, the thermal stability of whole muscles decreased. The pH increase (5.0-8.0) significantly (p < 0.01) decreased the denaturation enthalpies (deltaH total, deltaH peakI, and deltaH peakII) of whole striated muscles. A significant decrease (p < 0.05) in the deltaH total and the deltaH peakI was also observed in DSC thermograms of smooth muscles at pH 8.0. Denaturation enthalpies (deltaH total and deltaH peakI) significantly decreased (p < 0.01) when the ionic strength increased from 0.05 to 0.5 in both types of muscles. Striated muscles were more affected than smooth muscles by changes in the chemical environment.

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Section: Thermal Behavior Of Both Striated and Smooth Wholesupporting

confidence: 95%

Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamyspatagonica). A Differential Scanning Calorimetric Study

Paredi

Tomás

Crupkin

2002

J. Agric. Food Chem.

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“…Under such increasingly exacting conditions, the myosins of tropical fish appear to be disrupted similarly to the otherwise less stable cold-water fish. Davies et al (1988) observed a similar effect for isolated red snapper (tropical) myosin compared to cod (cold-water) myosin. They suggested that differences in the aggregation characteristics of fish myosins may partly explain their different thermal denaturation properties in vitro.…”

Section: Discussionsupporting

confidence: 70%

Thermal stability of fish myofibrils: a differential scanning calorimetric study

Howell

Matthews

Donnelly

1991

Int J of Food Sci Tech

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The variation in myofibrillar protein thermostability was compared for various fish species, using differential scanning calorimetry. The tropical fish, catfish (Clariw gariepinus), carp (Cyprinus carpio), Nile perch (Lutes niloticus) , red snapper (Lutianus sebae) , red mullet (Parpeneus barberinus), sea bream (Gyrnnocranius rivalatus), and cold-water reared trout (Salmo gairdneri) and cod (Gadus morhua) were analysed. Onset temperature of myofibrillar protein denaturation occurred at up to 11°C higher for tropical species (43.5"C, catfish), than cod (32.6"C) at pH 7 and low ionic strength (I). As pH (6.0-8.0) and I (0.05-1.00) were increased, thermal denaturation temperatures of myosins from tropical, but not cold-water, species decreased. Enthalpies of myofibrillar denaturation decreased for all species with increasing pH and I. Only one thermal transition was detected for myosin at pH 6 and low I, increasing to three as pH and I were increased. Changes in thermal characteristics of myosin subunits over iced and frozen storage suggest more rapid deterioration in cold-water than in tropical fish. The differences in myofibrillar stability of fish from different habitat temperatures have implications for the processing and storage of tropical fish. KeywordsCold-water fish muscle, protein stability, storage, thermal denaturation temperature, warm-water fish muscle.

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“…2 Amongst ®sh species, myosin from cold-water ®sh is more sensitive to changes in the physicochemical environment than myosin from warm-water ®sh. 3 Fish muscle proteins, especially myosin, show an optimal thermal gelation around pH 6.0. 3±6 As the pH increases above this value, the transition temperature of myosin decreases, 5 and this is associated with protein destabilisation and consequently a lower gelforming ability.…”

Section: Introductionmentioning

confidence: 99%

Thermal gelation of brown trout myofibrils from white and red muscles: effect of pH and ionic strength

Lefèvre¹,

Fauconneau²,

Ouali³

et al. 2002

J Sci Food Agric

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The effects of pH and ionic strength on the thermal gelation of brown trout myo®brils from white and red muscles were analysed by thermal scanning rheometry. The highest gelation ability was obtained at low pH (around 5.6) whatever the ionic strength. No effect of ionic strength was observed at pH 5.6; however, at pH 6.0, lowering the salt (KCl) concentration to 0.3 M or less improved the characteristics of the gels formed. The effects of pH and ionic strength on myo®brils from both muscle types appeared to be similar, but red muscle proteins were less sensitive to changes in their physicochemical environment. Consequently, the differences between muscle types appeared to be dependent on pH and ionic strength. Solubility measurements revealed large differences between muscle types and between different pH values. Ultrastructural observations con®rmed that different kinds of gels were formed depending on the physicochemical conditions and muscle type origin. INTRODUCTIONThe thermal gelation properties of myo®brillar proteins have been studied in a large variety of animals. 1 The capacity to produce gels at relatively low temperature is speci®cally observed in aquatic organisms, and this property has been used for processing ®sh myo®brils in surimi-like products. Thermal gelation properties based on interactions between proteins are very dependent on the physicochemical environment, especially pH and ionic strength. 1 Both ionic strength and pH act on myo®bril dissociation prior to heating and on protein charges, which in turn affect protein±protein and protein±solvent interactions during heating. Susceptibility of thermal gelation to physicochemical conditions varies between animal species. Proteins from ®sh are much more sensitive to changes in pH and ionic strength than those from mammals and birds and can form a gel only in a narrow range of pH and salt concentration. 2 Amongst ®sh species, myosin from cold-water ®sh is more sensitive to changes in the physicochemical environment than myosin from warm-water ®sh. 3 Fish muscle proteins, especially myosin, show an optimal thermal gelation around pH 6.0. 3±6 As the pH increases above this value, the transition temperature of myosin decreases, 5 and this is associated with protein destabilisation and consequently a lower gel-

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Myosin thermal stability in fish muscle

Cited by 39 publications

References 15 publications

Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamyspatagonica). A Differential Scanning Calorimetric Study

Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamyspatagonica). A Differential Scanning Calorimetric Study

Thermal stability of fish myofibrils: a differential scanning calorimetric study

Thermal gelation of brown trout myofibrils from white and red muscles: effect of pH and ionic strength

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