Changes in Protein Solubility and Gelation Properties of Chicken Myofibrils during Storage

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

doi:10.1111/j.1365-2621.1989.tb05941.x

Cited by 107 publications

(70 citation statements)

References 34 publications

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“…As the gel strength decreased beyond this period, the proportion of actin increased progressively. These results are in agreement with those of Martinez et a/ (1986) and Xiong and Brekke (1989), which showed an improved gelling ability as the M/A ratio increased. It is therefore likely that the MHC/A ratio has a major influence on the gelling properties of the actomyosin isolated from fish of different post-mortem history.…”

Section: Electrophoretic Studies On Natural Actomyosin During Ageing supporting

confidence: 95%

“…Other authors have observed an increase in the MHC/A ratio of actomyosin of chicken myofibrils during storage for 24 h at refrigerated temperatures in 0.6 M KCl and that this was in parallel with an increase in the gel rigidity of these myofibrils (Xiong and Brekke 1989). Some authors have tried to use the MHC/A ratio as an index for predicting the strength of surimi gels (Martinez et a1 1986).…”

Section: Electrophoretic Studies On Natural Actomyosin During Ageing mentioning

confidence: 96%

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Properties of actomyosin isolated from cod (Gadus morhua) after various periods of storage in ice

Chalmers¹,

Careche²,

Mackie³

1992

J Sci Food Agric

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Natural actomyosin was isolated from cod (Gadus rnorhua L) stored in ice for up to 28 days. The gelling properties, apparent viscosity, Ca2+-ATPase activity and component protein composition by sodium dodecyl sulphate (SDS) electrophoresis were determined for each preparation of natural actomyosin. The apparent viscosity, protease activity, trimethylamine (TMA) content and p H of the fish muscle were also determined. The results showed that the apparent viscosity and Ca2+-ATPase activity tended to decrease slightly during ageing of the fish in ice, whereas some of the gelling properties showed a maximum between 3 and 6 days of storage. However, there was no change in the apparent viscosity of the muscle as a whole even after the fish were considered to be stale according to the TMA values. The ratio of myosin heavy chain to actin in the actomyosin changed with the time of storage of the fish, being highest at 3 days when gelling properties were maximal and decreasing progressively thereafter.

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Section: Electrophoretic Studies On Natural Actomyosin During Ageing supporting

confidence: 95%

Section: Electrophoretic Studies On Natural Actomyosin During Ageing mentioning

confidence: 96%

Properties of actomyosin isolated from cod (Gadus morhua) after various periods of storage in ice

Chalmers¹,

Careche²,

Mackie³

1992

J Sci Food Agric

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show abstract

“…Their relative solubility is dependent gels that were stronger than those of myosin dependent not only o n ionic strength, pH (Richardson from red (leg) muscle. These findings were substantiated and Jones 1987), species (Amato et al 1989) and postlater by several studies (Fretheim et a1 1986;Foegeding 1987;Xiong and Brekke 1989), although some * To whom correspondence should be addressed.…”

Section: Introductionsupporting

confidence: 67%

Protein extractability and thermal gel formability of myofibrils isolated from skeletal and cardiac muscles at different post‐mortem periods

et al. 1992

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Abstract:The effects of the post-mortem ageing period on the extractability of myofibrillar proteins from pork cardiac and rabbit skeletal muscles under various conditions of pH and ionic strength were studied with particular reference to the changes in the solubility of individual myofibrillar proteins and their denaturation characteristics. The ultimate influence of these changes on the heat-induced gel forming ability of myofibrils isolated from cardiac and skeletal muscles at different post-mortem stages was also investigated.Results showed that pork cardiac myofibrils always exhibited lower solubility than those from rabbit skeletal muscles under identical conditions of pH, ionic strength and temperature. SDS-PAGE profiles indicated several quantitative differences in the relative proportion of individual protein species present in cardiac and skeletal myofibrils. The solubility of various proteins present in myofibrils was also affected differently on heating in 0.1 and 0.6 M NaCl solution at various pH values. Thermal denaturation of cardiac myofibrils occurred at about 10°C higher than that of skeletal myofibrils as revealed by differential scanning calorimetry. Cardiac myofibrils formed much weaker heat-induced gels than those produced by skeletal myofibrils under identical conditions of temperature, pH, ionic strength and protein content.

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“…Viscosity of myosin within pH range from 5.4 to 6.0 [14] and at pH 7.0 [2], myofibrillar proteins at pH 6.5 [19], myofibrils at pH 6.0 [20] and SSP within pH range from 5.75 to 8.0 [25] from chicken or hen breast muscles was greater than from leg/thigh muscles. The differences in viscosity of myosin from white and red muscles could be attributed to different shapes of these molecules.…”

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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Changes in Protein Solubility and Gelation Properties of Chicken Myofibrils during Storage

Cited by 107 publications

References 34 publications

Properties of actomyosin isolated from cod (Gadus morhua) after various periods of storage in ice

Properties of actomyosin isolated from cod (Gadus morhua) after various periods of storage in ice

Protein extractability and thermal gel formability of myofibrils isolated from skeletal and cardiac muscles at different post‐mortem periods

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

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