NMR relaxometry and differential scanning calorimetry during meat cooking

Water binding in fat-in-water emulsions with native potato starch was investigated at the molecular level using the low-field nuclear magnetic resonance method. Analysis of relaxation time changes with temperature allowed determination of activation energy values for water molecules. Application of potato starch as an emulsifier required selection of an appropriate polymer content. Optimal water binding was recorded when emulsions contained 6 parts of potato starch per 10 parts of fat. Activation energy values of water molecule rotations were more than twice values in comparable gels. Emulsions were more stable than starch gels with the same polymer concentration in water. Comparison of fat-water emulsions demonstrated that use of porcine fat allowed development of emulsions in which water was more strongly bound.

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“…In this approach, results are used most frequently for analysis of water binding at the molecular level (19)(20)(21)(22)(23)(24)(25)(26).…”

Section: Introductionmentioning

confidence: 99%

Emulsions stabilized using potato starch

Baranowska

Rezler

2015

Food Sci Biotechnol

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“…Similar methods have been used to study thermal denaturation behavior of myosin [20][21][22] and actin 23,24 . Nevertheless, most of these methods require extraction and solubilization of the protein of interest and are neither applicable for the investigation of complex tissues nor do they allow for simultaneous observation of ongoing structural changes at the required optical resolution.…”

Section: Introductionmentioning

confidence: 99%

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

et al. 2009

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Myofibers and collagen show non-linear optical properties enabling imaging using second harmonic generation (SHG) microscopy. The technique is evaluated for use as a tool for real-time studies of thermally induced changes in thin samples of unfixed and unstained pork. The forward and the backward scattered SHG light reveal complementary features of the structures of myofibers and collagen fibers. Upon heating the myofibers show no structural changes before reaching a temperature of 53°C. At this temperature the SHG signal becomes extinct. The extinction of the SHG at 53°C coincides with a low-temperature endotherm peak observable in the differential scanning calorimetry (DSC) thermograms. DSC analysis of epimysium, the connective tissue layer that enfold skeletal muscles, produces one large endotherm starting at 57°C and peaking at 59.5°C. SHG microscopy of collagen fibers reveals a variability of thermal stability. Some fibers show severe shrinkage at 57°C, before the signal for most of them vanishes between 59°C and 61°C and thus coinciding with the endotherm of the thermograms. However, in some areas, strong SHG signals from collagen can be visualized even after prolonged heating to 67°C and thus indicating regions of much higher thermal stability. It is seen that the benefits of the structural and temporal information available from SHG microscopy reveals complementary information to a traditional DSC measurement and enables a more complete understanding of the thermal denaturation process.

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“…On the thermal curve, three endothermic transitions are visible, which can be ascribed to the denaturation temperatures (T max ) of myosin (51°C), sarcoplasmic and connective tissue proteins (56°C), and actin (68°C). Typical transition temperatures of chicken breast muscle (pectoralis major) can range from 49°C to 57°C for myosin and its subunits, 61-67°C for sarcoplasmic proteins, and 76-79°C for actin (Xiong et al 1987;Kijowski & Mast 1988;Wang & Smith 1994;Murphy et al 1998;Wattanachant et al 2005;Bertram et al 2006). On the basis of the collected results (Table 2), it may be stated that the values of enthalpy and denaturation temperature in all marinated samples differed significantly (P < 0.05) from the non-marinated sample, for which the highest values of enthalpy and denaturation temperatures of myosin and actin were recorded.…”

Section: Resultsmentioning

confidence: 99%

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

Tomaszewska-Gras¹,

Konieczny²

2012

Czech J. Food Sci.

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Tomaszewska-Gras J., Konieczny P. (2012): Effect of marination on the thermodynamic properties of chicken muscle proteins studied by DSC. Czech J. Food Sci., 30: 302-308.The marination of meat is a method applied to improve the sensory values like tenderness and juiciness of meat, and to enhance microbiological safety of the product. The effects of specific marinades on the thermal stability of the muscle proteins using differential scanning calorimetry (DSC) was examined. Various marinades were tested, composed mainly of NaCl as well as triphosphates and organic acids, self made marinades, and ready-to-use marinades used in industrial practice. As a result of the experiment conducted, it was found that all marinades used changed significantly the thermal stability of muscle proteins. The use of sodium chloride and sodium triphosphate for marination caused a reduction of enthalpy and denaturation temperature of myosin and actin. However, a greater influence on the stability of muscle proteins was observed with marinades containing organic acids (acetic and citric). The most significant reduction of the denaturation temperatures and enthalpy (to the lowest level of 0.56 J/g) was found for self made marinade composed of 20.7% cider vinegar and 16% lemon juice.

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NMR relaxometry and differential scanning calorimetry during meat cooking

Cited by 98 publications

References 17 publications

Emulsions stabilized using potato starch

Emulsions stabilized using potato starch

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

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

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