• 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.

• Journal of Life Science
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• v.7 no.4
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• pp.336-341
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• 1997

This study was conducted to investigate the effects of carcass grade on the hardness, myofibrillar fragmentations index, protein extractability and Mg-ATPase activity of myofibril and actomyosin obtained from 1, 2, 3 and D carcass grade)subgrade) in Korean native cow. Proximate component, hardness, chewiness, myofibril fragmentation index, protein extractability and Mg-ATPase activity if myofibril or actomyosin were not significantly different between 1st and 2nd carcass grade loin. The hardness and chewiness of 2nd carcass grade loin's were significantly lower than 3th grade loin's, but the myofibril fragmentation index, sarcoplasmic protein extractability and Mg-ATPase activity of myofibril were higher. The myofibrillar protein extractability and Mg-ATPase activity of actomyosin obtained from 3th carcase grade loin's were significantly higher than D grade loin's, but the hardness, chewiness and stroma protein extractability were lower. In conclusion, the degree of toughness in Korean native cow's loin was not significantly different between 1st and 2nd grade, but 3rd and D carcass grade were significantly higher, regardless of before and after aging.

• Korean Journal of Food Science and Technology
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• v.28 no.3
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• pp.566-572
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• 1996

The relationship between the myofibrillar fragmentation and zeugmatin during post-mortem aging was in vestigated by indirect immunofluorescence method using antizeugmatin Antiserum as a measure of meat tenderization. The antizeugmatin antiserum was prepared using bands separated by SDS-PAGE and reacted specifically with zeugmatin, showing no cross-reactivity with the other myofibrillar proteins. By the indirect immunofluorescence method, this antiserum stained the fresh myofibrillar However, the fluorescence intensity decreased with post-mortem time and almost disappeared within 24 hr of storage, in parallel with the myofibrillar fragmentation. It was therefore concluded that zeugmatin can be conveniently used as a measure of meat tenderization during post-mortem aging by immunoflurescence method.

• The Korean Journal of Food And Nutrition
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• v.2 no.2
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• pp.21-26
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• 1989

The morphological changes of fresh beef treated with ficin(0.1% : 2 hrs, 6 hrs)were examined with transmission electron microscope(TEM), the results obtained were as follows ; Connective tissue protein in fresh beef treated with ficin became gradually fragmentation and was occurred solubilization with time The length of sarcomere in myofibrillar protein was elongated, M-line became dim, and the 1-band of Z-line was broken and beck me fragmentation with time.

• The Korean Journal of Food And Nutrition
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• v.11 no.4
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• pp.409-415
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• 1998

This study was carried out to investigate the effects of freezing temperature on quality of vacuum packaging freezed beef. In case of thaw drip loss, the freezing of -3$^{\circ}C$ and -20$^{\circ}C$ were 5.23% and 5.17% to 60 days respectively, were increased significantly during freezing. The cooking loss of water bath and pan were increased significantly during freezing than the beginning of freezing, but were no different between -3$^{\circ}C$ and -20$^{\circ}C$. The salt soluble protein extractability was decreased during freezing, the -20$^{\circ}C$ freezing was higher than -3$^{\circ}C$freezing. The water soluble protein extractability was increased during freezing higher than during freezing. The myoglobin denatured percentage of the -3$^{\circ}C$ freezing was higher than -20$^{\circ}C$ freezing, the 15 days storage of -3$^{\circ}C$ freezing was highest to 96%. The shear force value was not change during freezing, the myofibrillar fragmentation index during freezing was higher than the beginning of freezing, but was not change during freezing. The pH was decreased to freezing 45 days, after that increased.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.5
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• pp.721-724
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• 2002

Postmortem Proteolysis of breast (BM) and leg (LM) muscles in Chiayi native chickens at $5^{\circ}C$ were compared. Myofibrils were purified from BM and LM samples that were randomly taken from carcasses after 0, 1, 3, 7 and 14 days of storage at $5^{\circ}C$. Fragmentation of myofibrils were determined, and degradation of myofibrillar proteins were analyzed by the SDS-PAGE and western blots. The results showed that myofibril fragmentation index (MFI) was significantly (p<0.05) higher in BM than in LM samples. Disappearance of titin and nebulin and appearance of the 30 kDa component were more rapidly as seen on SDS-PAGE in BM than in LM samples. Western blots labeled with a monoclonal antibody to desmin also demonstrated that desmin degraded more quickly in BM samples. Our data suggested that postmortem proteolysis occurred more rapidly in breast muscles in Chiayi native chickens.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.4
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• pp.647-653
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• 1997

To establish the index of aging stage for cold storage beef tenderloin, shear force value(SFV), Mg-ATPase activity, myofibrillar fragmentation index(MFI), myofibrillar fragmentation ratio(MFR) and appearance of 30KD(30KD) were measured as the parameters for the indices of aging stage. Aging index of air-packed beef tenderloin stored for 14 days at 3$^{\circ}C$ were useful in the order of SFV(r=-0.893)>MFR (r=0.863) >30KD(r=0.853)>MFI(r=0.814)>Mg-ATPase activity(г=0.804). Vacuum-packed beef tenderloin stored for 28 days at 3$^{\circ}C$ were useful in the order of MFR(r=0.880)>30KD(r=0.836). In case of the correlation between aging indices of air-packed beef tenderloin, MFR had relation with SFV, Mg-ATPase activity, MFI and 30KD. In case of the correlation between aging indices of vacuum-packed beef ten- derloin, MFR had relations with 30KD.

• Food Science of Animal Resources
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• v.18 no.3
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• pp.216-223
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• 1998

This study was conducted to investigate the effects of the tenderness for the vacuum chilled, the air-frozen or the rechilled Holstein beef loin. The vacuum packaged beef was stored at 1$^{\circ}C$ and the air-packaged 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. Hardness and chewiness of the vacuum chilled beef were better than those of the air-frozen beef. Hardness and chewiness were improved significantly(p＜0.05) after the 40 days storage for the vacuum chilled beef, but there was no significant improvement for the air-frozen beef during the 60 days storage. By the rechilling process, tenderness and myofibrillar fragmentation index of the vacuum chilled and air-frozen beef improved. Especially those were improved significantly(p＜0.05) in the vacuum chilled beef after the 20 days storage, and in the air-frozen beef after the 40 and 60 days storage.

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.482-487
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• 1998

This study was carried out to investigate the effects of freezing temperature on quality of thawed beef loin. In case of thaw drip loss, the freezing of -3$^{\circ}C$ and -2$0^{\circ}C$ were higest by 3.4% to 30 days and by 1.8% to 60 days, respectively. And the thaw drip loss of -3$^{\circ}C$ freezing was more than -2$0^{\circ}C$ freezing. The cooking loss of water bath and pan boiling were increased significantly during freezing than the beginning of freezing, but were not different -3$^{\circ}C$ and -2$0^{\circ}C$. The salt soluble protein extractability was decreased during freezing, the -2$0^{\circ}C$ freezing was higher than -3$^{\circ}C$ freezing. The water soluble protein extractability of -3$^{\circ}C$ freezing was not significant different during freezing storage, that freezed at -2$0^{\circ}C$ was increased during freezing. The "L" value of the beginning of freezing was higher than during freezing, the "a" value was not different during freezing, and the "b" value during freezing was higher than the beginning of freezing. The myoglobin denatured percentage of the -3$^{\circ}C$ and -2$0^{\circ}C$ freezing were highest by 94.4% to 45 days and by 94.0% to 15 days, respectively. The shear force value during freezing was higher than the beginning of freezing, the myofibrillar fragmentation index was not significant different during freezing. The pH was increased to freezing 30 days, after that was decreased.ays, after that was decreased.

• Food Science of Animal Resources
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• v.31 no.3
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• pp.389-397
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• 2011

This study was conducted to examine the effect of salt concentration in soybean sauce (ganjang) on pre-rigor ground Hanwoo (Korean native cattle) muscle. Although adding soybean sauce reduced pH of pre-rigor Hanwoo muscle, it improved the water holding capacity (WHC), cooking loss, total protein solubility, myofibrillar fragmentation index (MFI), 2-thiobar-bituric acid (TBA) values, and textural properties by increasing salt concentration in the soybean sauce. In particular, adding soybean sauce inhibited lipid oxidation despite increasing salt concentration. An increased salt concentration in the soybean sauce in pre-rigor Hanwoo muscle tended to make the meat have lower lightness and higher redness and yellowness values. Although soybean sauce had a significantly lower pre-rigor salting effect than sodium chloride in terms of cooking loss and total protein solubility (p<0.05), soybean sauce improved myofibrillar fragmentation and lipid oxidation when compared with sodium chloride. Furthermore, no significant differences in textural properties were observed between adding soybean sauce and sodium chloride at the same salt concentrations. Therefore, soybean sauce can be a functional curing material for pre-rigor muscle.