• Food Science of Animal Resources
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• v.39 no.2
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• pp.229-239
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• 2019

The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.

• Korean Journal of Food Science and Technology
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• v.23 no.4
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• pp.428-432
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• 1991

This study was carried out to investigate the effect of NaCl, pH and phosphate on the functional properties of a mixed system of plasma protein and myofibrillar proteins. The solubility of plasma protein, myofibrillar protein and the mixture (plasma+myofibrillar protein) increased according to the increase of NaCl concentration ($0{\sim}4%$) and pH $pH4{\sim}8$). The solubility, emulsifying activity and capacity of the mixture were lower than those of plasma protein, whereas higher than those of myofibrillar protein. The gel strength of the mixture and myofibrillar protein showed a significant increase when NaCl concentration was increased from 2 to 3%. The gel strength of myofibrillar protein increased about four times when 0.3% polyphosphate added to the sample containing 2% NaCl, whereas the moisture loss of the mixture and myofibrillar protein decreased significantly. The gel strength of plasma protein, myofibrillar protein and the mixture increased slightly at $3{\sim}5%$ protein concentration, whereas the gel strength of those increased significantly as the protein concentration increased from 5 to 9%.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.4
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• pp.574-578
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• 2001

Myofibrillar proteins were prepared from red muscle and white muscle of fresh water fish and sea water fish, and their thermostabilities and effect of temperature on the myofibrillar ATPase activities were compared. Differences in temperature dependency of myofibrillar ATPase activities were found between two species. Thermodynamic data for inactivation of myofibrillar proteins, such as D value, Z value, $\Delta$ $H^{{\neq}}$, $\Delta$ $G^{{\neq}}$ and $\Delta$ $S^{\neq}$ revealed that thermostabilities of myofibrillar proteins from fresh water fish were higher than those from sea water fish, and that myofibrillar proteins from red muscle were more heat labile than those from white muscle.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.10
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• pp.1611-1620
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• 2019

Objective: The aim was to investigate the influence of ultrasound and adenosine 5'-monophosphate (AMP) marination (UAMP) on tenderness and structure of myofibrillar proteins of beef. Methods: Five groups, the untreated meat (Control), deionized water marination (DW), ultrasound followed by DW (UDW), AMP marination (AMP), and ultrasound followed by AMP (UAMP) were studied. Myofibrillar fragmentation, cooking loss, shear force, thermograms, histological observation of meats and myofibrillar proteins properties were investigated in these different treatments. Results: The results showed that UAMP significantly increased myofibrillar fragmentation index from 152 (Control), 231 (AMP), and 307 (UDW) to 355 (p<0.05), respectively. The lowest cooking loss, shear force and peak denaturation temperature were observed in UAMP. In histological observation, UDW and UAMP had more fragmented muscular bundles than the others. Furthermore, a drastic increase in ${\alpha}$-helix and decrease in ${\beta}$-sheet of myofibrillar proteins was observed in UAMP, implying the disaggregation of protein samples. The synchronous fluorescence spectra of myofibrillar proteins in UAMP suggested the combination of ultrasound and AMP could accelerate the unfolding molecular structure and destroying hydrophobic interactions. The results of circular dichroism and synchronous fluorescence spectra for myofibrillar proteins coincided with the microstructures of beef. Conclusion: The results indicate that ultrasound combined with AMP improved meat tenderness not only by disruption in muscle integrity, increasing water retention, but also altering their spatial structure of myofibrillar proteins.

• The Korean Journal of Food And Nutrition
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• v.10 no.2
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• pp.160-165
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• 1997

The actomyosin and myosin of the squid at 3$0^{\circ}C$ showed the highest Vmax and the actomyosin and myosin of the clam at 35$^{\circ}C$ and HMM at $25^{\circ}C$ showed the highest Vmax the thermostability of myofibrillar proteins is changed greatly according to the difference of KCI concentration. The myofibrillar proteins of the clam showed a higher thermostability than the myofibrillar proteins of the squid. When 3% ethanol solution was added and heated myofibrillar proteins, denaturation was accelerated and it was shown that there was a difference between animals in the denaturation velocity.

• The Korean Journal of Food And Nutrition
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• v.10 no.2
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• pp.151-159
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• 1997

In order to compare and examine the general characteristics of myofibrillar proteins which is an important protein source as a food resource and relates directly with muscle contraction, we have extracted the myofibrillar proteins from squid and clam. The ionic strength of myofibrillar proteins connected with Ca-ATPase activity, Mg-ATPase activity and EDTA-ATPase activity showed distinct differences between squid and clam. In the activity-pH curve, actomyosin of the clam had a weak biphasic response. In the low concentration of dioxane, myofibrillar proteins of the squid showed a sudden decrease in activity but myofibrillar proteins of the clam showed in increase in activity. Ethanol and metanol in low concentration caused myosin and HMM from the squid and clam to increase their activities. If we cause modification by NEM, under 10-6M concentration, the activity was increased but above 10-5M concentration, there was a sudden decrease in activity.

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.536-541
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• 1998

This study was carried out to investigate the changes of characteristics of myofibrillar protein for the vacuum chilled, the air frozen or the rechilled Holstein beef loin. The vacuum chilled beef was stored at 1$^{\circ}C$ and the air frozen beef was stored at -20$^{\circ}C$ for 60 days. The rechilled beef was restored for 3 days at 1$^{\circ}C$ by using the vacuum chilled or the air frozen beef. Myofibrillar protein extractability, 30,000 dalton component content and Mg-ATP ase activity for the vacuum chilled beef were higher than those of the air frozen beef. Each parameters increased significantly for the vacuum chilled beef after the 20 days storage, but there was no significant difference for the vacuum chilled beef after the 20 days storage, but there was no significant difference for the air frozen beef during the 60 days storage. By the rechilling process, myofibrillar protein extractability of the vacuum chilled and the frozen beef were not significant difference. The 30,000 dalton component of the vacuum chilled beef was showed not significant increment by rechilling, but the frozen beef was showed significant increment by rechilling. The Mg-ATPase activity of myofibrillar protein of the vacuum chilled beef was not changes by rechilling, but the frozen beef after the 20 days storage was significant increment by rechilling.

• Korean Journal of Food Science and Technology
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• v.20 no.6
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• pp.862-867
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• 1988

Myofibrillar proteins were prepared from cold(pollack, salmon) and warm current fish(shark), and their thermostabilities were compared. Thermodynamic data for inactivation of myofibrillar proteins, such as D-value, Kd-value, revealed that thermostability of myofibrillar proteins from warm current fish was higher than that from cold current fish.

• Korean Journal of Food Science and Technology
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• v.22 no.4
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• pp.466-472
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• 1990

The effect of sugar addition and heat treatment on the myofibrillar protein extractability was studied. Maillard reaction was dependent on heating time significantly and glucose revealed the highest reactivity for Maillard reaction. The extractability of myofibrillar proteins was lowest in case of glucose addition and decreased according to increasing of heating time, Higher extractability was resulted in by digestion of myofibrillar proteins with enzymes after sugar addition and heat treatment than the undigested samples, as the sample was digested with trypsin that is the highest. And by digestion with trypsin, chymotrypsin and peptidase at a time the extractability of meat proteins increased remarkably.

• Korean Journal of Food Science and Technology
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• v.20 no.3
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• pp.371-379
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• 1988

To investigate on the biochemical characteristics of myofibrillar proteins between cold(pollack, salmon) and warm current fish (yellow corbina, shark), myofibrils and actomyosin were prepared, and their biological activities, effect of temperature on the myofibrillar ATPase activities and SDS-polyacrylamide gel electrophoretic patterns of myofibrils were compared. SDS-polyacrylamide gel electrophoretic analysis showed that electrophoretic patterns of myofibril vary from fish to fish. Difference in KCl concentration dependency of myofibrillar ATPase activities and ATPase activity- pH curve were found among fish species. Myofibrillar proteins from cold current fish showed higher specific activity at low temperature $(5^{\circ}C-10^{\circ}C)$ than those from warm current fish.