Myofibrillar Protein Gelation: Viscoelastic Changes Related to Heating Procedures

Xiong, Youling L.; Blanchard, Suzanne P.

doi:10.1111/j.1365-2621.1994.tb08115.x

Cited by 88 publications

(51 citation statements)

References 17 publications

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“…CyTA -Journal of Food 65 Xiong and Blanchard (1994) found that the myofibrillar protein storage modulus value changed at 46°C during heating, and Samejima, Ishioroshi, and Yasui (1981) found that rabbit myosin had two elastic transition points; one at 43°C and another at 53°C, which is similar to the findings of the present research. The storage modulus and loss modulus values of gel were stable when the temperature rose to about 70°C, which is consistent with the results of myofibrillar proteins (Westphalen, Briggs, & Lonergan, 2006).…”

Section: Rheological Propertiessupporting

confidence: 92%

The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation

Han

Wang

et al. 2014

CyTA - Journal of Food

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2015) The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation,The objective of this study was to track the changes and the relationship between structure and functional properties of rabbit myosin during heat-induced gelation, and to provide more insight into the gelation properties of rabbit myosin. Storage modulus (G′) and loss modulus (G′′) during the heat-induced gelation process were measured by a rheometer, and the water holding capacity (WHC) and hardness of the heatinduced gel were measured by centrifugation method and texture analyzer, respectively. The quantitative analysis of secondary structural content was performed by circular dichroism (CD). The CD data were fitted to three secondary structures, which were α-helix, β-sheet, and random coil. The results showed that the WHC, hardness, G′, G′′, β-sheet, and random coil increased with the increase of temperature, while the α-helix decreased. The changes of structural properties of myosin determined the functional properties during the heat-induced gelation process, and they had a very strong correlation.El objetivo de este estudio consistió en dar seguimiento a los cambios ocurridos durante la gelificación inducida por calor y a la relación existente entre la estructura y las propiedades funcionales de la miosina de conejo durante dicho proceso. Asimismo, el estudio pretendió generar más información acerca de las propiedades de gelificación de la miosina de conejo. En el transcurso del proceso de gelificación inducida por calor, se midieron el módulo de almacenamiento (G′) y el módulo de pérdida (G′′) mediante el uso del reómetro; mientras que, la capacidad de retención de agua (WHC) y la dureza del gel inducida por el calor, fueron medidas empleando el método de centrifugación y el analizador de textura, respectivamente. El análisis cuantitativo del contenido estructural secundario fue realizado mediante dicroísmo circular (CD). Los datos obtenidos a partir del CD se aplicaron a tres estructuras secundarias: hélice α, lámina β, y espiral al azar (random coil). Los resultados demostraron que cuando se incrementó la temperatura, la WHC, la dureza, G′, G′′, la lámina β y la espiral al azar aumentaron, mientras que la hélice α disminuyó. Los cambios experimentados por las propiedades estructurales de la miosina determinaron las propiedades funcionales durante el proceso de gelificación inducida por calor, demostrando, además, un grado de correlación muy alto.

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Section: Rheological Propertiessupporting

confidence: 92%

The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation

Han

Wang

et al. 2014

CyTA - Journal of Food

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“…Such a profile has been reported with minced meat from rainbow trout (Autio et al, 1989) and carp actomyosin paste (Sano et al, 1989), and also with myofibrillar protein solution from rabbit (Culioli et al, 1993;Boyer et al, 1996a), poultry (Xiong and Blanchard, 1994) and beef myosin (Fretheim et al, 1986).…”

Section: White Muscle Rheological Measurementsmentioning

confidence: 69%

“…Compared with rabbit (Boyer et al, 1996a) and poultry (Xiong and Blanchard, 1994), using similar measurement conditions, brown trout seemed to have low gelling ability.…”

Section: White Muscle Rheological Measurementsmentioning

confidence: 87%

Thermal Gelation of Brown Trout Myofibrils: Effect of Muscle Type, Heating Rate and Protein Concentration

Lefèvre

Fauconneau

Ouali³

et al. 1998

Journal of Food Science

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The thermal gelation properties of myofibril solutions (KCl 0.6M; pH 6.0) from reared brown trout white and red muscles were analyzed by thermal scanning rheometry. With a heating rate of 1°C/min, red muscle myofibrils exhibited a lower gelation capacity than white muscle myofibrils at low temperatures. No difference was observed above 60°C where solid gels were formed from the two myofibril types. Increasing protein concentration or reducing heating rate increased the values of the rheological parameters at 80°C for the two muscle type myofibrils. With a low heating rate (0.25°C/min), white muscle myofibrils formed stronger gels whatever the temperature.

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“…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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Myofibrillar Protein Gelation: Viscoelastic Changes Related to Heating Procedures

Cited by 88 publications

References 17 publications

The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation

The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation

Thermal Gelation of Brown Trout Myofibrils: Effect of Muscle Type, Heating Rate and Protein Concentration

Optimization of conditions for myofibril preparation from mechanically recovered chicken meat

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