Binding of Meat Pieces: A Comparison of Myosin, Actomyosin and Sarcoplasmic Proteins as Binding Agents

Macfarlane, J. J.; Schmidt, Gerald D.; Turner, Roy H.

doi:10.1111/j.1365-2621.1977.tb08437.x

Cited by 121 publications

(62 citation statements)

References 15 publications

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“…24 ) In contrast, this investigation with cardiac myosin and reconstituted acto-myosin complexes suggests that myosin alone forms stronger heat-induced gels than actomyosin does. This partly agrees with the observation of Macfarlane et al 6 ) who reported a higher binding power of myosin than that of actomyosin. In previous studies with skeletal muscle actin-myosin complexes, the strongest gels were produced at.…”

Section: Ultrastructural Features Of the Gelsupporting

confidence: 82%

Effects of Temperature, Actin-myosin Ratio, pH, and Salt and Protein Concentrations on Heat-induced Gelling of Cardiac Myosin and Reconstituted Actomyosin

Samejima¹,

Oka²,

Yamamoto³

et al. 1986

Agricultural and Biological Chemistry

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Section: Ultrastructural Features Of the Gelsupporting

confidence: 82%

Effects of Temperature, Actin-myosin Ratio, pH, and Salt and Protein Concentrations on Heat-induced Gelling of Cardiac Myosin and Reconstituted Actomyosin

Samejima¹,

Oka²,

Yamamoto³

et al. 1986

Agricultural and Biological Chemistry

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“…

IntroductionFunctional properties of heat-induced myofibrillar protein gel were important for meat products (Fukazawa et al, 1961;Macfarlane et al, 1977;Siegel and Schmidt, 1979). Gel formation was typically induced by association of unfolded protein molecules via various chemical forces, namely disulfide linkages, electrostatic, hydrophobic interactions, and hydrogen bonds (Mulvihill and Kinsella, 1987;Oakenfull et al, 1997).

…”

mentioning

confidence: 99%

Effects of Ionic Strength on Chemical Forces and Functional Properties of Heat-induced Myofibrillar Protein Gel

Zhang

Yang

Tang

et al. 2015

FSTR

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IntroductionFunctional properties of heat-induced myofibrillar protein gel were important for meat products (Fukazawa et al., 1961;Macfarlane et al., 1977;Siegel and Schmidt, 1979). Gel formation was typically induced by association of unfolded protein molecules via various chemical forces, namely disulfide linkages, electrostatic, hydrophobic interactions, and hydrogen bonds (Mulvihill and Kinsella, 1987;Oakenfull et al., 1997). Functional properties of heat-induced myofibrillar protein gel were mainly depended on chemical forces (Joseph et al., 1994;Wan et al., 1994). Previous literatures have showed the importance of chemical forces in heat-induced protein gels. Smyth et al. (1998) found that hardness of myosin gel could be weakened by adding dithiothreitol (DTT) to prevent the formation of disulfide bonds.Liu and Hsieh (2007) studied the molecular interactions of protein gels by adding DTT, urea and other reagents, and they concluded that non-covalent bonds played a more important role than disulfide bonds in the formation of heat-induced protein gels. Hermansson (1979) found that when less net electric charge were distributed on the surface of protein molecules, the electrostatic repulsion, hydrophobic attractions and intermolecular hydrogen bonds could keep a better balance, which made it easier to form ordered gel network. Hayakawa and Nakai (1985) reported that hydrophobic interactions of myosin were proposed to be the prerequisites for the formation of large aggregates. However, up to now, available data on chemical forces and the relationships between chemical forces and functional properties of MP gel are limited.Raman spectroscopy could be employed to investigate the chemical forces of heat-induced protein gel (Ikeda and Li-Chan, 2004;Li-Chan, 1996;Liu et al., 2011). Tryptophan (Trp) was a hydrophobic amino acid with hydrophobic residues. The normalized intensity of the Raman band near 760 cm −1 was assigned to the stretching vibration of the tryptophan residues ring and could be used to investigate the hydrophobicity of the Trpresidues, and then reflect the hydrophobic interactions of protein gel (Ikeda and Li-Chan, 2004;Li-Chan, 1996;Tu, 1982 -Chan, 2004;Li-Chan, 1996). Zeta potential presents the potential difference between the dispersion medium and the stationary layer of fluid attached to the dispersed particle and can be used to indicate the degree of electrostatic interactions between adjacent, similarly charged particles in a dispersion (Runkana et al., 2004).Several studies had been performed to investigate the effects of ionic strength on functional properties such as G', hardness and WHC (Bjorg et al, 1986;Boyer et al., 1996;Laure et al., 2014;Stone and Stanley, 1994 Materials and MethodsMaterials Six week-old commercial broilers (AA type) were purchased from a commercial chicken farm in Nanjing, China.Bovine serum albumin (BSA) was obtained from Sinopharm Chemical Reagent Co., Ltd (Shanghai, China). All chemicals used were of analytical grade. Methods Extraction of myofibrillar protein ...

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“…Helicity corresponding to the reduced mean residue rotation at 233 nm ([m ' h33) was calculated as described by Samejima et al 23 ) Measurements ofgel strength. Heat-induced gel strength (rigidity) of myosin was estimated by the method of Yasui et al2 4 ) Other conditions (ionic strengths, pH, protein concentrations, temperature) are defined at appropriate places in the text.…”

Section: Methodsmentioning

confidence: 99%

Physicochemical Properties and Heat-induced Gelling of Cardiac Myosin in Model System

Samejima

Hara

Yamamoto

et al. 1985

Agricultural and Biological Chemistry

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Binding of Meat Pieces: A Comparison of Myosin, Actomyosin and Sarcoplasmic Proteins as Binding Agents

Cited by 121 publications

References 15 publications

Effects of Temperature, Actin-myosin Ratio, pH, and Salt and Protein Concentrations on Heat-induced Gelling of Cardiac Myosin and Reconstituted Actomyosin

Effects of Temperature, Actin-myosin Ratio, pH, and Salt and Protein Concentrations on Heat-induced Gelling of Cardiac Myosin and Reconstituted Actomyosin

Effects of Ionic Strength on Chemical Forces and Functional Properties of Heat-induced Myofibrillar Protein Gel

Physicochemical Properties and Heat-induced Gelling of Cardiac Myosin in Model System

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