Trial Determination of the Ratio of Myosin and Actin in Raw Meat by Differential Scanning Calorimetry

Mochizuki, Yoshinori; Mizuno, Haruo; Ogawa, Hiroo; Iso, Naomichi

doi:10.2331/fishsci.61.723

Cited by 10 publications

(3 citation statements)

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“…As presented in Figure a, the endothermic enthalpy Δ H I was 0.210 ± 0.022 J/g, and Δ H II was 0.088 ± 0.011 J/g for myosin and actin, respectively. These data were computed by the Gauss area numerical integration of the fractions in the DSC thermogram (Mochizuki, Mizuno, Ogawa, & Iso, ), and the proportion between the two proteins was 0.706:0.294, suggesting that the myosin content was 2.4 times the weight of actin in the false abalone pleopod.…”

Section: Resultsmentioning

confidence: 99%

“…(c) Calculated changes of the nondenaturation ratios of myosin and actin with the increase of temperature at a heating rate of 10 C /min, and the predicted peak temperature (T max 0 ) of each protein in the DSC measurement myosin and actin, respectively. These data were computed by the Gauss area numerical integration of the fractions in the DSC thermogram (Mochizuki, Mizuno, Ogawa, & Iso, 1995), and the proportion between the two proteins was 0.706:0.294, suggesting that the myosin content was 2.4 times the weight of actin in the false abalone pleopod.…”

Section: Muscle Protein Denaturation Kineticsmentioning

confidence: 99%

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Effects of muscle protein denaturation and water distribution on the quality of false abalone (Volutharpa ampullacea perryi) during wet heating

Sun

et al. 2018

J Food Process Engineering

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The effects of wet heating at 95–100 °C on the degree of myosin and actin denaturation in false abalone (Volutharpa ampullacea perryi) were predicted by a heat transfer model. The contributions of water mobility and tenderness to sensory acceptability were assessed after 5, 10, 15, 30, and 60 min heating treatments. 3D finite element heat transfer analysis and reaction kinetics demonstrated that the muscle proteins were completely denatured in 60–80 s during wet heating. In the low field 1H nuclear magnetic resonance (LF‐NMR) and magnetic resonance imaging (MRI) analyses, the content of immobilized water was reduced with extended cooking time, and the shear force also decreased. Sensory acceptability was reduced with the increase of cooking time. Partial least squares (PLS) analysis indicated a high correlation among immobilized water, color, taste, and sensory acceptability. Our results may help in understanding the mechanisms of quality assessment and control during seafood cooking. Practical applications False abalone (Volutharpa ampullacea perryi) has been widely consumed as it can provide a high quality of nutrition with a relatively inexpensive cost. Wet heating is the most conventional processing procedure, then the effects of heating on the sensory and textual properties of false abalone meat should be carefully controlled. Since most researches are concerning the changes of collagen, the present study provided quantitative characterizations of muscle protein denaturation and water distribution on the quality of false abalone using 3D finite element heat transfer analysis, LF‐NMR, MRI techniques, and PLS analysis. The results would be useful to simulate actin and myosin denaturation as well as the protons distribution under different thermal schedules of food cooking, and they could be applied for the food quality control in the industry.

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Section: Resultsmentioning

confidence: 99%

Section: Muscle Protein Denaturation Kineticsmentioning

confidence: 99%

Effects of muscle protein denaturation and water distribution on the quality of false abalone (Volutharpa ampullacea perryi) during wet heating

Sun

et al. 2018

J Food Process Engineering

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“…As shown in Figure 4, two major endothermic transitions with the temperature maximums (Tm) of 50.92°C (ΔH I = 1.589 J/g) and 74.09°C (ΔH II = 2.019 J/g) were observed. These were considered to correspond to the two main constituents of myofibrillar protein, myosin and actin, respectively, based on the information Response surface graph for the effect of E/S ratio, time and temperature on hydroxyl radical scavenging activity of grass carp myofibrillar protein hydrolysates, where X 1 is E/S ratio (%, w/w); X 2 is time (h); X 3 is temperature (°C); and Y is hydroxyl radical scavenging activity expressed as IC 50 value (μg/ml): (A) the temperature (X 3 ) was set at the center of its leval viz 52.5°C; (B) the time (X 2 ) was set at the center of its leval viz 6.5 h; (C) the E/S ratio (X 1 ) was set at the center of its leval viz 0.5% (w/w) (A) (B) obtained from the reports by Damodaran (1997) and Mochizuki et al (1995). The transition at 111.85°C was not well resolved and, consequently, was not further analysed.…”

Section: Resultsmentioning

confidence: 99%

Enzymatic hydrolysis of grass carp myofibrillar protein and antioxidant properties of hydrolysates

Ren¹,

Wang²,

Zhao³

et al. 2010

Czech J. Food Sci.

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Ren J., Wang H., Zhao M., Cui Ch., Hu X. (2010): Enzymatic hydrolysis of grass carp myofibrillar protein and antioxidant properties of hydrolysates. Czech J. Food Sci., 28: 475-484.Myofibrillar protein was extracted from grass carp, a freshwater fish, and hydrolysed using five commercial proteases (papain, pancreatin 6.0, bromelain, Neutrase 1.5MG, and Alcalase 2.4 L). The antioxidant activities of the hydrolysates were determined. Pancreatin 6.0 proved to be the most efficient protease for hydrolysing myofibrillar protein with a very high protein recovery (90.20%), its hydrolysates exhibiting the highest hydroxyl radical (•OH) scavenging activity (IC 50 = 349.89 ± 11.50 μg/ml) out of all five hydrolysates. Molecular weight distribution analysis revealed that pancreatin 6.0 hydrolysate rendered a higher proportion of the 6−10 kDa fraction and a lower proportion of the 3−6 kDa fraction as compared with other hydrolysates. The maximum •OH scavenging activity for pancreatin 6.0 hydrolysate (IC 50 = 229.90 µg/ml) was obtained at the enzyme to substrate ratio of 0.52%, the incubation time of 7.03 h, and the incubation temperature of 50.56°C, as optimised by response surface methodology. In vitro antioxidant experiments proved that pancreatin 6.0 hydrolysates had obvious inhibitory effects on lipid peroxidation and low-density lipoproteins oxidation under optimised conditions.

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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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Trial Determination of the Ratio of Myosin and Actin in Raw Meat by Differential Scanning Calorimetry

Cited by 10 publications

References 0 publications

Effects of muscle protein denaturation and water distribution on the quality of false abalone (Volutharpa ampullacea perryi) during wet heating

Effects of muscle protein denaturation and water distribution on the quality of false abalone (Volutharpa ampullacea perryi) during wet heating

Enzymatic hydrolysis of grass carp myofibrillar protein and antioxidant properties of hydrolysates

Differential Scanning Calorimetry

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