Muscle Polymorphism and Gelling Properties of Myofibrillar Proteins from Poultry, Mammals, and Fish

Lefèvre, Florence; Culioli, Joseph; Joandel-Monier, S.; Ouali, Ahmed

doi:10.1007/978-1-4615-4731-0_25

Cited by 10 publications

(15 citation statements)

References 127 publications

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“…The solubility of slow muscle myo®brillar protein is reported to be lower than that of fast muscle myo®brillar protein in mammals and poultry, 1,49,50 and this was con®rmed for white and red muscle myo®brils of brown trout. This could be related to a higher extractability of fast muscle proteins due to a higher post mortem proteolysis activity in fast muscle type, 50 but also to characteristics of protein isoforms which demonstrate signi®cant differences in surface hydrophobicity.…”

Section: Effect Of Muscle Typementioning

confidence: 93%

“…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.…”

Section: Introductionmentioning

confidence: 99%

“…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.…”

Section: Introductionmentioning

confidence: 99%

“…The effect of muscle type on the heat-induced gelation of proteins is well documented in mammals and poultry, but only a few studies have been realised in ®sh. 1 Fish skeletal muscle comprises two main muscles which are homogeneous in their ®bre type composition. The red skeletal muscle, located super®cially especially along the lateral line, is composed only of slow-twitch oxidative ®bres.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Effect Of Muscle Typementioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

View full text Add to dashboard Cite

show abstract

“…It is well established that dark muscle and light muscle differ in processing properties due to their respective preponderances in red and white fiber contents that tend to produce different functionalities (Lefevre, Culioli, Joandel-Monier, & Ouali, 1999;Xiong, 1994). Hence, the response of myofibrils isolated from chicken gastrocnemius (red fibers) to phosphate treatment was compared with that of the chicken pectoralis major (white fibers) counterpart.…”

Section: Ultrastructural Changes In Marinated Myofibrilsmentioning

confidence: 99%