Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation

Westphalen, Amity Dawn; Briggs, John; Lonergan, Steven M.

doi:10.1016/j.meatsci.2005.01.015

Cited by 83 publications

(56 citation statements)

References 16 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. Liu et al (2010) also found that the WHC of myosin gel decreased as the pH decreased close to the pI and proteins tended to coagulate due to increased protein-protein interactions.…”

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

confidence: 80%

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: 80%

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 CY at pH 5.5 was also improved with higher salt level (0.6 M). Although WHC was lowest at the isoelectric point (PI) of protein, increased salt levels improved WHC (Westphalen et al, 2005). Thus, CY at high salt level (0.6 M) improved, regardless of the pH value.…”

Section: Cooking Yield and Gel Strengthmentioning

confidence: 96%

Emulsifying and Gelling Properties of Pork Myofibrillar Protein as Affected by Various NaCl Levels and pH Values

Jang¹,

Chin²

2011

Korean Journal for Food Science of Animal Resources

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The effects of various NaCl levels (0, 0.3, and 0.6 M) and pH values (pH 5.0, 5.5, 6.0, and 6.5) on the emulsifying and gelling properties of pork myofibrillar protein (MP) were assessed. The emulsion stability index (ESI), emulsifying activity index (EAI), and creaming index were measured at a 1:20 ratio of MP to corn oil. The EAI and ESI of pork MP showed maximum values at pHs 6.0 and 6.5 and at 0.3 M NaCl, resulting in better emulsion properties. Additionally, the cooking yield (CY) and gel strength (GS) of emulsified MP gel were measured at an MP: corn oil ratio of 1: 2; GS increased with increasing levels of salt. At 0.6 M NaCl, GS decreased with decreasing pH from 5.5 to 6.5. GS and gelling properties were optimal at pH 5.5 in 0.6 M salt. The highest CY was observed at 0.6 M NaCl, regardless of the pH value. However, increasing pH increased CY at salt levels of 0 and 0.3 M. These results indicate that NaCl and pH profoundly affected the emulsified MP system. Future work will be conducted on the rheological properties of the pork emulsified system as affected by adding non-meat protein.

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“…The dynamic oscillatory measurements were performed using a method described by Westphalen, Briggs, and Lonergan (2005) with slight modifications on a rheometer (Anton Paar, Physica MCR 301, Austria) in oscillatory mode. A 25 mm-parallel steel plate geometry with a 500 μm gap was used.…”

Section: Dynamic Rheological Measurementsmentioning

confidence: 99%

“…G 0 in Table 3 is defined as the initial G' before heating. And the rate of gelation from 60 to 80°C is extracted from the slope of the storage modulus versus time (Westphalen et al, 2005), which is associated with the degree of protein unfolding and aggregation. In consequence, it would affect gel properties.…”

Section: Effects Of Ph On the Rheological Properties Of Mp-fg Gelmentioning

confidence: 99%

Thermal gelling properties and mechanism of porcine myofibrillar protein containing flaxseed gum at various pH values

Pan

Feng

Sun

et al. 2016

CyTA - Journal of Food

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Flaxseed gum (FG) was reported to enhance the water holding capacity and thermal stability of myofibrillar protein (MP). However, the role of pH in the interaction of MP and FG is still unclear. The aim of this study was to evaluate gelling properties and physicochemical properties of MP-FG gel at various pH values, to explore the mechanism. The results reveal that higher pH value could increase the water holding capacity of MP-FG gels and the highest gel strength is achieved at pH 6.5. Raman spectroscopic analysis reveals that decreasing the pH from 7.5 to 5.5 induces the partial transformation of α-helices into β-sheets. At the same pH value, addition of FG also leads to the transformation of α-helices into β-sheets, affecting the formation of gel. The storage modulus (G') values and gelation rates during gelation process gradually declines with the increasing pH, which might be conducted to form a fine dense network.Las propiedades térmicas de gelificación y el mecanismo de la proteína miofibrilar porcina que contiene goma de linaza con diferentes valores pH RESUMEN Se declaró que la goma de linaza (FG) mejora la capacidad de retención del agua y la estabilidad térmica de la proteína miofibrilar (MP). Sin embargo, el papel del pH en la interacción de MP y FG aún no está claro. El objetivo de este estudio fue evaluar las propiedades de gelificación y las propiedades fisicoquímicas del gel MP-FG con diferentes valores pH para explorar su mecanismo. Los resultados revelan que un valor pH mayor podría aumentar la capacidad de retención de agua de los geles MP-FG, además la mayor fuerza del gel se consiguió con un pH 6,5. El análisis espectroscópico Raman reveló que reducir el pH de 7,5 a 5,5 induce a la transformación parcial de hélices α a láminas beta β. Con el mismo valor pH, la adición de FG también conlleva a la transformación de hélices α a láminas beta β, afectando la formación de gel. Los valores del módulo de almacenamiento (G') y el índice de gelificación durante el proceso de gelificación se reducen gradualmente con el incremento del pH, lo cual puede conducir a la formación de una densa red. ARTICLE HISTORY

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Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation

Cited by 83 publications

References 16 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

Emulsifying and Gelling Properties of Pork Myofibrillar Protein as Affected by Various NaCl Levels and pH Values

Thermal gelling properties and mechanism of porcine myofibrillar protein containing flaxseed gum at various pH values

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