• 한국축산식품학회지
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• 제35권5호
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• pp.577-584
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• 2015

This study was conducted to evaluate the effect of pre-rigor salting level (0-4% NaCl concentration) on physicochemical and textural properties of pre-rigor chicken breast muscles. The pre-rigor chicken breast muscles were de-boned 10 min post-mortem and salted within 25 min post-mortem. An increase in pre-rigor salting level led to the formation of high ultimate pH of chicken breast muscles at post-mortem 24 h. The addition of minimum of 2% NaCl significantly improved water holding capacity, cooking loss, protein solubility, and hardness when compared to the non-salting chicken breast muscle (p<0.05). On the other hand, the increase in pre-rigor salting level caused the inhibition of myofibrillar protein degradation and the acceleration of lipid oxidation. However, the difference in NaCl concentration between 3% and 4% had no great differences in the results of physicochemical and textural properties due to pre-rigor salting effects (p>0.05). Therefore, our study certified the pre-rigor salting effect of chicken breast muscle salted with 2% NaCl when compared to post-rigor muscle salted with equal NaCl concentration, and suggests that the 2% NaCl concentration is minimally required to ensure the definite pre-rigor salting effect on chicken breast muscle.

• 디지털콘텐츠
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• 12호통권127호
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• pp.160-165
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• 2003

• Applied Biological Chemistry
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• 제14권2호
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• pp.165-169
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• 1971

Slushed ice와 dry chilling chamber에 각각 도계 직후 냉장한 12주생 영계의 가슴 및 다리 근육으로부터 KCl-phosphate buffer를 사용하여 도계후 $1{\sim}25$시간 사이에 함질소물을 추출했다. Extractable nitrogen의 변화는 주로 myosin의 extractability 감소, 그리고 어느정도 actomyosin의 extractability 증가 결과로 일어남이 밝혀졌으며, 한편 stroma. sarcoplasmic protein 및 비단백함질소물(none protein nitrogen)의 변화는 적었다. Myosin extractability는 도계후 처음 3시간 동안에 급격히 감소하여 그후 계속적으로 wet chilling 동안 감소했으나 dry chilling의 경우 myosin extractability의 감소는 가슴근육보다 다리근육에서 더 많았으며 extractability는 도계 17시간 후부터 증가했다. Actomyosin은 wet chilling의 경우 계속적으로 소량밖에 추출되지 않았으나 dry chilling의 경우 도계후 17시간 이후부터 증가했는데, 이런 경향은 breast muscle과 leg muscle이 동일했다.

• 한국축산식품학회지
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• 제40권3호
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• pp.415-425
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• 2020

It is believed that two main proteolytic systems are involved in the tenderization of meat: the cathepsins and the calpains. Many researchers consider the calpain system to be the major contributor to meat tenderness during post-mortem storage. However, the role and activity of cathepsins during post-mortem storage or low temperature meat processing is unclear, particularly for the tough meat cuts like brisket. Thus, the study was designed to investigate the effects of cold (refrigerated and frozen) storage and sous vide processing on the activities of cathepsin B, H, and L in beef brisket. There were no significant changes in pH and cathepsin H activity throughout the 18 d of storage at both temperatures. However, an increase in cathepsin B activity was observed during the first 4 d at both storage temperatures, but subsequently the activity remained unchanged. Cathepsins B and L were found to be more heat stable at sous vide temperatures (50℃ for 24 h, 55℃ for 5 h and at 60℃ and 70℃ for 1 h) compared to cathepsin H. Cathepsin B+L activity was found to increase after sous vide cooking at 50℃ for 1 h but decreased to about 47% relative to the uncooked control after 24 h of cooking. These results suggest that cathepsins B and L may contribute to the improved meat tenderness usually seen in sous vide cooked brisket meat.

• 사상체질의학회지
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• 제18권2호
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• pp.83-95
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• 2006

1. Objectives and Methods The purpose of this study was to objectify the diagnosis of Sasang constitution. It analyzed the adult male and female voices into 23factors using PSSC-2004. The study was conducted by subjects inputting 2.5-3 sec of [a] in 586 men and women's voices to PSSC-2004. The statistical analyses are applied to three groups: total group, male group, female group. The group with a total of 586 was composed of 155 Soyangin, 230 Taeumin and 201 Soeumin. The male group was composed with 61 Soyangin, 127 Taeumin and 87 Soeumin. The female group was composed with 94 Soyangin, 103 Taeumin and 114 Soeumin. Taeyangin were excluded for a more accurate statistical analysis. 2. Results (I) In total group, Taeumin's peak sum was significantly high compared with the others(P=0.021). It was significant for distinction between Taeumin and Soyangin at the result of post mortem. (2) In total group, the Soyangin's rank6, rank7 and rank8 were significantly high compared with the others (P=0.050)(0.043)(0.034). (3) In total group, the Soyangin's rank9 was significantly high compared with the others(P=0.025). It was significant for distinction between Taeumin and Soyangin at the result of post mortem. (4) In male group, the Soyangin's code3 was significantly high compared with the others(P=0.050). (5) In male group, the Soyangin's code1 was significantly low compared with the others(P=0.004). It was significant for distinction between Taeumin and Soyangin at the result of post mortem. (6) In male group, the Soyangin's rank1, rank2, rank3 and rank4 were significantly high compared with the others(P=0.017)(0.008) (0.005)(0.002). They were significant for distinction between Taeumin and Soyangin at the result of post mortem. (7) In female group, the Taeumin's code1 was significantly low compared with the others(P=0.016). It was significant for distinction between Taeumin and Soeumin at the result of post mortem. 3. Conclusion From above result, there is the possibility of efficiency standard gide for constitutional diagnosis by analyzation of the voices.

• 한국식품과학회지
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• 제9권4호
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• pp.295-305
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• 1977

근원성유로 부터 근수축조절단백질들을 추출정제하고 저장중의 변화를 연구하여 다음과 같은 결과를 얻었다. 1. ${\alpha}-actinin$은 그 분자형(分子形)이나 생물활성(生物活性)에 아무런 변화도 일으키지 않았다. 2. 근육저장중에 근원섬유의 troponin-troponin complex의 함량은 감소되고 있으며 troponin-tropomyosin complex의 troponin함유비(含有比)는 낮아지고 있다.

• Animal Bioscience
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• 제34권11호
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• pp.1849-1858
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• 2021

Objective: Tenderness is a very complex feature, and the process of its formation is very complicated and not fully understood. Its diversification is one of the most important problems of beef production, as a result beef aging is widely used to improve tenderness as it is believed to provide a homogeneous product to consumers. While few studies have evaluated the muscle structure properties in relation to tenderness from early post-mortem, there little to no information available on how the muscle nanostructure of beef carcasses changes during post-mortem ageing to determine the appropriate aging time for acceptable tenderness. Methods: Muscle nanostructure (myofibril diameter [MYD], myofibril spacing [MYS], muscle fibre diameter [MFD], muscle fibre spacing [MFS], and sarcomere length [SL]), meat tenderness and cooking loss [CL]) were measured on 20 A2 longissimus muscles of Bonsmara, Beefmaster, Hereford, and Simbra at 45_mins, 1, 3, and 7 days post-slaughter. Muscle nanostructure was measured using a scanning electron microscope, while tenderness was measured using Warner Bratzler shear force. Results: At 45 minutes post-slaughter, breed affected MYD and MYS only, while at 24_hrs it also affected MFD and MFS. On day 3 breed effected MFS and SL, while on day 7 breed effected tenderness only. As the muscles matured, both MYD and MYS decreased while CL increased, and the muscles became tender. There was no uniformity on muscle texture features (surface structure, fibre separation, muscle contraction, and relaxation) throughout the ageing period. Conclusion: Meat tenderness can be directly linked to breed related myofibril structure changes during aging in particular the MYD, spacing between myofibrils and their interaction; while the MFD, spacing between muscle fibres, SL, and CL explain the non-uniformity in beef tenderness.

• 해양환경안전학회:학술대회논문집
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• 해양환경안전학회 2018년도 공동국제학술발표회
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• pp.10-10
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• 2018

• 한국언론정보학보
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• 제68권
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• pp.65-86
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• 2014

이 논문은 사진과 죽음이 맺는 관계를 고찰하면서 매체로서의 사진이 가진 독특한 특성이 이 관계에 어떻게 영향을 미치고 있는지를 살펴보고 실제로 사진이 죽음을 재현하는 여러 방식들의 구체적 사례들을 분류, 분석함으로써 죽음을 재현하는 사진의 사회적 역할을 이해하는 기회를 제공하고자 한다. 조사 결과, 죽음 사진은 영정사진, 사후사진, 재해 및 전쟁사진, 처형사진, 의학과 법의학적 사진으로 구분되며 애도와 추모, 저항과 투쟁, 통치와 지배, 폭로와 고발의 역할을 한다.

• 한국축산식품학회지
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• 제18권4호
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• pp.292-300
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• 1998

This study was undertaken to determine the influence in the Z-disk domain of titin on the tenderization of meat by the structure change of myofibrillar Z-disks during post-mortem aging. After weakening the structure of Z-disks, the Z-disk region was splitted. As the results, myofibrils were fragmented by mechanical strength. Using indirect immunofluorescence microscopy, we show that the Z-disk domain of titin was disappeared from myofibrils in this period. There phenomenon were also shown by treating myofibrils with a solution containing 0.1mM $Ca^{2+}$. We conclude that change in Z-disk domain of titin is directly effected on the tenderization of meat during post-mortem aging and these change is due to manily calcium ions.