Effect of pH on the gel properties and secondary structure of fish myosin

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

doi:10.1016/j.foodchem.2009.12.030

Cited by 156 publications

(81 citation statements)

References 37 publications

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“…δ Exhibited almost the exact opposite pattern of G′, except for the initial obvious decrease which indicated preliminary protein-protein interactions and network development (Liu et al, 2010). Further heating above 55°C resulted in a sudden decrease in δ indicating that the transition from sol to gel occurred, which occurred at a higher temperature than the one in 0.6 mol/L KCl; this result is consistent with the SEM results in Figure 3.…”

Section: Rheological Properties Of Myofibril Solutions During Heatingsupporting

confidence: 88%

“…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. Xiong and Brekke (1989) showed that increasing the negative charges on proteins above the pI resulted in strengthened proteinwater interactions and weakened protein-protein interactions, which contributed to improving the WHCs of myofibril gels.…”

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

confidence: 87%

“…The rheological thermogram (Figure 4(a)) indicated that the transition temperature during gelation was approximately 58°C (Wu, Xiong, Chen, Tang, & Zhou, 2009). As the temperature increased to 65°C, a denser elastic gel matrix had formed through compact and extensive cross-links and diversified protein-protein interactions (Figure 3(e)) with the δ lower than 5° (Liu et al, 2010).…”

Section: Rheological Properties Of Myofibril Solutions During Heatingmentioning

confidence: 99%

“…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%

“…That is, the main reason for various gel strengths is the solubility of the proteins, which explained the higher gel strength in 0.6 mol/L KCl in Table 1. In some studies, gel strength was described as a function of salt concentration (Hermansson et al, 1986), and some even expressed gel strength using the storage modulus (Liu et al, 2010).…”

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: Rheological Properties Of Myofibril Solutions During Heatingsupporting

confidence: 88%

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

confidence: 87%

Section: Rheological Properties Of Myofibril Solutions During Heatingmentioning

confidence: 99%

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

confidence: 99%

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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The interaction mechanism of different ionic polysaccharides with myofibrillar protein and its contribution to the heat‐induced gels

Li,

Lin,

Jiang

et al. 2024

Food Frontiers

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Polysaccharides are widely used as quality improvers for meat products. However, the mechanisms of how different ionic polysaccharides regulate the gelling properties of myofibrillar protein (MP) are still unclear. This study aimed to elucidate the contribution of different ionic polysaccharides to MP gelation and its mechanism. The enhancement of hydrogen bond, hydrophobic interaction, and disulfide bond between carboxymethyl cellulose sodium (CMC‐Na, anionic polysaccharide) and MP made them bind tightly, which contributes to the improvement of gel strength, water‐holding capacity, and viscoelasticity. Konjac glucomannan (neutral polysaccharide) mainly relied on physical filling to support the gel network and improve the gel characteristics. The electrostatic attraction between cationic polysaccharides and MP enhanced the binding between them. However, due to the large structure of chitosan (cationic polysaccharide) sugar chain, it can only attach to the surface of protein, which limits the interaction between them. These findings will provide guidance for the application of polysaccharides as food quality improvers or fat substitutes and the design of new low‐fat restructured meat products.

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Quality evaluation of surimi and fish nuggets from Queen fish (Scomberoides commersonnianus)

Moosavi‐Nasab

Asgari

Oliyaei

2019

Food Science & Nutrition

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The purpose of this study was formulation and evaluation of physicochemical properties of fish and surimi nuggets prepared from Queen fish (Scomberiodes commersonnianus) during 90 days of storage. Chemical analysis showed that surimi nuggets contained less protein, fat, and ash due to washing steps during surimi preparation. The titratable acidity, peroxide, and TBA values for fish nuggets were significantly higher than surimi nuggets during frozen storage (p < .05). Moreover, the textural properties of the products exhibited more firmness of surimi nuggets before cooking compared with fish nuggets (p < .05) and more firmness of fish nuggets after cooking compared with surimi one (p < .05). Furthermore, surimi nuggets were lighter and had lower total bacterial counts rather than fish nuggets during frozen storage (p < .05). SDS‐PAGE of the samples during storage exhibited more intensity of the bands related to α‐actinin, actin, and β‐tropomyosin in surimi nuggets compared with that for fish nuggets. Moreover, the sensory evaluation showed that acceptability of surimi nuggets was more than that for fish nuggets after frozen storage. These results showed that surimi nuggets had higher quality indicators rather than fish nuggets.

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Effect of pH on the gel properties and secondary structure of fish myosin

Cited by 156 publications

References 37 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

The interaction mechanism of different ionic polysaccharides with myofibrillar protein and its contribution to the heat‐induced gels

Quality evaluation of surimi and fish nuggets from Queen fish (Scomberoides commersonnianus)

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