FUNCTIONAL DIFFERENCES OF MYOFIBRILLAR PROTEINS FROM FAST AND SLOW TWITCH MUSCLES<sup>1</sup>

Foegeding, E. Allen; Liu, M.N.

doi:10.1111/j.1745-4573.1995.tb00561.x

Cited by 9 publications

(7 citation statements)

References 47 publications

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“…However, signi®cant rigidity was observed in such gels composed of an irregular matrix, as we used nondestructive conditions of measurement which protect the gel from any disruption. 57 Such a heterogeneous structure of the gels from red muscle myo®brils has previously been described for rabbit myo®brils. 33 …”

Section: Effect Of Muscle Typementioning

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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Section: Effect Of Muscle Typementioning

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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“…However, the primary sequences of both fast and slow myosin isoforms would be necessary to confirm our hypothesis and predict such an structural model. Unfortunately, only very few amino acid sequences of myosin isoforms have been determined yet (Foegeding and Liu 1995).…”

Section: Changes In Hydrophobicity Of Slow and Fast Myosins During Hementioning

confidence: 99%

Determination of Surface Hydrophobicity of Fast and Slow Myosins from Rabbit Skeletal Muscles: Implication in Heat-Induced Gelation

Boyer¹,

Joandel²,

Ouali³

et al. 1996

J. Sci. Food Agric.

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Both aliphatic and aromatic surface hydrophobicities of myosins from fast‐twitch psoas majorand slow‐twitchsemimembranosus propriusmuscles were investigated using fluorescence probes (cis‐parinaric acid and 8‐analino‐1‐naphthalene sulphonic acid). Surface hydrophobicity of unheated slow myosin was 1·5‐fold higher than that of fast myosin. However, heating led to an increased enhancement of fast myosin hydrophobicity which became, after heating, higher than that exhibited by heated slow myosin. Whatever the myosin isoforms, most surface hydrophobicity was on the myosin heads. Heating induced a rise in hydrophobicity of the S1‐subfragment from slow and fast myosins. However, the hydrophobicity of rods from fast myosin was increased three‐fold more by heating than did that from slow myosin. Finally, the blocking of hydrophobic binding sites affected differently the heat‐induced gelation in high ionic strength (0·6MKCl) of both myosin isoforms and confirmed that the molecular mechanisms involved in the gelation were muscle‐type dependent.

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“…Bovine muscles are often classified by fiber type based on twitch speed (slow or fast), appearance (red or white), or metabolism (oxidative or glycolytic) (1). Common adult bovine skeletal muscle types are I (slow, oxidative, red), IIb (fast, glycolytic, white), and IIa (fast, oxidative, intermediate) (2).…”

Section: Introductionmentioning

confidence: 99%

“…Numerous researchers have reported differences in the quality of products made from light (white) and dark (red) meat, although the reasons for these differences are poorly understood (3). Many of these differences have been attributed to myosin isoform; however, the results have been confounded by the presence of many other muscle proteins within the test system and by the lack of pH control or the use of only a single pH (1).…”

Section: Introductionmentioning

confidence: 99%

Denaturation and Aggregation of Myosin from Two Bovine Muscle Types

Vega-Warner

Smith

2001

J. Agric. Food Chem.

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The thermal behaviors of myosin from bovine vastus intermedius (VI, predominantly red muscle) and semimembranosus (SM, predominantly white muscle) at pH 6.05 (ultimate pH of VI muscle) and 5.50 (ultimate pH of SM muscle) were compared. Differential scanning microcalorimetry and turbidity measurements were used to monitor changes in myosin during heating from 25 to 80 degrees C at 1 degrees C/min. VI and SM myosin heavy chain isoforms were identified on gradient SDS-PAGE. Endotherms of VI myosin at pH 6.05 had three transition temperatures (T(m)) of 45, 53, and 57 degrees C, whereas at pH 5.50 two transitions were observed at 42 and 59 degrees C. SM myosin had two T(m) values of 46 and 58 degrees C at pH 6.05 and T(m) values of 43 and 62 degrees C at pH 5.5. SM myosin at its ultimate pH was less heat stable than VI myosin at its ultimate pH; however, when SM and VI myosin were compared at the same pH, VI myosin was less stable.

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FUNCTIONAL DIFFERENCES OF MYOFIBRILLAR PROTEINS FROM FAST AND SLOW TWITCH MUSCLES¹

Cited by 9 publications

References 47 publications

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

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

Determination of Surface Hydrophobicity of Fast and Slow Myosins from Rabbit Skeletal Muscles: Implication in Heat-Induced Gelation

Denaturation and Aggregation of Myosin from Two Bovine Muscle Types

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FUNCTIONAL DIFFERENCES OF MYOFIBRILLAR PROTEINS FROM FAST AND SLOW TWITCH MUSCLES1

Cited by 9 publications

References 47 publications

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

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

Determination of Surface Hydrophobicity of Fast and Slow Myosins from Rabbit Skeletal Muscles: Implication in Heat-Induced Gelation

Denaturation and Aggregation of Myosin from Two Bovine Muscle Types

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FUNCTIONAL DIFFERENCES OF MYOFIBRILLAR PROTEINS FROM FAST AND SLOW TWITCH MUSCLES¹