Protein Extractability and Thermally Induced Gelation Properties of Myofibrils Isolated from Pre‐ and Postrigor Chicken Muscles

Xiong, Youling L.; Brekke, C. J.

doi:10.1111/j.1365-2621.1991.tb08013.x

Cited by 90 publications

(61 citation statements)

References 42 publications

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“…After chilling to room temperature, samples were ®xed in 4% paraformaldehyde and 0.1% glutaraldehyde for 1 h at 4°C. Post-®xation was performed in 0.2% osmium tetroxide and the samples were gradually dehydrated in ethanol baths (25,50,75, 95 and 100% successively). Samples were dried using carbon dioxide critical point drying, coated with a 25 nm gold layer in a vacuum evaporator and analysed with a Philips 505 scanning electron microscope (Philips Electronique Industrielle SA, Limeil, Brevannes, France) at an accelerating voltage of 25 kV.…”

Section: Scanning Electron Microscopy (Sem)mentioning

confidence: 99%

“…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: 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: Scanning Electron Microscopy (Sem)mentioning

confidence: 99%

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

View full text Add to dashboard Cite

show abstract

“…Literature analysis of the values of molecular weight and electrophoretic separation of proteins from muscle tissues made it possible to find a series of different proteins in the myofibril preparation [26,28,30,32]. Probably above the myosin heavy chain band (205 kDa), cytoskeletal proteins such as e.g.…”

Section: Electrophoretic Analysismentioning

confidence: 99%

Optimization of conditions for myofibril preparation from mechanically recovered chicken meat

Stangierski¹,

Kijowski

2000

Nahrung

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The influence of various conditions affecting the isolation of a myofibrillar preparation (MP) from chicken mechanically recovered meat (MRM), i.e. the time of additional chopping in a bowel chopper, washing time, the number of washings, and the water to MRM ratio, on the recovery of dry matter and myofibrillar protein, and fat content in the preparation was investigated. The following particular steps were determined to be the most desirable parameters: chopping MRM for 10 minutes, washing time of 15 minutes, 3 (or 2) consecutive washings, 3:1 water to MRM ratio (v/w). Under these conditions a significant decrease of fat content (93% on average) was found in comparison to the content in MRM. The removal of fat, sarcoplasmic protein and connective tissue increased the concentration of myofibrillar protein. The number of aqueous washings of MRM had the biggest influence on the protein and fat content in the concentrate. Electrophoretic analysis (SDS-PAGE) of protein in the preparation obtained under optimal conditions showed that myosin heavy chains (MHC) and actin constituted approximately 50% of all the proteins in the preparation.

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“…The differences in viscosity of myosin from white and red muscles could be attributed to different shapes of these molecules. Moreover, the discrepancy in viscosity between white and red myofibrils or salt soluble proteins could be explained by pH dependent differences in extractability of myofibrillar proteins from chicken or hen breast and leg/thigh muscles [20,21,22,24] or by different fibrils distribution in both muscles [1,8,18] and resulting from these differences in size and composition [6,20] as well as occurrence of myosin, troponin and tropomyosin isoforms [6,17,20,21].…”

Section: Introductionmentioning

confidence: 99%

Apparent viscosity of chicken muscle homogenates. Influence of pH and muscle type

Lesiów¹

2000

Nahrung

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The effect of pH and type of muscle on apparent viscosity of chicken breast, thigh and combined B/T muscles was investigated. The apparent viscosity of thigh muscle homogenate at pH from 5.8 to 6.6, and combined B/T muscle homogenate at pH from 5.8 to 6.3 was increasing. The apparent viscosity of breast muscle homogenate increased with pH increase, reaching a maximum at pH 6.3 and then decreased. When pH raised from 5.8 to 6.3, breast muscle homogenate apparent viscosity increased 3.5-6.0 times more than apparent viscosity of thigh muscle homogenate. An increase of combined B/T muscle homogenate apparent viscosity under shear rate 0.3333-48.6 (s-1) was approximately an average of increases for its individual muscles. At pH 5.8 and 6.0, apparent viscosity of thigh muscle homogenate was approximately two times higher than that of breast muscle homogenate, and reversibly, at pH 6.3, breast muscle homogenate apparent viscosity was about 20% higher than that of thigh muscle homogenate. The apparent viscosity of combined B/T muscle homogenate at pH 5.8 and 6.0, was greater than apparent viscosity of breast muscle homogenate, and at pH 6.3, was greater than apparent viscosity of thigh muscle homogenate. The present data extend the results reported by other researches that there are remarkable differences not only in functional and rheological properties of myofibrillar proteins (SSP, myosin) but also in those of homogenates from chicken white and red muscles.

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Protein Extractability and Thermally Induced Gelation Properties of Myofibrils Isolated from Pre‐ and Postrigor Chicken Muscles

Cited by 90 publications

References 42 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

Optimization of conditions for myofibril preparation from mechanically recovered chicken meat

Apparent viscosity of chicken muscle homogenates. Influence of pH and muscle type

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