Heat-induced Gelation of Myosin Filaments at a Low Salt Concentration

Ishioroshi, Makoto; Samejima, Kunihiko; Yasui, Tsutomu

doi:10.1080/00021369.1983.10866029

Cited by 19 publications

(21 citation statements)

References 12 publications

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“…As the pH increased, the gel strength and gelation rate decreased (Liu et al, 2010). Ishioroshi et al (1983) found that the rigidity of the myosin gel in 0.2 mol/L KCl at pH 6.0 was greater than that in 0.6 mol/L KCl at pH 6.5 after incubation for 20 min at 65°C, which is somewhat contrary to our research, and that could be the result of the interaction between myosin molecules and other myofibrillar proteins (Lefevre et al, 2002).…”

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

confidence: 56%

“…The myofibril solubility increased with pH because proteins were highly charged and protein-water interaction increased at pH far away from the pI (Lefevre et al, 2002). A drastic decrease in rigidity was caused by the addition of ATP (Ishioroshi et al, 1983). Liu and Xiong (1997) proved that the gel strength of chicken myofibrillar proteins increased with increased salt concentration via the redistribution of charges on the surfaces of proteins, which affected the protein-protein electrostatic interactions and the protein stabilities, thus promoting the unfolding of the proteins to form gels.…”

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

confidence: 96%

“…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). As pH was raised, gel strength gradually increased until reaching a maximum.…”

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%

“…The water holding and binding capacities of processed meat are based on the capability of myosin to form wellstructured thermal gels that can effectively bound and immobilize water through capillary forces (Ishioroshi, Samejima, & Yasui, 1983;Wu et al, 2009). 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).…”

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

confidence: 56%