Differential Scanning Calorimetry of Fish Muscle: The Effect of Processing and Species Variation

Hastings, R.; Rodger, G.; Park, Robin; Matthews, Anthony D.; Anderson, Eric

doi:10.1111/j.1365-2621.1985.tb13437.x

Cited by 106 publications

(58 citation statements)

References 10 publications

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“…2 was suggested to result from thermal transition of collagen, and the shoulder labelled as no. 1 was an overlap of myosin and collagen transitions according to Hastings et al (1985). Similar values (T 0 = 34, 40.3°C and T max = 40.1, 44.4°C) have been reported for the onset and maximum transition temperatures for cod connective tissue (Poulter, Ledward, Godber, Hall, & Rowlands, 1985).…”

Section: Evaluation Of the Dsc Of The Fresh Cod Musclesupporting

confidence: 71%

“…4-8). These assumptions were based on our results from the electrophoresis and other DSC studies (Hastings et al, 1985;Samejima et al, 1983;Smyth, Smith, VegaWarner, & O'Neill, 1996;Wright & Wilding, 1984). However, Fig.…”

Section: Dsc-profiles Of Cod Muscle During Salting and Rehydrationmentioning

confidence: 95%

“…These results were in agreement with earlier findings for cod. Reported T max -values for myosin, sarcoplasmic proteins and actin are 44, 55-59 and 73-74°C, respectively (Geirsdottir, 1998;Hastings, Rodger, Park, Matthews, & Anderson, 1985;Thorarinsdottir et al, 2002).…”

Section: Evaluation Of the Dsc Of The Fresh Cod Musclementioning

confidence: 99%

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Effects of different pre-salting methods on protein aggregation during heavy salting of cod fillets

et al. 2011

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Section: Evaluation Of the Dsc Of The Fresh Cod Musclesupporting

confidence: 71%

Section: Dsc-profiles Of Cod Muscle During Salting and Rehydrationmentioning

confidence: 95%

See 1 more Smart Citation

Effects of different pre-salting methods on protein aggregation during heavy salting of cod fillets

et al. 2011

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“…This technique allows protein behavior to be studied in situ in very small amounts. DSC was widely used to analyze the proteins of muscle tissue from chicken, beef, pork and fish meat [11,12]. The DSC studies characterizing the thermal properties of muscle proteins in squid (Illex argentinus) [13] or scallop (Zygochlamys patagonica) [14] were reported.…”

Section: Introductionmentioning

confidence: 99%

DSC and electrophoretic studies on protein denaturation of Anodonta woodiana (Lea, 1834)

Konieczny

Tomaszewska-Gras

Andrzejewski

et al. 2016

J Therm Anal Calorim

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The aim of this study was to examine the thermal denaturation properties of proteins from fresh and frozen pond mussels Anodonta woodiana by differential scanning calorimetry (DSC). The A. woodiana (Lea, 1834) mussels were collected from the bottom of a lake located in West Poland. Three parts of the mussel: adductor muscle (AM), foot muscle (FO) and part of internal organs (IO), were taken for analysis. The DSC technique was used to characterize the stability of the protein system, and SDS-PAGE was applied for the separation and identification of proteins. Thermal analysis in all parts of the mussel revealed two main endothermic transitions: the first at 60-61°C and the second at 69-70°C. Denaturation transition occurred in the temperature range from 42 to 76°C. The highest enthalpy of denaturation was observed for FO and was 15.75 J g -1 (per 1 g of protein) and 14.01 J g -1 for AM. The lower-temperature peak, related to myosin and paramyosin, accounted for approximately 70-80 % of the total area of transition. Electrophoretic analysis (SDS-PAGE) confirmed that the paramyosin, with a mass of approx. 98-107 kDa, constituted the largest percentage, i.e., 24 % in AM and 17 % in IO and FO. Two other main myofibrillar proteins were also present in significant amounts: myosin with a molecular mass of 230-245 kDa (12-14 %) and actin with a mass of 47 kDa (18-20 %). In this study, the effect of freezing on protein stability was also investigated. The results of DSC analyses revealed that the process of freezing did not have a significant influence on the first and second peak temperature. Significant differences in enthalpy between fresh and frozen samples were observed only for AM, for which the total enthalpy (DH) decreased by 33 %. This study provided insight into the biochemistry of A. woodiana meat and offers an area of scientific novelty. Recognizing quality properties of meat tissue from freshwater Chinese pond mussels collected from selected water ecosystems seems to be important with respect to the potential possibility of using it for feed, pet food or even in food products.

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“…The first and second peaks were postulated to be the transitions of myosin and actin, respectively (Hastings, Rodger, Park, Matthews, & Anderson, 1985). The observed T max of myosin and actin were in the temperature range reported for various fish species.…”

Section: Thermal Transitionmentioning

confidence: 93%

Impact of zinc salts on heat-induced aggregation of natural actomyosin from yellow stripe trevally

Arfat

Benjakul

2012

Food Chemistry

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Differential Scanning Calorimetry of Fish Muscle: The Effect of Processing and Species Variation

Cited by 106 publications

References 10 publications

Effects of different pre-salting methods on protein aggregation during heavy salting of cod fillets

Effects of different pre-salting methods on protein aggregation during heavy salting of cod fillets

DSC and electrophoretic studies on protein denaturation of Anodonta woodiana (Lea, 1834)

Impact of zinc salts on heat-induced aggregation of natural actomyosin from yellow stripe trevally

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