Rheological properties of fish actomyosin and pork actomyosin solutions

Liu, Ru; Zhao, Siming; Xiong, Shanbai; Qiu, Cheng-guang; Xie, Bijun

doi:10.1016/j.jfoodeng.2007.06.031

Cited by 43 publications

(16 citation statements)

References 23 publications

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“…The physicochemical properties of salt-soluble proteins have been found to be strongly pH-and temperature-dependent [8][9][10]. It has also been reported [11] that the ideal gelling properties of a protein at a given temperature can be achieved by varying the pH.…”

Section: Introductionmentioning

confidence: 97%

Effect of pH on the physicochemical and heat-induced gel properties of scallop Patinopecten yessoensis actomyosin

Dong

Zheng

et al. 2014

Fish Sci

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Gelation is an important functional property of protein in meats. In this study, we prepared actomyosin from scallop Patinopecten yessoensis adductor muscles and studied the effects of pH on the physicochemical properties of the actomyosin preparation and on its heat-induced gelforming properties. The results showed that the turbidity and surface hydrophobicity of scallop actomyosin increased with increases in the heating temperature, while the a-helical content concomitantly decreased. Higher turbidity and surface hydrophobicity and lower a-helical content were found to be easily obtained at lower pH values. A high water-holding capacity, strong gel strength, fine gel network and uniform ice crystals were all clearly observed at pH 7.0, indicating that a neutral pH was most beneficial for formation of the heat-induced scallop actomyosin gel. We therefore conclude that both the physicochemical properties of scallop actomyosin and its gelforming ability during the heating process are pH dependent.

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Section: Introductionmentioning

confidence: 97%

Effect of pH on the physicochemical and heat-induced gel properties of scallop Patinopecten yessoensis actomyosin

Dong

Zheng

et al. 2014

Fish Sci

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“…In our previous study, gelling of porcine myosin involved a change in myosin conformation with protein-protein and protein-water interactions. The rheological properties of salt soluble proteins were strongly pH and temperature dependent (Liu, Zhao, Xiong, Qiu, & Xie, 2008a;Liu, Zhao, Xiong, Xie, & Qin, 2008b;Raghavan & Kristinsson, 2008). It has been suggested that altering the pH of meat products could result in the attainment of the desired gel strength at a given temperature (Westphalen, Briggs, & Lonergan, 2005).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2010

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“…Heating decreases the viscosity due to an increase in the kinetic energy, and thus thermal denaturation contributes to the rheology of the protein system [4]. The pH and ionic strength of macromolecular systems affect its rheological properties by altering the electrostatic charge [5]. Differences in the functional properties of different gels may also derive from inherent factors (protein structure, molecular mass, and amino acid composition) [6,7].…”

Section: Introductionmentioning

confidence: 99%

Relationship between the water molecules in fish-meat gel and the gel structure

2012

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To elucidate the structure of the network of the water retention mechanism of fish-meat gel, the microscopic relationship between the water content and viscoelasticity was investigated, and the specific surface area (S) where the water molecules are adsorbed was also measured. The gel structures of fish-meat, actomyosin (AM), and myosin (M) were investigated. In the fish-meat gel, as the water content increased, the number of network chains (m) decreased and the molecular weight between the cross-linking points (M e ) increased. At 10 % salinity and approximately 79 % moisture, m decreased to a minimum and M e began to increase remarkably. In addition, when the moisture increased to 78 %, S increased about 1.5 times and the elasticity decreased significantly, indicating that this level of water content is the limit for sufficiently forming a gel structure in fish-meat gel. In the AM and M gels, M e and S were similar to those observed in the fishmeat gels. When the moisture content increased, they also increased, regardless of the salt concentration. This result suggests that the size of the network was enlarged or that the network chains were cleaved.

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Rheological properties of fish actomyosin and pork actomyosin solutions

Cited by 43 publications

References 23 publications

Effect of pH on the physicochemical and heat-induced gel properties of scallop Patinopecten yessoensis actomyosin

Effect of pH on the physicochemical and heat-induced gel properties of scallop Patinopecten yessoensis actomyosin

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

Relationship between the water molecules in fish-meat gel and the gel structure

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