Gelation of Turkey Breast and Thigh Myofibrils: Changes During Isolation of Myofibrils

NORTHCUlT, J.K.; Lavelle, Christophe; Foegeding, E. Allen

doi:10.1111/j.1365-2621.1993.tb06094.x

Cited by 8 publications

(4 citation statements)

References 24 publications

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“…more concentrated solutions, association may occur between segments of different molecules with network formation. Using a torsion twisting test, and Northcutt et al (1993) reported that, at 8% protein, turkey breast and thigh myofibril gels had equivalent rheological properties. They suggested that protein isoforms were not the major factor influencing gel structure formation.…”

Section: Resultsmentioning

confidence: 99%

Thermal Gelation of Myofibrils from Pork, Beef, Fish, Chicken and Turkey

Lan

Novakofski

McCusker

et al. 1995

Journal of Food Science

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Myofibril gels with 5, 7, or 10% protein and 2% NaCl were prepared from pork, beef, fish, chicken and turkey muscles using a heating rate of 0.7"C/min and pH 6.0 to compare the thermal gelation properties of myofibrillar protein from different species. The force required to rupture gel (Pf), force required to move plunger through gel (Fp), viscosity index (Ni), and elasticity (Ea) increased and cooking loss decreased with increasing protein contents. Myofibrils of chicken breast and thigh had lower and fish and turkey thigh had higher cooking loss at protein contents of 7% or 10%.

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Section: Resultsmentioning

confidence: 99%

Thermal Gelation of Myofibrils from Pork, Beef, Fish, Chicken and Turkey

Lan

Novakofski

McCusker

et al. 1995

Journal of Food Science

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“…The absence of isoform-associated differences has also been seen in fracture properties (i.e., large-strain) of gels determined at 25 °C. Thermally induced gels made from turkey breast and thigh myofibrils have similar stress at fracture and strain at fracture values at 25 °C (Lavelle and Foegeding, 1993;Northcutt et al, 1993). Lavelle and Foegeding (1993) also evaluated G values from the nonfracture region of torsional force-deformation curves.…”

Section: Discussionmentioning

confidence: 99%

Thermally Induced Gelation of Chicken Myosin Isoforms

Liu¹,

Foegeding²

1996

J. Agric. Food Chem.

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Thermally induced gelation of one white muscle myosin (pectoralis) and two red muscle myosins (iliotibialis and gastrocnemius) from chicken was investigated using small-strain oscillatory rheology. In dynamic heating conditions (25-75 °C at 1 °C/min), pectoralis myosin gelled at an onset temperature 5 °C lower and developed a greater storage modulus (G′) than red muscle myosins. Gel curing at 75 °C for 3 h after dynamic heating increased in G′ values, but the relative magnitudes in G′ remained the same for all myosins. The isoform-associated rheological differences at 75 °C were lost when gels were evaluated at 25 °C. This was true for G′ values determined over a 0.16 s interval and G (shear modulus) values after 1 h of imposed strain. Differences were also noted with isothermic gelation (45, 50, or 55 °C). The pectoralis myosin gelled at 45 °C, but the two red muscle myosins did not. The G′ values for pectoralis and iliotibialis myosins gels were not significantly different at 50 °C; however, they were significantly greater than values for gastrocnemius myosin gels. There was no significant differences among the G′ values for gels at 55 °C. These results indicate that the dynamics of gelation and temperature sensitivity of intramatrix forces are different among myosin isoforms. Therefore, any relative evaluation of rheological properties must be under temperature conditions that reflect those typical of the meat product application.

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“…The concentration of extracted myofibrillar protein (pH ≈ 7, I ) 0.3) estimated to be about 7.3 ( 0.9% was determined by drying to obtain the solid content (8.4%) and subtracting from this the estimated potassium chloride content (1.1%). Turkey breast myofibrillar protein was prepared by the method of Northcutt et al (1993). The extracted sample had a solid content of 17.0%, and the concentration of salt (sodium chloride, magnesium chloride, ethylenediamine tetraacetic acid (EDTA), and sodium phosphate) was 3.1% giving an estimated protein concentration (pH ≈ 7.2, I ) 0.75) of 13.9 ( 0.1%.…”

Section: Methodsmentioning

confidence: 99%

Effects of High Pressure on the Myofibrillar Proteins of Cod and Turkey Muscle

Angsupanich

Edde

Ledward

1998

J. Agric. Food Chem.

157

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When turkey breast muscle and isolated myofibrillar protein and myosin of cod or turkey (pH approximately 7) were subjected to pressures up to 800 MPa for 20 min, DSC and electrophoresis (SDS-PAGE) indicated that high pressure-induced denaturation of myosin led to the formation of structures that contained hydrogen bonds and were additionally stabilized by disulfide bonds. Disulfide bonds were also important in heat-induced myosin gels. Hardness of whole cod muscle, estimated by texture profile analysis, showed pressure-treated samples (400 MPa) to be harder than cooked (50 degrees C) or cooked and then pressure-treated or pressure-treated and then cooked samples, supporting the suggestion that pressure induces the formation of heat labile hydrogen-bonded structures while heat treatment gives rise to structures that are primarily stabilized by disulfide bonds and hydrophobic interactions. As expected, turkey myosin is more stable than that of cod; however, it seems their pressure-induced gelation mechanisms are similar.

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Gelation of Turkey Breast and Thigh Myofibrils: Changes During Isolation of Myofibrils

Cited by 8 publications

References 24 publications

Thermal Gelation of Myofibrils from Pork, Beef, Fish, Chicken and Turkey

Thermal Gelation of Myofibrils from Pork, Beef, Fish, Chicken and Turkey

Thermally Induced Gelation of Chicken Myosin Isoforms

Effects of High Pressure on the Myofibrillar Proteins of Cod and Turkey Muscle

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