Conformational changes and dynamic rheological properties of fish sarcoplasmic proteins treated at various pHs

Tadpitchayangkoon, Panchaporn; Park, Jae W.; Yongsawatdigul, Jirawat

doi:10.1016/j.foodchem.2010.01.046

Cited by 64 publications

(48 citation statements)

References 32 publications

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“…When pH was increased to 4.5 and above, it was found that only sarcoplasmic proteins were soluble in water, especially just below 60 kDa proteins at pH 5.0 and 5.5. This phenomenon was quite similar to the sarcoplasmic proteins of striped catfish (26). However, in the case of NaCl addition, MHC and actin were well dissolved at pH 5.5-7.0, but they were not solubilized at pH 3.0-5.0.…”

Section: Surimi Protein Solubilitysupporting

confidence: 63%

Silver Carp (Hypophthalmichthys molitrix) Surimi Acid-Induced Gel Extract Characteristics: A Comparison with Heat-Induced Gel

Weng

Zheng

2015

International Journal of Food Properties

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Traditional surimi-based products are usually prepared through a heating process, which often causes high energy consumption and increased production cost. Acid-induced surimi gel as a new preparation technique were prepared from silver carp surimi by soaking in acetic acid in this study, and their properties and formation mechanism were investigated and compared to heat-induced gel. The moisture content, breaking force, deformation and whiteness of acid-induced surimi gel were all higher than those of heat-induced gel, irrespective of acid ACCEPTED MANUSCRIPT ACCEPTED MANUSCRIPT 2 concentration. The textural properties, color values and water holding capacity of acid-induced gel were increased with acetic acid concentration increase from 1 to 3%. On the other hand, the high molecular weight fractions were also formed with myosin heavy chain based on electrophoresis analysis. The data of protein subunits solubilized in various solvents revealed that the most important associative force in acid-induce gel was hydrophobic interactions.Furthermore, the compact and fine fiber microstructure in acid-induced surimi gel was observed by scanning electron microscopy. It is concluded that a tri-dimensional network was formed within the acid induced surimi gel through hydrophobic interactions and disulfide bonds with the presence of MHC and actin, resulting in formation of compact fine fiber microstructures.

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Section: Surimi Protein Solubilitysupporting

confidence: 63%

Silver Carp (Hypophthalmichthys molitrix) Surimi Acid-Induced Gel Extract Characteristics: A Comparison with Heat-Induced Gel

Weng

Zheng

2015

International Journal of Food Properties

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“…It may be hypothesized that blending PS‐CF was more sensitive to heat than blending CS‐CF, and led to a higher degree of unfolding and conformational changes. Comparable results were presented by Fukushiima, Okazaki, Fukuda, and Watabe () and Tadpitchayangkoon, Park, and Yongsawatdigul, (), which demonstrated the thermal stability of samples affected denaturation and aggregation temperatures.…”

Section: Resultsmentioning

confidence: 66%

Optimal blending of differently refined fish proteins based on their functional properties

Kobayashi

Park

2017

J Food Process Preserv

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Two different mixtures (Alaska pollock surimi with grass carp fish protein isolate (FPI) and grass carp surimi with grass carp FPI) were investigated for their compatibility and functionalities. As the proportion of FPI increased, it was observed surface hydrophobicity and surface reactive sulfhydryl (SRSH) content increased significantly, indicating the degree of fish protein unfolding prior to gelation was much higher than surimi alone. Comparable results were shown as measured by storage modulus (G 0 ) in oscillatory dynamic rheology, demonstrating the gelling temperature was reduced when the proportion of FPI increased. Effects of mixing surimi and FPI on gel functionality (hardness, cohesiveness, and whiteness) exhibited a linear pattern when the proportion of surimi was larger than or equal to that of FPI. However, there were no linear relationships when the proportion of FPI exceeded that of surimi. Practical applicationsCommercial surimi has been successfully used in the Western world over 30 years. Unlike surimi which is a refined fish myofibrillar protein composite, fish protein isolate (FPI) is a refined composite of myofibrillar protein and sarcoplasmic protein. The former is made by avoiding any chemical/ physical denaturation, while the latter can be made by inducing chemical denaturation and renaturation with pH shift. Even though FPI is not currently available in a commercial scale, it has a great potential to replace all or a part of surimi for the manufacture of fish protein gel products. This study reveals how to optimally mixed these two differently refined fish proteins based on their functional properties. The results suggested that blending surimi and FPI may be feasible only when the proportion of FPI does not exceed 50%.

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“…The G', G″ and tan δ values for hydrogels were also dependent on pH ( Figure 5). And there have been some reports on the viscoelastic properties of protein- polysaccharide systems (Miquelim et al, 2010;Tadpitchayangkoon et al, 2010;Romero et al, 2009;Ribotta et al, 2007;Bazinet et al, 2004;Mohamed and Xu, 2003;Gaaloul et al, 2009). From Figure 5, it can be seen that G' and G″ display the similar changing tendency as with pH change.…”

Section: Influence Of Ph On the Rheological Propertiesmentioning

confidence: 99%

Influence of temperature, pH, and ionic strength on the rheological properties of oviductus ranae hydrogels

Liang¹,

Zhang²,

Xu³

et al. 2014

Afr. J. Biotechnol.

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The main rheological features of oviductus ranae (OR) hydrogels were investigated as a function of temperature, pH and ionic strength. With respect to the steady shear measurements, a reduction in viscosity was observed as the temperature increased. The flow behavior can be well described by the Herschel-Bulkley model in the down curve at a shear rate of 300 to 0 s, where standard error is lower than 20, and it behaved like a viscoplastic fluid. OR gels showed greater extent of thixotropy with the increase of temperature. Temperature dependence on apparent viscosity at a specified shear rate can be described by the Arrhenius model with high R 2 values. The thermostability of OR hydrogels were verified by temperature sweep test, which showed that there was no phase transition observed in the temperature range of 10 to 90°C. It was found that at pH 5 to 10 and the salt concentration of 0 to 10 g/L, the OR hydrogels showed very weakly pH-dependent and salt-dependent rheological properties and dominant elastic behavior. All data indicated that OR has great potential for application as gelling and thickening agent with multiple healthy functions.

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Conformational changes and dynamic rheological properties of fish sarcoplasmic proteins treated at various pHs

Cited by 64 publications

References 32 publications

Silver Carp (Hypophthalmichthys molitrix) Surimi Acid-Induced Gel Extract Characteristics: A Comparison with Heat-Induced Gel

Silver Carp (Hypophthalmichthys molitrix) Surimi Acid-Induced Gel Extract Characteristics: A Comparison with Heat-Induced Gel

Optimal blending of differently refined fish proteins based on their functional properties

Influence of temperature, pH, and ionic strength on the rheological properties of oviductus ranae hydrogels

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