Thermal Denaturation of Aulacomya ater ater (Molina) Myofibrillar Proteins: A Differential Scanning Calorimetric Study

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

doi:10.1021/jf00040a006

Cited by 23 publications

(38 citation statements)

References 20 publications

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“…5b, c. The last peak No. 6 with an area of 17.73 % for AM, 13.75 % for IO and 22.96 % for FO corresponds to actin, according to Paredi et al [16]. In turn, the peak No.…”

Section: Resultsmentioning

confidence: 84%

“…The differences observed in DSC traces between chicken breast muscle and the A. woodiana mussel arise from the fact that this mussel is an invertebrate; thus, we may expect that its protein structure will be different. According to Paredi et al [16], peak with a maximum at around 60-61°C corresponds to myosin and paramyosin, and the second peak is related to the next myofibrillar protein, actin. Kantha et al [17] similarly stated that except for myosin and actin, muscles of marine invertebrates contain one more characteristic protein, namely paramyosin.…”

Section: Resultsmentioning

confidence: 99%

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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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“…5b, c. The last peak No. 6 with an area of 17.73 % for AM, 13.75 % for IO and 22.96 % for FO corresponds to actin, according to Paredi et al [16]. In turn, the peak No.…”

Section: Resultsmentioning

confidence: 84%

Section: Resultsmentioning

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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“…Particularmente, as características funcionais e texturais da carne cozida dependem do comportamento tér-mico das proteínas miofibrilares [14].…”

Section: -Introduçãounclassified

“…Alguns trabalhos foram realizados com músculos de peixes apenas lavados [16] e com proteínas miofibrilares extraídas de músculos de pescados, verificando-se o efeito do processamento, do pH e da adição de sal e sacarose sobre a desnaturação protéica [14,15]. KIJOWSKI & MAST [10] determinaram a temperatura e a entalpia de desnaturação de proteínas de diversas partes da carcaça de frangos (carne, pele e sangue) e das proteínas dos músculos (miosina, actina, proteínas sarcoplasmáticas e do teci- Outros trabalhos foram realizados com proteínas de mamíferos.…”

Section: -Introduçãounclassified

“…Particularmente, as características funcionais e texturais da carne cozida dependem do comportamento tér-mico das proteínas miofibrilares [14].A estrutura nativa das proteínas é estabilizada por forças moleculares internas, que são reduzidas com o aumento da temperatura [16]. Acima de certa temperatura, ocorre uma transição do tipo ordem-desordem, quando as proteínas são desenroladas ("unfolded"), ocorrendo um fenômeno conhecido como desnaturação.…”

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Análise térmica da carne de coelhos

Furukawa¹,

Sobral²,

Habitante³

et al. 2004

Ciênc. Tecnol. Aliment.

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-INTRODUÇÃOO aquecimento da carne durante seu cozimento produz alterações na sua aparência, no seu sabor e na sua textura, ocorrendo encolhimento, liberação de suco celular, descoloração, que são causados por mudanças nas proteínas do músculo, que são termosensíveis [9]. Particularmente, as características funcionais e texturais da carne cozida dependem do comportamento tér-mico das proteínas miofibrilares [14].A estrutura nativa das proteínas é estabilizada por forças moleculares internas, que são reduzidas com o aumento da temperatura [16]. Acima de certa temperatura, ocorre uma transição do tipo ordem-desordem, quando as proteínas são desenroladas ("unfolded"), ocorrendo um fenômeno conhecido como desnaturação. Esse fenômeno é uma transição de fase de primeira ordem, e pode ser caracterizado pela temperatura (Td) e entalpia de desnaturação (rHd RESUMOO objetivo deste trabalho foi avaliar o efeito da adição de condimentos na carne de coelho, sobre a estabilidade térmica de suas proteínas miofibrilares. Retalhos de 24 músculos Longissimus dorsis foram moídos e misturados, para a obtenção de um lote homogê-neo. Foram adicionados, em alíquotas dessa carne: 1,0; 2,0 ou 3,0% de sal; 2,5; 5,0 ou 7,5% de sacarose e 1,5; 3,0 ou 4,5% de ácido acético 3% em solução aquosa, e uma mistura perfazendo 3% de sal, 5% de sacarose e 3% da mesma solução de ácido acético. Após homogeneização manual, as amostras foram mantidas em repouso sob refrigeração, por 30 minutos. Alíquotas da ordem de 10mg foram usadas para análise térmica e o restante, para análises de pH, proteínas e umidade. As análises térmicas foram realizadas em um calorímetro diferencial de varredura DSC-TA2010, a 10ºC/min, entre 0 e 100ºC. As curvas de DSC da carne pura apresentaram endotermas nas temperaturas de (Td) 58,4(0,7ºC (miosina) e 78,2(0,2ºC (actina), envolvendo entalpia (rHd) de 17,5J/g de proteínas. O sal e o ácido acético desestabilizaram as proteínas, provocando redução da Td da miosina e actina, contrariamente à sacarose, que apresentou efeito estabilizante. A adição da mistura dos condimentos desestabilizou as proteínas miofibrilares. Apenas o ácido, adicionado acima de 1,5%, provocou desnaturação das proteínas. Palavras-chave: proteínas miofibrilares; desnaturação; análise calorimétrica diferencial; sal; sacarose; ácido acético. SUMMARYTHERMAL ANALYSIS OF RABBIT MEAT. The objective of this work was to evaluate the effect of some additives over the myofibrillar protein thermal stability of rabbit meat. Steaks of 24 Longissimus dorsis muscle were ground and mixed to obtain a homogeneous portion. Samples of this meat were added with: 1.0, 2.0, or 3.0% of salt; 2.5, 5.0, or 7.5% of saccharose and 1.5, 3.0 or 4.5% of acid acetic solution 3%, and a mixture with 3% salt, 5% saccharose and 3% of the same acid acetic solution. After manual homogenization, the samples were stored refrigerated for 30 minutes. The meat was analyzed for thermal behavior, pH, protein and water content. The thermal analysis was done with a differential scanning calorimeter DSC-T...

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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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Thermal Denaturation of Aulacomya ater ater (Molina) Myofibrillar Proteins: A Differential Scanning Calorimetric Study

Cited by 23 publications

References 20 publications

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

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

Análise térmica da carne de coelhos

Differential Scanning Calorimetry

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