Role of secondary structures in the gelation of porcine myosin at different pH values

Liu, Ru; Zhao, Siming; Xiong, Shanbai; Xie, Bijun; Qin, Lihong

doi:10.1016/j.meatsci.2008.02.014

Cited by 300 publications

(145 citation statements)

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“…The initial increase in G′ trend indicated the onset of gelation or the formation of the preliminary elastic protein network, which was probably due to the unfolding and cross-linking of heavy meromyosin (Egelandsdal, Fretheim, & Samejima, 1986;Jiang & Xiong, 2013). The temporary decrease in G′ was attributed to the denaturation of the myosin tails, which involved the disentanglement of noncovalent, short-term intermolecular interactions to increase the mobility of muscle proteins (Liu, Zhao, Xiong, Xie, & Qin, 2008;Xiong, 1997). On further heating, the formation of hydrophobic and sulfhydryl-disulfide interactions created the cross-links between protein aggregates or strands for an increase in G′, indicating the transformation of the viscous sol into an elastic gel network (Ferris, Sandoval, Barreiro, Sánchez, & Müller, 2009;Zhao et al, 2014).…”

Section: Storage Modulus (G′)mentioning

confidence: 99%

A comparative study of chemical composition, color, and thermal gelling properties of normal and PSE-like chicken breast meat

Li¹,

Chen²,

Zhao³

et al. 2014

CyTA - Journal of Food

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The objective of this study was to evaluate the differences between normal and pale, soft, exudative (PSE)-like chicken breast meat in the chemical composition, pH, color, water binding capacity, textural properties, salt-soluble protein (SSP) extraction as well as dynamic rheological properties. Compared with normal meat, PSE-like chicken meat showed similar moisture, fat, and ash content (P > 0.05), but significantly lower protein content (P < 0.05). It had a significantly higher L* and lower pH and SSP extraction (P < 0.05). Heated PSE-like meat batter had lower water-binding capacity, textural characteristics (P < 0.05) and reduced gel elasticity (G′) and viscosity. However, the color variation of PSE-like meat gels was decreased. No significant changes were observed in the SSP electrophoretic patterns by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). In conclusion, PSE-like poultry meat changed the chemical composition and impaired protein functionality; however, the difference in color was small when used in further products.Keywords: PSE-like; chicken; gel properties; salt-soluble protein; dynamic rheology El objetivo del presente estudio se dirigió a evaluar las diferencias existentes entre la carne de pechuga de pollo normal y la de tipo PSE en términos de su composición química, pH, color, capacidad de retención de agua, propiedades texturales, extracción de proteína soluble en sal (PSS), así como sus propiedades reológicas dinámicas. En comparación con la carne de pollo normal, se constató que la carne de pollo tipo PSE exhibe un contenido de humedad, de grasa y de ceniza similar (P > 0,05), mientras que su contenido de proteína es significativamente inferior (P < 0,05). Asimismo, se observó que la carne tipo PSE tiene un nivel de L* más elevado, en tanto su pH y su extracción SSP son inferiores (P < 0,05). Al ser calentada, la masa de carne tipo PSE acusa niveles inferiores de capacidad de retención de agua, de características texturales (P < 0,05), reduciéndose, al mismo tiempo, la elasticidad de gel (G′) y la viscosidad. Sin embargo, en los geles de carne tipo PSE se constató la disminución de la variación de color. Frente a la aplicación de la SDS-PAGE, no se observaron cambios significativos en los patrones electroforéticos en la PSS. Se concluye que la composición química de la carne de pollo tipo PSE se ve alterada, lo cual limita su funcionalidad proteica. Sin embargo, la diferencia de color es reducida si se utiliza en productos posteriores.

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Section: Storage Modulus (G′)mentioning

confidence: 99%

A comparative study of chemical composition, color, and thermal gelling properties of normal and PSE-like chicken breast meat

Li¹,

Chen²,

Zhao³

et al. 2014

CyTA - Journal of Food

View full text Add to dashboard Cite

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“…The water holding capacity of a hydrocolloid gel can be attributed to increasing moisture content with increasing levels of konjac (Osburn and Keeton, 2004). In general, the increased water holding capacity can be largely attributed to the total amount of solubilized myosin, since myosin is largely responsible (Choi et al, 2011; Nakayama and Sato, 1971), and heat-induced gel requires the association of myosin and actin chains, which produces a continuous three-dimensional network in which water is captured (Liu et al, 2008).…”

Section: Resultsmentioning

confidence: 99%

Interactions between Chicken Salt-soluble Meat Proteins and Makgeolli Lees Fiber in Heat-induced Gels

Choi¹,

Park²,

Kim³

et al. 2011

Korean Journal for Food Science of Animal Resources

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The technological effects of Makgeolli lees fiber (0, 0.5, 1.0, 2.0, and 4.0%) on chicken salt-soluble breast meat proteins in a model system on proximate composition, physicochemical properties, and textural properties were investigated. Makgeolli lees fiber was obtained from Makgeolli brew processing, and the by-products showed good dietary fiber. The moisture and ash contents, water holding capacity, redness, yellowness, hardness, and apparent viscosity of chicken salt-soluble meat protein heat-induced gel systems with Makgeolli lees fiber were all higher than the control without Makgeolli lees fiber. However, protein solubility and electrophoretic patterns did not differ among the control and treatments with Makgeolli lees fiber samples. The chicken salt-soluble protein heat-induced gel systems incorporating Makgeolli lees fiber had improved water holding capacity, textural properties, and viscosity due to Makgeolli lees fiber addition. These results suggest that the addition of 4.0% Makgeolli lees fiber to gel is helpful to improve the physical properties of heat-induced gels.

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“…Gel strength, which was evaluated as rigid, was influenced by many factors according to previous studies (Camou et al, 1989;Ishioroshi et al, 1983;Lesiów & Xiong, 2001;Liu et al, 2010), such as the heating rate, pH, ionic strength, the lengths of the filaments before heating and the addition of other components like ATP, most of which mainly functioned by affecting protein-protein attractive interactions (hydrogen bonds, ionic bonds, sulfhydryl bonds and hydrophobic interactions), repulsive interactions (mainly electrostatic but also sometimes steric) and proteinwater interactions (Liu, Zhao, Xiong, Xie, & Qin, 2008). The gel strength decreased as the heating rate increased (Camou et al, 1989).…”

Section: Gel Strength Of Heat-induced Myofibrillar Gel At 65°cmentioning

confidence: 99%

The mechanics of formation of heat-induced myofibrillar protein gel from rabbitpsoas major

Wei

Cui

Jamali

et al. 2016

CyTA - Journal of Food

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(2017) The mechanics of formation of heat-induced myofibrillar protein gel from rabbit psoas major, CyTA -Journal of Food, 15:2, 181-190, DOI: 10.1080/19476337.2016 To link to this article: https://doi.org/10. 1080/19476337.2016 The present study was designed to analyze the formation mechanics of heat-induced myofibrillar gels from rabbit psoas major at 0.6 mol/L KCl (pH 6.5) and 0.2 mol/L KCl (pH 6.0; n = 3). Morphological structure changes were observed using phase-contrast microscopy, transmission electron microscopy, scanning electron microscopy (SEM) and gel properties were determined through water-holding capacity (WHC), gel strength and dynamic rheological test. The results revealed that myofibrillar filaments aggregated and formed larger oligomers by side-by-side interactions when heated from 25 to 65°C. In higher ionic strength at higher pH, the filaments formed a more compact homogeneous network structure and the G′ value was much lower with higher WHC and gel strength, suggesting that the myofibril gel properties could be described by ΔG′. Based on the present study, it is suggested that the desired structural and textural attributes of myofibril gel can be manipulated by temperature, ionic strength and pH.El mecanismo de la formación de gel proteínico miofibrilar inducido con calor de psoas mayor de conejo RESUMEN El presente estudio se diseñó para analizar la formación de los mecanismos de geles miofibrilares inducidos con calor de psoas mayor de conejo (PM) a 0,6 mol/L de KCl (pH 6,5) y 0,2 mol/L de KCl (pH 6,0) (n=3). Se observaron cambios en la estructura morfológica utilizando microscopio de contraste de fase, microscopio electrónico de transmisión (TEM) y microscopía electrónica de barrido (SEM), además se determinaron las propiedades del gel examinando la capacidad de retención de agua, la resistencia del gel y el ensayo reológico dinámico. Los resultados revelaron que los filamentos miofibrilares agregaron y formaron oligómeros más grandes mediante interacciones conjuntas cuando se calentaron de 25°C a 65°C. Con la mayor fuerza iónica y el mayor pH, los filamentos formaron una estructura de red homogénea más compacta y el valor G' fue más bajo con los mayores valores de WHC y resistencia del gel, sugiriendo que las propiedades miofibrilares del gel podrían describirse con ΔG'. En base al presente estudio, se sugiere que los atributos estructurales y texturales deseados del gel miofibrilar pueden ser manipulados con la temperatura, la fuerza iónica y el pH.

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Role of secondary structures in the gelation of porcine myosin at different pH values

Cited by 300 publications

References 31 publications

A comparative study of chemical composition, color, and thermal gelling properties of normal and PSE-like chicken breast meat

A comparative study of chemical composition, color, and thermal gelling properties of normal and PSE-like chicken breast meat

Interactions between Chicken Salt-soluble Meat Proteins and Makgeolli Lees Fiber in Heat-induced Gels

The mechanics of formation of heat-induced myofibrillar protein gel from rabbitpsoas major

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