• 한국축산식품학회지
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• 제41권4호
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• pp.589-607
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• 2021

Meat proteolytic systems play a crucial role in meat tenderisation. Understanding the effects of processing technologies and post-mortem storage conditions on these systems is important due to their crucial role in determining the quality characteristics of meat and meat products. It has recently been proposed that tenderisation occurs due to the synergistic action of numerous endogenous proteolytic systems. There is strong evidence suggesting the importance of μ-calpain during the initial post-mortem aging phase, while m-calpain may have a role during long-term aging. The caspase proteolytic system is also a candidate for cell degradation in the initial stages of conversion of muscle to meat. The role of cathepsins, which are found in the lysosomes, in post-mortem aging is controversial. Lysosomes need to be ruptured, through aging, or other forms of processing to release cathepsins into the cytosol for participation in proteolysis. A combination of optimum storage conditions along with suitable processing may accelerate protease activity within meat, which can potentially lead to improved meat tenderness. Processing technologies such as high pressure, ultrasound, and shockwave processing have been reported to disrupt muscle structure, which can facilitate proteolysis and potentially enhance the aging process. This paper reviews the recent literature on the impacts of processing technologies along with post-mortem storage conditions on the activities of endogenous proteases in meat. The information provided in the review may be helpful in selecting optimum post-mortem meat storage and processing conditions to achieve improved muscle tenderness within shorter aging and cooking times.

• 식품보건융합연구
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• 제4권3호
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• pp.12-21
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• 2018

This research was conducted at agric physical lab, Department of Animal science, Faculty of Agriculture to determines the effects of marinating spent layer meat with basil leaf paste on drip loss and sensory attributes under different post mortem conditions. In the light of this, the poultry industry is obliged to continuously grow for a steady supply of quality poultry meat. Marinating the spent layer hen's meat with fresh basil leaves (Ocimum basilicum) in addition to subjecting the meat to 0, 6, 12, and at 24 hours post mortem aging before cooking increased it's organoleptic attributes which was readily acceptable to consumers. Marination of meat with herbs or spices like basil leaves paste had enhanced consumer's preference for taste, texture aroma, colour and overall acceptance. Marination improved consumer acceptance of spent layer meat irrespective of parts and post mortem aging. However, the majority of the respondents preferred meat marinated and subjected to 12 hours of post mortem aging. It is recommended that more quantity of marinate should be added further studies should in order to determine more effect of fresh basil leaves rough paste. And more hours of postmortem aging should be increased in order to determine more effect of fresh basil leaves rough paste marinate.

• Asian-Australasian Journal of Animal Sciences
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• 제26권3호
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• pp.443-454
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• 2013

Tenderness is the most important meat quality trait, which is determined by intracellular environment and extracellular matrix. Particularly, specific protein degradation and protein modification can disrupt the architecture and integrity of muscle cells so that improves the meat tenderness. Endogenous proteolytic systems are responsible for modifying proteinases as well as the meat tenderization. Abundant evidence has testified that calpains (CAPNs) including calpain I (CAPN1) and calpastatin (CAST) have the closest relationship with tenderness in livestock. They are involved in a wide range of physiological processes including muscle growth and differentiation, pathological conditions and post-mortem meat aging. Whereas, Calpain3 (CAPN3) has been established as an important activating enzyme specifically expressed in livestock's skeletal muscle, but its role in domestic animals meat tenderization remains controversial. In this review, we summarize the role of CAPN1, calpain II (CAPN2) and CAST in post-mortem meat tenderization, and analyse the relationship between CAPN3 and tenderness in domestic animals. Besides, the possible mechanism affecting post-mortem meat aging and improving meat tenderization, and current possible causes responsible for divergence (whether CAPN3 contributes to animal meat tenderization or not) are inferred. Only the possible mechanism of CAPN3 in meat tenderization has been confirmed, while its exact role still needs to be studied further.

• 한국식품과학회지
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• 제28권3호
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• pp.566-572
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• 1996

본 연구에서는 숙성 중 야기되는 식육의 인화정도를 파악할 수 있는 척도로서 이용하기 위하여, 근원섬유 Z선의 구성단백질의 하나인 zeugmatin에 대한 항체를 조제, 간접연역형광법으로 zeugmatin의 숙성중 변화와 근원섬유의 소편화와의 관계를 알아 보았다. Zeugmatin은 변성하기 쉬운 단백질로서 재래식 방법으로는 정제가 블가능하므로 이 단백질을 함유하는 획분을 정제과정 중에 채취하여 전기영동으로 전개, 이에 해당하는 band를 분리하여 polyclonal항체를 용이하게 받을 수 있었으며, 이 조제된 항체는 zeugmatin과 특이적으로 반응하였다. 조제된 항체를 이용하여 간접면역형광법으로 식육의 숙성중에 zeugmatin의 변화와 근원섬유의 소편화로 나타나는 식육의 연화와의 상관관계를 알아 본 결과, 이 두가지 변화는 특이적으로 일치하였다 즉, 닭의 흉근을 $4^{\circ}C$에서 숙성하면서 측정한 근원섬유의 소편화도는 도살 후 6시간에서 24시간 사이에 급속히 증가하여 이 시간대에 식육이 급속히 부드러워짐을 나타내었고, zeugmatin에 대한 항체가 나타내는 형광광도도 도살 후 6시간에서 24시간 사이의 동일한 시간대에 급적히 약화되어 zeugmatin이 이 시간대에 급속히 인화하였음을 나타내었다. 이상의 결과로 근원섬유 Z선의 구성단백질 중 하나인 zeugmatin은 숙성에 따라 야기되는 식육의 연화정도, 즉 식육의 숙성도를 나타내는 척도로서 이용될수 있으며, 그 이용방법으로는 간접면역형광법이 가장 간편한 방법인 것으로 판단되었다.

• 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.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• 제22권2호
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• pp.282-288
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• 2009

The present paper describes the effects of pressure and post-mortem aging treatments on in situ proteasome activity in rabbit and bovine skeletal muscles. Synthetic peptide hydrolyzing activity of rabbit proteasomes remained in the muscle after exposure to pressures up to 100 MPa. However, when a pressure of 400 MPa or more was applied, proteasomes were markedly inactivated. The extraction of proteasomes from excessively pressurized muscle appeared to be difficult. Proteasomes in aged muscle remained relatively stable throughout the aging process, with activity after 168 h (7 days) being 35%, 48%, 53% and 31% of the 0 h post-mortem LLVY, LSTR, AAF and LLE total hydrolyzing activities, respectively. The synthetic peptide hydrolyzing activities of bovine muscle proteasomes were similar to those of rabbit skeletal muscle proteasomes. The results suggest that synthetic peptide hydrolyzing activity remains in muscle exposed to relatively low pressures. Furthermore, it is known that high-pressure treatment induces fragmentation of myofibrils, modification of actin-myosin interaction and activation of intramuscular proteinases, cathepsins and calpains. Thus, proteasomes are probably involved in the tenderization process in combination with other intramuscular proteinases under high-pressure conditions. Our findings confirmed that proteasomes play a role in meat tenderization induced by high-pressure treatment or aging.

• 한국축산식품학회지
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• 제39권3호
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• pp.474-493
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• 2019

The aim of the study was to evaluate the effect of an early post-mortem low voltage electrical stimulation (ES) to localized part of carcasses [m. longissimus lumborum (LL) and m. biceps femoris (BF)] and determined the tenderness and flavor compounds of Hanwoo steers (n=16). Carcasses were stimulated within 30 min post-mortem for 60s using 60 volts and muscles aged 2 and 14 d. Degradation of Troponin-T were accelerated by ES and degraded little faster in BF muscle than LL. Level of free amino acid content of stimulated and aged muscles was significantly (p<0.05) greater than control for both muscles. Totally 63 volatile compounds were identified by using SPME-GC. The ES treatment significantly (p<0.05) affected the level of 20 volatile compounds of LL as well 15 volatiles in BF muscle along with total amounts of ketones, sulfur containing, pyrazines and furans. Low voltage ES could be applied to reduce the aging time and improve volatile flavor development by increasing important desirable volatile compounds such as 2-methylpyrazine, 2,5-dimethylpyrazines and 2-acetylthiazole etc. due to released free amino acids from protein degradation.

• 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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• 제36권2호
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• pp.159-169
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• 2016

Animal muscles are stored for specific period (aging) at refrigerated temperatures, during and after which the living muscles start to convert into meat and thus, attain certain superior properties in the final product. Proteolysis, lipolysis, and oxidation are the major biochemical processes involved during the postmortem aging of meat that affect the tenderness, juiciness, and flavor, as well as sometimes may introduce certain undesirable traits. This review analyzes the role of pre- and post-mortem factors that are important for aging and their effect on the chemical and physical changes in the “dry- and wet-aged meat.” Thus, if the meat processing manufacturers optimize the effects of aging for specific muscles, the palatability, color, and the shelf life of the aged meat products could be significantly enhanced.