Ionic Strength Effects on Heat‐induced Gelation of Myofibrils and Myosin from Fast‐ and Slow‐twitch Rabbit Muscles

Boyer, C S; Joandel, S.; Ouali, Ahmed; Culioli, Joseph

doi:10.1111/j.1365-2621.1996.tb10949.x

Cited by 32 publications

(34 citation statements)

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“…6. Changes of G' with lower ionic strength had a myosin usually existed in a monomeric or dimeric form (Boyer et al, 1996). In high ionic strength solutions, protein swelled, unfolded and became flexible upon absorbing solvent.…”

Section: Effects Of Ionic Strength On Functional Properties Of Mp Gelmentioning

confidence: 99%

“…With high ionic strength (0.6 mol/L KCl), myosin usually existed in a monomeric or dimeric form, after denaturation, myosin formed aggregated particles, cross-linking with each other to form a more uniform network structure with small pores and good porosity to hold more water molecules (Boyer et al, 1996;Samejima et al, 1986;Sharp and Offer, 1992).…”

Section: Samejimamentioning

confidence: 99%

“…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 …”

Section: Introductionmentioning

confidence: 99%

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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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Section: Effects Of Ionic Strength On Functional Properties Of Mp Gelmentioning

confidence: 99%

Section: Samejimamentioning

confidence: 99%

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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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“…La técnica de reestructurar permite la comercialización de especies de bajo valor comercial así como la utilización de restos del fileteado de especies comerciales (Noriega-Rodríguez et al, 2009;Pacheco-Aguilar et al, 2010). Las proteínas miofibrilares (concretamente la miosina) son las responsables de la agregación inducida por calor incluyendo los mecanismos de gelificación y unión proteica (Boyer et al, 1996). El nivel de sal utilizado es importante y determina la cantidad de exudado proteico que posteriormente actuará como agente ligante permitiendo la agregación proteica.…”

Section: I3 Tendencias Del Mercado De Pescado Nuevos Productos Prunclassified

“…La fuerza iónica generada en la matriz proteica influye en la forma en la que se ligan las proteínas (miosina). Así pues, se ha observado que a baja fuerza iónica las agregaciones que se producen son inducidas por uniones laterales entre las cadenas de miosina, mientras que a alta fuerza iónica se producen uniones entre las cabezas de las cadenas de miosina, lo que implicará un sistema mucho más estructurado (Boyer et al, 1996;.…”

Section: I3 Tendencias Del Mercado De Pescado Nuevos Productos Prunclassified

Aplicación de nuevas tecnologías para el diseño y desarrollo de productos de dorada (Sparus aurata) procedente de acuicultura

Bello¹,

Desamparados²

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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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Ionic Strength Effects on Heat‐induced Gelation of Myofibrils and Myosin from Fast‐ and Slow‐twitch Rabbit Muscles

Cited by 32 publications

References 34 publications

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

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

Aplicación de nuevas tecnologías para el diseño y desarrollo de productos de dorada (Sparus aurata) procedente de acuicultura

Thermal gelation of brown trout myofibrils from white and red muscles: effect of pH and ionic strength

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