Effect of marination on the thermodynamic properties of chicken muscle proteins studied by DSC

Tomaszewska-Gras, Jolanta; Konieczny, P.

doi:10.17221/297/2011-cjfs

Cited by 11 publications

(4 citation statements)

References 16 publications

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“…Following numerous studies, both marine and freshwater A. woodiana may constitute safe biomaterial of potential processability [3,5,6]. Evaluation of the possibility to use them requires extensive and multidirectional studies including the studies of the functional properties of proteins, i.e., those physicochemical properties that influence the behavior of proteins during processing, storage and feed/food consumption [7].…”

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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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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“…In addition, during the continuous heating process, the loss of water caused a gradual increase in cooking loss. Note that 50 • C was known as the coagulation temperature of myosin in duck meat, which was lower around 10 • C than the collagen degeneration temperature (Tomaszewska-Gras & Konieczny, 2012). When heated to 70 • C, the muscle fibers contract which attribute to denaturation and coagulation of myosin, and the water in the muscle is squeezed out, thus more water would be lost (Zielbauer et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Study on the water state, migration, and microstructure modification during the process of salt‐reduced stewed duck

Kuang

et al. 2021

Journal of Food Science

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High salt content is one of the major problems for stewed products. To help address this issue, the effect of salt reduction on water migration in stewed ducks was investigated through diverse approaches, including water activity (Aw) and water-holding capacity (WHC) assay, as well as low-field nuclear magnetic resonance (LF-NMR) and scanning electron microscopy (SEM) observation. Our results showed that Aw value remained stable, while centrifugal loss decreased, and cooking loss increased significantly (p < 0.05). The analysis of NMR indicated that, during the marinating stage, the proportion of immobilized water increased from 86.86%-89.66% (sodium chloride group) and 90.51% (saltreduced group), respectively. After 2 h, the free water content became 0, and then became stable until the end of marinating. In the stewing stage, at the beginning 20 min, relaxation time of immobilized water decreased to about 35 ms and the ratio of immobilized water significantly reduced (p < 0.05) by 5.38% (sodium chloride group) and 5.95% (salt-reduced group), respectively. Free water peak was detected upon stewing of 10 min, and 20 min later, there was no significant difference in the proportion of free water (p > 0.05). In general, no significance was observed in water behavior and microstructure of stewed duck meat between the salt reduction group and sodium chloride group. In addition, SEM analysis revealed that marinating could expand the muscle fiber gap to accommodate more immobilized water. However, the fiber was looser at the initial stage of stewing and then became more compact. Practical Application: This work demonstrates potentially feasible to produce salt-reduced duck products.

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“…This technique enables the investigation of protein behaviour in situ in very small amounts. DSC has been widely used to analyse the muscle proteins from chicken, beef, pork [14][15][16], fish meat, and other freshwater sources [17,18].…”

Section: Introductionmentioning

confidence: 99%

The effect of deep pectoral myopathy on the properties of broiler chicken muscles characterised by selected instrumental techniques

Stangierski

Tomaszewska-Gras

Baranowska

et al. 2018

Eur Food Res Technol

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Changes in the biophysical traits of the pectoral muscles of chickens with deep pectoral myopathy (DPM) were analysed with selected instrumental techniques. For comparative purposes, the research used both samples of pectoralis minor muscles of 39-42-day-old Cobb 500 broiler chickens and pectoralis major muscles with DPM symptoms, as well. Computer Image Analysis (CIA) revealed that the pectoral minor muscles with DPM were characterised by smaller area of muscle fibres' cross-sectional area (CSA) than normal muscles. A longitudinal section of DPM muscles also confirmed the presence of large spaces between the bundles of muscle fibres. The results of Differential Scanning Calorimetry (DSC) analysis showed that all the temperatures of transformations referring to minor muscles with myopathy symptoms were significantly lower than the temperatures noted in the muscles without DPM. The enthalpy values observed in both pectoral muscles with DPM were significantly lower than the values noted in healthy muscles. The water dynamics analysed by low-field NMR showed that the values of spin-lattice relaxation time T 1 in p. major muscles without DPM were higher than the values in the muscles with the defect. On the other hand, an inverse dependence was observed in p. minor muscles samples. The value of the long relaxation time T 22 was reduced in both muscles with pathological lesions. In conclusion, three advanced analytical tools used in this study (CIA, DSC, and LF NMR) provide new insight into the characterization of protein changes observed in the pectoral muscles of chicken broilers with DPM.

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Effect of marination on the thermodynamic properties of chicken muscle proteins studied by DSC

Cited by 11 publications

References 16 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)

Study on the water state, migration, and microstructure modification during the process of salt‐reduced stewed duck

The effect of deep pectoral myopathy on the properties of broiler chicken muscles characterised by selected instrumental techniques

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