Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (<i>Zygochlamys</i><i>patagonica</i>). A Differential Scanning Calorimetric Study

Paredi, María E.; Tomás, Mabel Cristina; Crupkin, Marcos

doi:10.1021/jf010767q

Cited by 22 publications

(11 citation statements)

References 28 publications

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“…ΔH signifi cantly decreased when ionic strength increased from 0.05 to 0.5 in both types of muscle. Striated muscles were affected more than smooth muscles by changes in the chemical environment (Paredi et al 2002). Three major endothermic peaks at 50, 57 and 74 °C were found in the DSC curve of the mantle of cuttlefi sh (Sepia esculenta).…”

Section: Dsc Measurements Taken On Invertebratesmentioning

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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Section: Dsc Measurements Taken On Invertebratesmentioning

confidence: 99%

Differential Scanning Calorimetry

Schubring

2009

Fishery Products

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“…In this way, the lower superficial hydrophobicity of Aulacomya actomyosin could be due to a greater stability of this protein before the chemical environment. Differential scanning calorimetric (DSC) studies demonstrated that the myosin-paramyosin zone of the thermogram for Aulacomya has great thermal stability than those obtained in DSC thermograms of squid and scallop muscles (Paredi, Tomas, Crupkin, & An˜on, 1998b;Paredi, Tomas, & Crupkin, 2002). In addition, a great sensitivity of Patagonian scallop myofibrillar proteins to changes in the chemical environment was reported Paredi, Tomas, & Crupkin, 2003).…”

Section: Enzymatic Activity and Protein Surface Hydrophobicitymentioning

confidence: 99%

Physico-chemical and functional properties of myofibrillar proteins from different species of molluscs

Mignino¹,

Paredi²

2006

LWT - Food Science and Technology

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“…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. However, little DSC research has been done on muscle proteins from other marine or freshwater sources.…”

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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Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamyspatagonica). A Differential Scanning Calorimetric Study

Cited by 22 publications

References 28 publications

Differential Scanning Calorimetry

Differential Scanning Calorimetry

Physico-chemical and functional properties of myofibrillar proteins from different species of molluscs

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

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