Effect of Heating Rate and Protein Concentration on Gel Strength and Water Loss of Muscle Protein Gels

Camou, Juan Pedro; Sebranek, Joseph G.; Olson, D. G.

doi:10.1111/j.1365-2621.1989.tb07897.x

Cited by 81 publications

(53 citation statements)

References 13 publications

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“…The pH, ionic strength, temperature, heating rate, protein concentrations and other factors influenced the WHC (Camou, Sebranek, & Olson, 1989;Chou & Morr, 1979;Huff-Lonergan & Lonergan, 2005;Kristinsson & Hultin, 2003;Westphalen et al, 2005;Yongsawatdigul & Park, 1999). Westphalen et al (2005) found a direct linear relationship between WHC and pH, which was consistent with Offer and Trinick's findings (Offer & Trinick, 1983), and attributed the relationship to the possibility of increased protein-water hydrogen bonding at high pH values.…”

Section: Whc Of the Heat-induced Myofibrillar Gel At 65°csupporting

confidence: 78%

“…The gel strength decreased as the heating rate increased (Camou et al, 1989). The effect of the pH on the rigidity tended to be influenced by the ionic strength (Ishioroshi et al, 1983;Lefevre, Fauconneau, Ouali, & Culioli, 2002).…”

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

confidence: 98%

“…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%

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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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Section: Whc Of the Heat-induced Myofibrillar Gel At 65°csupporting

confidence: 78%

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

confidence: 98%

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

confidence: 99%

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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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“…Additionally, the heating rate plays an important role in gel properties because, if protein aggregation occurs slower than denaturation, more elastic gels are obtained. This suggests that slow heating favors more protein-protein interactions, which results in stronger gels (Camou, Sebranek, & Olson, 1989;Dong & Holley, 2011;Hermansson, 1979).…”

Section: Thermal Gelation Of the Myofibrillar Proteins Of Aquatic Orgmentioning

confidence: 99%

Thermal gelation of myofibrillar proteins from aquatic organisms

Tolano-Villaverde

Torres‐Arreola

Ocaño‐Higuera

et al. 2015

CyTA - Journal of Food

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Gelling ability is attributed to myosin, which is the main myofibrillar protein. Therefore, its integrity is very important. However, a gel with good textural characteristics and stability depends on the inherent characteristics of its proteins, as well as on external factors (primarily temperature, pH, protein concentration and added salt). The best gels from aquatic organism proteins are obtained at a pH value of approximately 7.0. However, the concentration of salt is often variable. In contrast, when proteins are recovered using acid/alkaline dissolution, gels with good textural characteristics are obtained without salt. Hydrophobic interactions, disulfide bonds, hydrogen bonds, and electrostatic interactions are the main interactions that stabilize the protein gel. Thus, this review focuses on the study of the main factors involved in protein gelation, as well as on the extraction method effect on the gelling capacity of proteins from aquatic organisms. Gelificación térmica de proteínas miofibrilares de organismos acuáticos RÉSUMÉMiosina es la principal proteína miofibrilar a la cual se le atribuye la habilidad gelificante, por lo tanto su integridad es muy importante. Sin embargo, las propiedades texturales y estabilidad de los geles depende de las características inherentes de sus proteínas, así como de factores externos (principalmente temperatura, pH, concentración de proteína y sal añadida). En general, los mejores geles proteicos obtenidos de organismos acuáticos se obtienen a pH cercano a 7.0, mientras que la concentración de sal suele ser variable; sin embargo, cuando la recuperación de proteínas se realiza a través de disoluciones ácidas/alcalinas, es posible obtenerse geles con buenas características texturales en ausencia de sal. Las principales interacciones involucradas en la estabilización de geles proteicos son: interacciones hidrofóbicas, puentes disulfuro, puentes de indrógeno e interacciones electrostáticas. Por esta razón, la presente revisión estudia los principales factores involucrados en la gelificación proteica, así como el efecto del método de extracción, sobre la capacidad gelificante de proteínas de organismos acuáticos. ARTICLE HISTORY

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“…The ground tissue was then placed in polyethylene bags, vacuum packaged using a vacuum packaging system (FJ-500XL, Fujee Tech, Korea) and stored at 0 C) for 1 h in a Supra 25 K high speed refrigerated centrifuge (Hanil Science Industrial, Korea). The protein extract was strained through three layers of cheesecloth (Camou et al, 1989). Protein concentrations of the meat solids and supernatant were determined using a Kjeltec® 2300 nitrogen analyzer (Foss Tecator AB, Sweden).…”

Section: Protein Extractionmentioning

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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Effect of Heating Rate and Protein Concentration on Gel Strength and Water Loss of Muscle Protein Gels

Cited by 81 publications

References 13 publications

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

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

Thermal gelation of myofibrillar proteins from aquatic organisms

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

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