Effect of Ice Storage on the Physicochemical and Dynamic Viscoelastic Properties of Ribbonfish (Trichiurus spp) Meat

Dileep, A.O.; Shamasundar, B.A.; Binsi, P.K.; Badii, Farah; Howell, Nazlin K.

doi:10.1111/j.1365-2621.2005.tb08316.x

Cited by 51 publications

(41 citation statements)

References 39 publications

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“…In the present study the TVBN values were less than 40 mg N/100 g of meat at the end of 17 days of ice storage. If one compares the TVBN production of fresh water fish and marine water fish, the increase in marine fish is higher than fresh water fish (Dileep et al 2005;Binsi et al 2007). This is possibly due to higher non protein nitrogen content in marine fishes.…”

Section: Resultsmentioning

confidence: 99%

Effect of ice storage on the functional properties of proteins from a few species of fresh water fish (Indian major carps) with special emphasis on gel forming ability

et al. 2011

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In the present study the effect of ice storage on physico-chemical and functional properties of proteins from Indian major carps with special emphasis on gel forming ability have been assessed for a period of 22 days. The solubility profile of proteins in high ionic strength buffer and calcium adenosine triphosphatase (ATPase) enzyme activity reduced significantly (p<0.05), while that of total volatile base nitrogen (TVB-N) increased significantly (p< 0.05) at the end of 22 days of ice storage. The major protein fraction showed association-dissociation-denaturation phenomenon during ice storage as revealed by gel filtration profile and viscosity measurements. The gel forming ability of three fish species both in fresh and during different periods of ice storage was assessed by measuring the gel strength of heat induced gel. Among the three species the gel strength of the gel obtained from Catla catla and Cirrhinus mrigala was higher (586 and 561 g.cm) than the gel obtained from Labeo rohita (395 g.cm) in fresh condition. The gel forming ability of three species was significantly affected (p<0.05) during ice storage. The TVB-N values of fish meat as a function of ice storage was within the prescribed limit up to 17 days of the ice storage.

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Section: Resultsmentioning

confidence: 99%

Effect of ice storage on the functional properties of proteins from a few species of fresh water fish (Indian major carps) with special emphasis on gel forming ability

et al. 2011

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“…Changes in thermal properties of ribbonfi sh (Trichiurus spp.) meat during different periods of ice storage were investigated (Dileep et al 2005). The DSC profi le of fresh ribbonfi sh meat revealed transitions at 33.2 °C, 48.9 °C and 61.0 °C, indicating the denaturation temperature of different protein fractions.…”

Section: Heat-induced Gelation Processmentioning

confidence: 99%

“…The gelatinisation temperature of tapioca starch solution was found to be in the range 60-65 °C, and for cornstarch 67-70 °C. The viscoelastic properties of ribbonfi sh meat were altered signifi cantly, both due to the addition of starch and ice-storage period (Dileep et al 2005). DSC was used to study the effect of fi sh protein, salt, sugar and monosodium glutamate (MSG) on gelatinisation of tapioca and sage starches in fi sh cracker mixtures.…”

Section: Heat-induced Gelation Processmentioning

confidence: 99%

Differential Scanning Calorimetry

Schubring

2009

Fishery Products

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Differential scanning calorimetry (DSC) is a well-established measuring method that is used on a large scale in different areas of research, development, and quality inspection and testing. Thermal effects can be quickly identifi ed and the relevant temperature and the characteristic caloric values determined using substance quantities in the mgmilligram range. Measurement values obtained by DSC allow heat capacity, heat of transition kinetic data, purity and glass transition to be determined. DSC curves serve to identify substances (Höhne et al. 1996). When a material undergoes a change in physical state such as melting or transition from one crystalline form to another, or when a material reacts chemically, heat is either absorbed or liberated. According to Lund (1983), DSC offers a tremendous potential for studying physicochemical changes that occur in foods. During the 1980s, its use in food research became apparent.DSC is characterised by its usefulness for analysing phase changes. Reactions that can lead to such phase changes are crystallisation of water (melting and freezing), evaporation of water and certain chemical reactions, for example protein denaturation. In DSC the temperature of the sample and reference are maintained the same and amount of heat required to achieve this is recorded. The DSC curve is a plot of heat fl ow against temperature. Consequently, the enthalpy change involved in the reaction can be determined from the area under the curve of heat-fl ow versus time. Material of known enthalpy can be used to calibrate the equipment. For samples containing water, evaporation is prevented using sealed containers. For examining frozen water in foods, results that are more reproducible are obtained while thawing frozen products than during cooling and freezing of products, because the variable phenomenon of super-cooling occurs during freezing. For proteins, the temperature corresponding to the maximum peak height is often used as an indication of the denaturation temperature, and the width of the peak as a measure of the complexity of the denaturation reaction. Using these assumptions, it is possible to observe how the denaturation temperature is affected by the changes in pH or the presence of other components, and the variation in enthalpy with denaturation temperature. As a protein becomes more denatured, the size of the peak should decrease. Phase changes in these both main components of the fi sh fl esh (water and protein) are subject of DSC investigation in this special fi eld. DSC has emerged 173 Fishery Products: Quality, safety and authenticity Edited by Hartmut Rehbein and Jörg Oehlenschläger

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“…G 0 ' is the energy stored and recovered per cycle of sinusoidal shear deformation. Its increase indicates rigidity of the sample associated with the formation of an elastic gel structure (Dileep et al, 2005). G 0 " is the energy dissipated or lost as heat per cycle of sinusoidal strain at angular frequency of 1 Hz, (Ferry, 1980).…”

Section: Calculation Of Power Law Parametersmentioning

confidence: 99%

Effects of alginate gel on rheological properties of hair-tail (Trichiurus lepturus) surimi

Xue

Liu

Zhang

et al. 2011

J. Ocean Univ. China

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Effects of alginate gel at different concentrations on rheological properties of hair-tail (Trichiurus lepturus) surimi were investigated. Alginate gel (1% -3%) exhibited enhanced effects, especially when alginate gel concentration increased. The rheological properties of mixture samples were studied by the time sweep, frequency sweep and temperature sweep. The critical strain values of the mixture samples for the onset of non-linear viscoelasticity were about 5%. The storage modulus G' of the mixture samples increased with time for 4 h. The frequency sweep showed that G' was greater than G" for all the mixture gels with different alginate gel concentrations, and values of both n' and n" for all samples were low (<0.2), these constants corresponding to G' and G", and indicating the elasticity of mixture gels. The values of storage modulus G' decreased during heating process and increased with decreasing temperature.

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Effect of Ice Storage on the Physicochemical and Dynamic Viscoelastic Properties of Ribbonfish (Trichiurus spp) Meat

Cited by 51 publications

References 39 publications

Effect of ice storage on the functional properties of proteins from a few species of fresh water fish (Indian major carps) with special emphasis on gel forming ability

Effect of ice storage on the functional properties of proteins from a few species of fresh water fish (Indian major carps) with special emphasis on gel forming ability

Differential Scanning Calorimetry

Effects of alginate gel on rheological properties of hair-tail (Trichiurus lepturus) surimi

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