• Asian-Australasian Journal of Animal Sciences
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• 제19권5호
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• pp.739-743
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• 2006

Postmortem proteolysis of breast (BM) and leg (LM) muscles from Taiwan colored chickens (TCC) and silkie bantams (SB) at $5^{\circ}C$ were compared. Myofibrils were prepared from BM and LM samples that were randomly taken from the carcasses of SB and TCC after 0, 1, 3, 7 and 14 days of storage at $5^{\circ}C$. pH of samples was determined, and degradation of myofibrillar proteins was analyzed by the SDS-PAGE and western blots. The results showed that pH was lower in BM than in LM samples from both avian strains. Appearance of 30 kDa components and disappearance of titin and nebulin 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 might suggest that postmortem proteolysis occurred more rapidly in BM than in LM from both TCC and SB.

• Asian-Australasian Journal of Animal Sciences
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• 제15권5호
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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.

• Asian-Australasian Journal of Animal Sciences
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• 제17권9호
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• pp.1296-1302
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• 2004

This study was conducted to evaluate the possible application of 2 D-SDS-PAGE (2 DE)-based proteome analysis techniques to the assessment of extreme proteolysis in postmortem skeletal muscle. Eight Hanwoo longissimus muscles were incubated immediately after slaughter for 24 h at 5$^{\circ}C$, 15$^{\circ}C$ or 36$^{\circ}C$. Warner Bratzler (WB)-shear force and ultrastructural configuration were determined at 24 h, and rate of proteolysis to 24 h was determined by 1 D-SDS-PAGE (1 DE) and 2 DE. In addition, tentative protein identification was performed from peptide mass fingerprints of MALDI-ToF analysis of major protein groups on 2 DE profiles. The result showed that although ultrastructural configuration was similar between the 5$^{\circ}C$ and 36$^{\circ}C$ treatments, meat at 5$^{\circ}C$ had higher WBshear force (approximately 5 kg greater). A higher rate of protein degradation at 36$^{\circ}C$ was observed based on Troponin-T degradation, 1 DE, and 2 DE analysis. This indicates that proteolysis during the early postmortem period was a significant determinant of shear force at 24 h. Little difference in proteolysis between 5$^{\circ}C$ and 15$^{\circ}C$ treatments was found based on classic 1 DE profile assessment. Meanwhile, considerable differences in the 2 DE profiles between the two treatments were revealed, with substantially higher rate of proteolysis at 15$^{\circ}C$ compared to 5$^{\circ}C$. Nuclease treatment improved 2 DE profile resolution. 400 ${\mu}$g and 600 ${\mu}$g of sample loading appeared to be appropriate for 24 cm pH 3-10 and pH 5-7 IPG strips, respectively. Protein detection and quantification of the 5$^{\circ}C$, 15$^{\circ}C$ and 36$^{\circ}C$ 2 DE profiles revealed 78, 163 and 232 protein spots respectively that were differentially modified in terms of their electrophoretic properties between approximately pI 5.3-7.7 with the molecular weight range of approximately 71-12 kDa. The current results demonstrated that 2 DE was a superior tool to 1 DE for characterising proteolysis in postmortem skeletal muscle.

• 한국축산식품학회지
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• 제42권5호
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• pp.723-743
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• 2022

Beef muscles from mature cows and bulls, especially those originating from the extremities of the carcass, are considered as underutilized due to unsatisfactory palatability. However, beef from culled animals comprises a substantial proportion of the total slaughter in the US and globally. Modern consumers typically favor cuts suitable for fast, dry-heat cookery, thereby creating challenges for the industry to market inherently tough muscles. In general, cull cow beef would be categorized as having a lower extent of postmortem proteolysis compared to youthful carcasses, coupled with a high amount of background toughness. The extent of cross-linking and resulting insolubility of intramuscular connective tissues typically serves as the limiting factor for tenderness development of mature beef. Thus, numerous post-harvest strategies have been developed to improve the quality and palatability attributes, often aimed at overcoming deficiencies in tenderness through enhancing the degradation of myofibrillar and stromal proteins or physically disrupting the tissue structure. The aim of this review is to highlight existing and recent innovations in the field that have been demonstrated as effective to enhance the tenderness and palatability traits of mature beef during the chilling and postmortem aging processes, as well as the use of physical interventions and enhancement.

• Journal of Animal Science and Technology
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• 제65권6호
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• pp.1151-1168
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• 2023

Tenderness and taste characteristics of meat are the key determinants of the meat choices of consumers. This review summarizes the contemporary research on the molecular mechanisms by which postmortem aging of meat improves the tenderness and taste characteristics. The fundamental mechanism by which postmortem aging improves the tenderness of meat involves the operation of the calpain system due to apoptosis, resulting in proteolytic enzyme-induced degradation of cytoskeletal myofibrillar proteins. The improvement of taste characteristics by postmortem aging is mainly explained by the increase in the content of taste-related peptides, free amino acids, and nucleotides produced by increased hydrolysis activity. This review improves our understanding of the published research on tenderness and taste characteristics of meat and provides insights to improve these attributes of meat through postmortem aging.

• 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.

• 한국수산과학회지
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• 제9권2호
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• pp.120-128
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• 1976

백색 육어류의 사후 기간중에 일어나는 단백질 분해의 본질을 규명하려는 방도로써 가자미류(English sole, Paraphyrus vetulus)와 볼락류(rockfish, sebastodes caurinus)의 어육을 시료로 하여 맨 먼저 가자미 전 어체를 빙장하는 동안 취하여 어육 slurry를 만든 후 $20^{\circ}C$에서 유지시키는 동안의 단백질 분해율을 측정하였다. 근육자가 소화효소 cathepsin에 의한 단백질 분해도를 규명키 위하며 어육 slurry 일부는 0.5Mrad 감마선조사로써 무균화시키면서 세균 면식활동에서 오는 단백질 분해가능성을 제거시켰다. 어육을 기계적으로 분쇄하여 얻은 slurry를 무균화한 후 $20^{\circ}C$ 수조에서 17시간 동만 유지시켰는데도 불구하고 단백질 분해가 전혀 검측되지 안했음은 cathepsin 작용이 없었음을 뜻한다. 이와 반면에 비조사구 slurry의 경우, $20^{\circ}C$ 수조에서의 유지기간중 총함수의 증가에 따라 약간의 단백질 분해가 이뤄줬으나 slurry로 만들어지기전의 어체의 부패도가 후기에 접어 들어 총균수가 최고선에 도달하였을 때 비로소 현저한 단백질 분해를 가져 왔다. 이는 부패초기에는 부패세균에 의한 단백질 분해효소의 합성이 거의 없음을 시사한다. 이어서 볼락어육을 무균적으로 취하여 그 일부는 단백질 분해력이 강한 Pseudomonad균을 접종하고, 나머지는 각각 0, 0.5, 그리고 2.0Mrad의 감마선에 조사한 후 $0^{\circ}\~2^{\circ}C$에서의 저장기간중에 일어나는 단백질 분해과정을 규명하였다. 세균번식이 없는 무균어육의 염용선(0.5M KCl) 총질소질과 $70\%$ 에타놀 용해성 아미노태 질소량은 저장기간중 약간 감소된 반면 Pseudomonad군을 접종한 어육의 질소질의 증가는 총균수 증가에 평행하였다. 이로써 어류의 사후 기간중에 일어나는 단백질 분해는 정상적인 어류부패과정의 일부분이기는 하나 부착세균의 번식이 진행되어 총균수가 최고선에 도달할 때까지 단백질 분해는 지연되며 최소한 백색 어육에 관한한 사후기간중 cathepsin에 의한 단백질 분해에의 기여도는 거의 무시될 수 있음이 확인되었다.

• Journal of Animal Science and Technology
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• 제48권6호
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• pp.921-932
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• 2006

쇠고기 연도 조절에 대한 연구는 오랜 역사를 가지고 있으나, 균일한 쇠고기 맛에 대한 소비자들의 요구 증가로 응용적 연구가 가속화 되고 있다. 도축 후 근절길이와 단백질 분해가 연도에 큰 영향을 미친다는 사실은 잘 밝혀졌다. 전기자극은 맛 보증 프로그램을 위해서 여러 나라에서 산업적으로 이용되고 있다. 전기자극이 연도를 향상(또는 질겨짐 감소)시키는 기전은 모두 밝혀지지 않았으나, 이 처리가 저온 단축을 막고 사후 강직을 단축시켜 단백질 분해를 증가시킨다는 결과는 명확해 보인다. 한편 Tenderstretch는 사후 강직기 동안 근섬유와 결체 조직에 장력을 가하여 고기의 질겨짐을 줄이는 작용을 하는 것으로 보인다. 선행 연구들은 도축 후 전기자극과 Tenderstretch 처리가 지방이 많은 가축과 냉각 온도가 느린 조건에서도 연도를 향상 시킨다는 사실들을 증명하였다. 최근 연구에 의하면 한국 소비자들도 연도가 쇠고기 맛을 결정하는데 중요한 요인이며, 국내 연구결과에 의하면 도축 후 전기자극 또는 tenderstretch 처리가 한우의 연도 및 육색을 증가시키는 것으로 나타났다. 특히 이 기법들은 도체의 크기 및 지방 침착도와 도축 후 냉각속도 조절이 어려운 국내 축산업 조건에서 연도의 균일성 및 개선을 보장할 수 있는 중요한 기법으로 판단되나, 국내 산업체에서는 이용되지 않고 있다. 이 논문은 이러한 기법에 대한 현재의 이론과 국내 쇠고기 산업에 주는 의미를 서술했다.

• 대한수의학회지
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• 제55권3호
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• pp.175-179
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• 2015

Proteases play important roles in parasite development and host parasite interactions. The protease of Kudoa spp. has been recognized as a key factor of severe proteolysis of fish muscle post-mortem; however, there is little information available regarding the protease of Kudoa (K.) septempunctata, which was recently identified as a cause of food poisoning in humans. The present study was conducted to isolate and characterize proteases to elucidate the type of protease contained in the parasite and determine the optimal pH for protease activity. We confirmed the cysteine protease and metalloprotease produced by K. septempunctata. While the cysteine protease showed optimal activity at pH 5 that decreased rapidly with increasing pH, the optimal activity of metalloprotease was pH 7, and it remained stable from pH 6 to pH 8. These results indicate that the pH of cysteine protease is not proper for fish muscle postmortem, and that metalloprotease can act in human intestines. Overall, the present study provides important information that improves our understanding of the role of protease physiology and the subsequent food poisoning caused by K. septempunctata.