Thermal stability of fish myofibrils: a differential scanning calorimetric study

Howell, Belinda K.; Matthews, Anthony D.; Donnelly, Andrew P.

doi:10.1111/j.1365-2621.1991.tb01165.x

Cited by 50 publications

(30 citation statements)

References 14 publications

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“…Increments of pH above 7 can promote a decrease of thermal stability and denaturation of myofibrillar proteins. 32,33 In this case, pH (initial value: 6.4) increased significantly after 7 days of storage, exceeding a value of 7 at 9 days.…”

Section: Protein Extractabilitymentioning

confidence: 93%

Lipid and protein deterioration during the chilled storage of minced sea salmon (Pseudopercis semifasciata)

2007

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Sea salmon is a very appreciated seafood. The aim of this work was to analyze changes in lipid and protein fractions of minced muscle during chilled storage (1 ± 1• C). Lipid oxidation was important during the first 6 days of storage according to 2-thiobarbituric acid (TBA) values determined, decreasing mainly ω3 22:6 fatty acid content. Lipid hydrolysis was evident after 9 days of storage. Interaction compounds between oxidation products and other cellular components were analyzed by fluorescence measurements. The results obtained showed evidence of the formation of interaction products involved, mainly polar components such as proteins. Decreases in myosin and actin thermal stability and myosin denaturation were recorded by differential scanning calorimetry. Solubility of total and myofibrillar proteins decreased after 6 days of storage. The electrophoretic profile of soluble fractions showed an increase in the intensity of bands corresponding to low-molecular-weight polypeptides and a decrease in high-molecular-weight species. Available lysine content did not change during chilled storage.

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Section: Protein Extractabilitymentioning

confidence: 93%

Lipid and protein deterioration during the chilled storage of minced sea salmon (Pseudopercis semifasciata)

2007

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“…The order of the denaturation temperature generally found during the investigation, namely 'rabbit, carp and scallop' appeared to refl ect the habitat temperature of these animals. The variation in myofi brillar protein thermal stability was compared by using DSC for various fi sh species (Howell et al 1991). Tropical freshwater and marine fi sh were compared with fi sh inhabiting cold waters.…”

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

confidence: 99%

“…As pH (6.0-8.0) and ionic strength (0.05-1.0) were increased, thermal denaturation temperatures of myosins from tropical, but not coldwater, species decreased. Enthalpies of myofi brillar denaturation decreased for all species with increasing pH and ionic strength (Howell 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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“…DSC has been reported to be a very use fuI technique for monitoring changes in fish muscle proteins during frozen storage (Herrera et al, 200 1;Howell et al, 1991;Poulter et al, 1985). DSC enables fish muscle proteins to be studied in situ.…”

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confidence: 99%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

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: The changes in protein structure associated with the preparation and frozen storage of surimi were investigated. Raw surimi was prepared by repeatedly washing Alaska pollock flesh with chilled water. The product was either slowly frozen or underwent rapid freezing using liquid air; in either case it was then subjected to frozen storage at ‐20 °C for 24 mo. Fourier transform infrared/attenuated total reflectance (FTIR/ATR) spectroscopy showed that during preparation of surimi, the a‐helix content increased with increased number of washing cycles. Differential scanning calorimetry (DSC) revealed a shift in the thermal transition of actin to a higher temperature during surimi preparation. Electrophoresis, FTIR/ATR spectroscopy, and DSC results revealed a loss of myofibrillar proteins from surimi after 3 washing cycles, suggesting that 3 washing cycles were adequate to prepare surimi. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) showed relatively minor changes in protein subunit structure with some loss of the myosin light chains (MLC); myosin heavy chain (MHC), actin, and tropomyosin were found to be relatively stable. Native‐PAGE showed no major changes in surimi after 24 mo storage at ‐20 °C. FTIR/ ATR spectroscopy indicated a significant decrease in a‐helix relative to p‐sheet structure in surimi after 2 y of storage at ‐20 °C. The loss of α‐helical content was more significant in slowly frozen surimi compared with rapid‐frozen surimi samples. DSC results revealed a shift in the thermal transition of actin to lower temperatures during frozen storage of surimi.

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Thermal stability of fish myofibrils: a differential scanning calorimetric study

Cited by 50 publications

References 14 publications

Lipid and protein deterioration during the chilled storage of minced sea salmon (Pseudopercis semifasciata)

Lipid and protein deterioration during the chilled storage of minced sea salmon (Pseudopercis semifasciata)

Differential Scanning Calorimetry

Protein Structural Changes During Preparation and Storage of Surimi

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