Differential scanning calorimetry on fish meat paste.

Iso, Naomichi; Mizumo, H.; Ogawa, Hiroo; Mochizuki, Yoshinori; Masuda, Nobuhisa

doi:10.2331/suisan.57.337

Cited by 9 publications

(3 citation statements)

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“…Thermal gelation of meat paste was governed by how proteins behave or interact with each other during heating. A small quantity of heat is generally used for the easy-setting meat (Iso, Mizuno, Ogawa, Mochizuki, & Masuda, 1991). Thermal stability of fish myosin varied with species.…”

Section: Resultsmentioning

confidence: 99%

Gelling properties of white shrimp (Penaeus vannamei) meat as influenced by setting condition and microbial transglutaminase

Tammatinna

Benjakul

Visessanguan

et al. 2007

LWT - Food Science and Technology

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Section: Resultsmentioning

confidence: 99%

Gelling properties of white shrimp (Penaeus vannamei) meat as influenced by setting condition and microbial transglutaminase

Tammatinna

Benjakul

Visessanguan

et al. 2007

LWT - Food Science and Technology

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“…The amount of DSC-measured bound water of the different starch-incorporated surimi gels correlated positively with compression force (r = 0.94) and penetration force (r = 0.99), but inversely with expressible moisture (r = −0.99). In DSC measurements on various fi sh species, it was found that the easy-setting meat and the easy-disintegrating meat required a small quantity of heat to change the structure (Iso et al 1991).…”

Section: First Applications Of Dsc On Fi Sh Muscle and Other Seafoodmentioning

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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“…The proteins of shark muscle showed higher thermal stabil ity than that of teleost. ', 16,17) The higher thermal stability of muscle required more quantity of heat to change the pro tein structure . 11,18) These results suggest a relationship be tween the high thermal stability and difficult suwari and modori characteristics of spotted shark surimi.…”

Section: Effects Of Setting On the Physical Properties Of Kamabokomentioning

confidence: 99%

The Effect of Setting on the Physical Properties of Surimi and Kamaboko under Various Water Content and Chopping Methods

Chen

1997

Fisheries science

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Differential scanning calorimetry on fish meat paste.

Cited by 9 publications

References 0 publications

Gelling properties of white shrimp (Penaeus vannamei) meat as influenced by setting condition and microbial transglutaminase

Gelling properties of white shrimp (Penaeus vannamei) meat as influenced by setting condition and microbial transglutaminase

Differential Scanning Calorimetry

The Effect of Setting on the Physical Properties of Surimi and Kamaboko under Various Water Content and Chopping Methods

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