Thermal Gelation of Brown Trout Myofibrils: Effect of Muscle Type, Heating Rate and Protein Concentration

Lefèvre, Florence; Fauconneau, Benoı̂t; Ouali, Ahmed; Culioli, Joseph

doi:10.1111/j.1365-2621.1998.tb15730.x

Cited by 41 publications

(23 citation statements)

References 57 publications

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“…It has been demonstrated in previous study that as the temperature decreased, the hydrogen bonds became stronger (Foegeding, Gonzalez, Hamann, & Case, ). Increase in gel rigidity with increase in protein concentration regardless of protein type has been reported by previous studies (Lefevre, Fauconneau, Ouali, & Culioli, ; Youssef & Barbut, ). The increased exposure of hydrophobic residues at 40°C temperature provides more pitches for protein interaction, which results in formation of connected gel network (Abdollahi, Rezaei, Jafarpour, & Undeland, ; Ingadottir & Kristinsson, ; Zhao et al, ).…”

Section: Resultssupporting

confidence: 80%

Functional properties and dynamic rheology of protein isolates extracted from male and female common carp (Cyprinus carpio) muscle subjected to pH‐shifting method

Singh

Kaur

et al. 2019

J Food Process Preserv

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The present study showed the physicochemical and functional properties of protein isolates prepared from male and female common carp (Cyprinus carpio) muscle using pH‐shift method. The alkali (BPIs) and acid (APIs) protein isolates showed higher protein content than raw muscle. The decline in fat and ash content due to the removal of connective tissue during separation process was observed. The color properties of isolates varied significantly between gender as well as processing methods which could be related to total pigment content. The processing methods and gender differences resulted a significant variation in water absorption capacity, emulsifying activity index, emulsifying stability index, foaming stability, storage modulus, loss modulus, and Greinforcement. The SDS‐PAGE analysis showed the presence of different molecular weight polypeptides influencing functional and rheological properties of protein isolates from both genders. The present study overall depicted rheological and functional properties of BPIs and APIs from male were better than that of female. Practical applications Common carp being an exotic fish is cultured throughout India, especially in northern region. The present study entails comparative analysis of physicochemical, functional, and rheological properties of FPIs (BPIs and APIs) by pH‐shift method from both genders. The results from present study suggested that understanding the functionality of protein isolates prepared from different genders and processing methods can enhance their application as ingredients in food industry to make them more suitable for human consumption.

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Section: Resultssupporting

confidence: 80%

Functional properties and dynamic rheology of protein isolates extracted from male and female common carp (Cyprinus carpio) muscle subjected to pH‐shifting method

Singh

Kaur

et al. 2019

J Food Process Preserv

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“…During study of the gelation properties of chicken and turkey white and red muscle myofibrils, Lesiów and Xiong (2001a) concluded that red muscle formed weaker gel than white one. Similar differences were seen in the study of Lefévre and others (1998) on reared brown trout, where, at a heating rate of 1 °C/min, the thermal gelation properties of red muscle myofibrils exhibited a lower gelation capacity than white muscle myofibrils. No differences were observed above 60 °C where solid gels were formed from both myofibril types.…”

Section: Type and Source Of Musclesupporting

confidence: 83%

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Sun

Holley

2010

Comp Rev Food Sci Food Safe

405

244

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Considerable research has been done to better understand the basis for gel formation by myofibrillar proteins (MPs) in effort to manufacture acceptable processed meats with lower cost and more desirable nutritional characteristics. Results from research available indicate that there is no substitute for the myofibrillar protein myosin in gel formation by proteins from a wide variety of animal and fish species. This report consolidates information on determinants of protein gel formation, examining types of muscles and fibers, the species influence, and interactions of the MPs actin and myosin with each other and with fat, gelatin, starch, hydrocolloids, some protein soy, whey, and nonprotein additives such as phosphates and acidifiers, and the influences of pH, ionic strength, rates of heating, and its absence, protein oxidation, as well as the use of transglutaminase and high hydrostatic pressure. It is of interest that myosin alone will form acceptable gels. Gel formation by MPs is optimized at pH 6, an ionic strength of 0.6 M, and at 60 to 70 °C. The observations that collagen‐derived gelatin can reduce the rubbery texture of low‐fat products and that solubilization of MPs is not always essential for gel formation, and the observation that good gels can be formed in the absence of salt, are exciting developments that should be considered as pressure mounts to continue to reduce fat and salt in the diet.

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“…In the case of fish paste, G ′ started to increase from 5 °C, reaching the 1st peak at 35 °C, indicating the transformation from a viscous sol to an elastic network (Egelandsdal and others 1986). The initial increase of G ′ to 35 °C could be related to interactions that occur at low temperatures between protein molecules (Lefèvre and others 1998; Lanier and others 2004). Subsequently, G ′ dropped abruptly, reaching a minimum at 51 °C.…”

Section: Resultsmentioning

confidence: 99%

Studies on Fish and Pork Paste Gelation by Dynamic Rheology and Circular Dichroism

Liu¹,

Zhao²,

Xiong³

et al. 2007

Journal of Food Science

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The muscle paste of fish, pork, and their mixtures were prepared to study the gelling characteristics by dynamic rheological measurement. The gelation mechanisms of muscle paste were also investigated by circular dichroism. Gel formation of fish paste occurred in 2 steps of 5 to 35 and 51 to 90 degrees C respectively, while pork paste mainly in 1 step of 49 to 72 degrees C. Gel formation was relative to the alpha-helix unfolding of myosin, which responded the melting temperatures of 40 and 50 degrees C for fish myosin and 50 and 60 degrees C for pork myosin, respectively. Alpha-helix unfolding of myosin was beneficial for gel formation. During gel formation, G' of muscle paste was linearly related to alpha-helical content of myosin. The interactions of fish and pork proteins at high temperature (>35 degrees C) could change the gel forming characteristics of muscle paste. Mixed paste exhibited a similar gelation pattern to individual fish paste with 2 visible increases in G'. Addition of pork could suppress the breakdown of fish gel structure at approximately 50 degrees C. Mixing pork and silver carp in a certain ratio could improve the gel properties of silver carp products.

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Thermal Gelation of Brown Trout Myofibrils: Effect of Muscle Type, Heating Rate and Protein Concentration

Cited by 41 publications

References 57 publications

Functional properties and dynamic rheology of protein isolates extracted from male and female common carp (Cyprinus carpio) muscle subjected to pH‐shifting method

Functional properties and dynamic rheology of protein isolates extracted from male and female common carp (Cyprinus carpio) muscle subjected to pH‐shifting method

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Studies on Fish and Pork Paste Gelation by Dynamic Rheology and Circular Dichroism

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