Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting

Hwang, Jyh-Sheng; Lai, Kung‐Ming; Hsu, Kuo‐Chiang

doi:10.1016/j.foodchem.2006.11.075

Cited by 98 publications

(64 citation statements)

References 33 publications

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“…For the latter situation, the strong effect of EDC outweighs the electrostatic phenomena. Indeed, the impact of EDC on WHC seemed to differ from the effect of MTGase, which did not alter water-binding properties in gels from sea bass [22,32] and pork muscle [33]. However, other studies have found a positive action of MTGase upon WHC or upon extracted water [2,34].…”

Section: Water Holding Capacity (Whc)mentioning

confidence: 86%

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Improvement of the gelling ability in restructured fish products: effect of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide level and pH

Cardoso

Ribeiro

Mendes

2012

Eur Food Res Technol

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The production of heat-induced gels from raw materials with poor gelling ability remains a technical challenge, for which new solutions have been proposed. The addition to the gel batters of a cross-linking chemical agent, such as 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC), may present a valuable tool for the improvement of gelling. Accordingly, a response surface methodology was used to optimize the conditions of EDC application, the EDC concentration (0.0-0.5 %, w/w) and the batters' pH (4.5-7.5). Results showed that textural, colour, and water-binding properties of heat-induced hake gels were extremely sensitive to EDC content and pH. It was possible to find an optimal EDC level-pH binary common to the various studied parameters, a pH between 4.0 and 5.0 and an EDC concentration of 0.5 %, w/w. Moreover, this experimental work proved to be feasible the achievement of gel products of acceptable textural quality from frozen hake through EDC incorporation in optimal conditions.

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Section: Water Holding Capacity (Whc)mentioning

confidence: 86%

“…This darkening effect can be interpreted as an indication of a lower denaturation of those gels containing MTGase. In fact, increased whiteness can be related to the degree of protein degradation, for instance, as it happens with cooking [22]. The cross-links catalyzed by MTGase during setting seem to avoid degradation during cooking.…”

Section: Colour Parametersmentioning

confidence: 99%

Improvement of the gelling ability in restructured fish products: effect of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide level and pH

Cardoso

Ribeiro

Mendes

2012

Eur Food Res Technol

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“…The latter is the most common approach (Hwang et al, 2007;Martínez et al, 2014;Totosaus, Montejano, Salazar, & GuerreroLegarreta, 2002). Therefore, the present review addresses the heat treatment gelling process.…”

Section: Protein Gelationmentioning

confidence: 99%

“…Denaturation can be caused using chemical (such as salts) and physical (such as heat and pressure) agents. Heat treatment is the most common method used to make such products (Hwang, Lai, & Hsu, 2007;Martínez et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Thermal gelation of myofibrillar proteins from aquatic organisms

Tolano-Villaverde

Torres‐Arreola

Ocaño‐Higuera

et al. 2015

CyTA - Journal of Food

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Gelling ability is attributed to myosin, which is the main myofibrillar protein. Therefore, its integrity is very important. However, a gel with good textural characteristics and stability depends on the inherent characteristics of its proteins, as well as on external factors (primarily temperature, pH, protein concentration and added salt). The best gels from aquatic organism proteins are obtained at a pH value of approximately 7.0. However, the concentration of salt is often variable. In contrast, when proteins are recovered using acid/alkaline dissolution, gels with good textural characteristics are obtained without salt. Hydrophobic interactions, disulfide bonds, hydrogen bonds, and electrostatic interactions are the main interactions that stabilize the protein gel. Thus, this review focuses on the study of the main factors involved in protein gelation, as well as on the extraction method effect on the gelling capacity of proteins from aquatic organisms. Gelificación térmica de proteínas miofibrilares de organismos acuáticos RÉSUMÉMiosina es la principal proteína miofibrilar a la cual se le atribuye la habilidad gelificante, por lo tanto su integridad es muy importante. Sin embargo, las propiedades texturales y estabilidad de los geles depende de las características inherentes de sus proteínas, así como de factores externos (principalmente temperatura, pH, concentración de proteína y sal añadida). En general, los mejores geles proteicos obtenidos de organismos acuáticos se obtienen a pH cercano a 7.0, mientras que la concentración de sal suele ser variable; sin embargo, cuando la recuperación de proteínas se realiza a través de disoluciones ácidas/alcalinas, es posible obtenerse geles con buenas características texturales en ausencia de sal. Las principales interacciones involucradas en la estabilización de geles proteicos son: interacciones hidrofóbicas, puentes disulfuro, puentes de indrógeno e interacciones electrostáticas. Por esta razón, la presente revisión estudia los principales factores involucrados en la gelificación proteica, así como el efecto del método de extracción, sobre la capacidad gelificante de proteínas de organismos acuáticos. ARTICLE HISTORY

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“…Certain information was published earlier by Hwang et al (2007) but their data referred to the rheological characteristics of fish surimi subjected to the action of increased pressure.…”

Section: Rheological Propertiesmentioning

confidence: 99%

Effect of enzymatic modification on chicken surimi

Stangierski¹,

Rezler²,

Baranowska³

et al. 2012

Czech J. Food Sci.

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Stangierski J., Rezler R., Baranowska H.M., Poliszko S. (2012): Effect of enzymatic modification on chicken surimi. Czech J. Food Sci., 30: 404-411.The impact of the addition and duration of protein modification with transglutaminase preparation of microbial origin (MTG) of a chicken surimi on its texture, rheological characteristics, water molecular dynamics, and water activity were assessed. Surimi samples were supplemented with 0.3 g/100 g MTG and incubated maximally for about 7 h at the temperature of 15°C. The greatest changes of the chicken surimi properties were observed during the initial period, i.e. during 3 h of proteins incubation with MTG. Surimi modification with transglutaminase increased the equilibrium water activity in comparison with the value obtained for the control sample. At the same time, the mean diffusion coefficient in the enzymatically modified poultry surimi sample reached the value nearly twice higher than in the control sample.

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Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting

Cited by 98 publications

References 33 publications

Improvement of the gelling ability in restructured fish products: effect of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide level and pH

Improvement of the gelling ability in restructured fish products: effect of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide level and pH

Thermal gelation of myofibrillar proteins from aquatic organisms

Effect of enzymatic modification on chicken surimi

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