• 제목/요약/키워드: postmortem storage

검색결과 41건 처리시간 0.031초

The Influence of Vacuum Packaging of Hot-Boned Lamb at Early Postmortem Time on Meat Quality during Postmortem Chilled Storage

  • Zhao, Yingxin;Chen, Li;Bruce, Heather L.;Wang, Zhenyu;Roy, Bimol C.;Li, Xin;Zhang, Dequan;Yang, Wei;Hou, Chengli
    • 한국축산식품학회지
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    • 제42권5호
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    • pp.816-832
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    • 2022
  • To evaluate the effects of early postmortem vacuum packaging (VP) on meat quality during postmortem chilled storage, hot-boned lamb was vacuum-packaged at 1, 6, 12, 24, and 48 h postmortem and stored around 2℃ until 168 h postmortem, with lamb packaged in plastic wrap as the control (aerobic packaging). Intramuscular pH decline was delayed when lamb was vacuum packaged at 1, 6, and 12 h postmortem (p<0.05). The lamb vacuum-packaged at 1 h postmortem (VP-1h group) had significantly lower shear force values and purge losses accompanied by lower free thiol group values than other treatments during postmortem storage and was also higher in extractable calpain-1 activity by 6 h postmortem (p<0.05). Free thiol group concentrations were significantly higher after VP at 6 and 12 h postmortem (p<0.05). Packaging lamb under vacuum very early postmortem produced the lowest shear force and purge loss, likely by slowing heat loss and muscle temperature decline, implying that lamb quality is improved by VP when applied very early postmortem. This was at the expense of protein oxidation, which was unrelated to other meat quality measurements, most likely because potential contracture during hot boning confounded its impact. Further research is required to understand the implications of the interaction between protein oxidation, VP, and hot boning on the acceptability of lamb.

Postmortem skeletal muscle metabolism of farm animals approached with metabolomics

  • Susumu Muroya
    • Animal Bioscience
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    • 제36권2_spc호
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    • pp.374-384
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    • 2023
  • Skeletal muscle metabolism regulates homeostatic balance in animals. The metabolic impact persists even after farm animal skeletal muscle is converted to edible meat through postmortem rigor mortis and aging. Muscle metabolites resulting from animal growth and postmortem storage have a significant impact on meat quality, including flavor and color. Metabolomics studies of postmortem muscle aging have identified metabolisms that contain signatures inherent to muscle properties and the altered metabolites by physiological adaptation, with glycolysis as the pivotal metabolism in postmortem aging. Metabolomics has also played a role in mining relevant postmortem metabolisms and pathways, such as the citrate cycle and mitochondrial metabolism. This leads to a deeper understanding of the mechanisms underlying the generation of key compounds that are associated with meat quality. Genetic background, feeding strategy, and muscle type primarily determine skeletal muscle properties in live animals and affect post-mortem muscle metabolism. With comprehensive metabolite detection, metabolomics is also beneficial for exploring biomarker candidates that could be useful to monitor meat production and predict the quality traits. The present review focuses on advances in farm animal muscle metabolomics, especially postmortem muscle metabolism associated with genetic factors and muscle type.

Acetylation of Sarcoplasmic and Myofibrillar Proteins were Associated with Ovine Meat Quality Attributes at Early Postmortem

  • Zhang, Yejun;Li, Xin;Zhang, Dequan;Ren, Chi;Bai, Yuqiang;Ijaz, Muawuz;Wang, Xu;Zhao, Yingxin
    • 한국축산식품학회지
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    • 제41권4호
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    • pp.650-663
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    • 2021
  • The objective of this study was to examine the relationship between meat quality attributes and the changes of sarcoplasmic protein acetylation and myofibrillar protein acetylation in lamb longissimus thoracis et lumborum muscles at different postmortem phases. Protein acetylation, color, pH, shear force, myofibril fragmentation index and cooking loss were measured. The total level of acetylated sarcoplasmic proteins showed a negative relation with pH, a positive relation with a*, b* and cooking loss at the pre-rigor phase. Sarcoplasmic proteins acetylation affected postmortem pH by regulating glycolysis, which in turn affects color and cooking loss. The total level of acetylated myofibrillar proteins showed a positive relation with shear force at the pre-rigor phase. Myofibrillar proteins acetylation affected meat tenderness by regulating muscle contraction. This study indicated that acetylation played a regulatory role of meat color, water-holding capacity, and tenderization process at early postmortem.

Comparison of myofibrillar protein degradation, antioxidant profile, fatty acids, metmyoglobin reducing activity, physicochemical properties and sensory attributes of gluteus medius and infraspinatus muscles in goats

  • Adeyemi, Kazeem D.;Shittu, Rafiat M.;Sabow, Azad B.;Abubakar, Ahmed A.;Karim, Roselina;Karsani, Saiful A.;Sazili, Awis Q.
    • Journal of Animal Science and Technology
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    • 제58권6호
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    • pp.23.1-23.17
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    • 2016
  • Background: The functionality of myofibrillar proteins is a major factor influencing the quality attributes of muscle foods. Nonetheless, the relationships between muscle type and oxidative changes in chevon during ageing are meagrely elucidated. Postmortem changes in antioxidant status and physicochemical properties of glycolytic gluteus medius (GM) and oxidative infraspinatus (IS) muscles in goats were compared. Methods: Twenty Boer bucks (9-10 months old, body weight of $36.9{\pm}0.725kg$) were slaughtered and the carcasses were subjected to chill storage ($4{\pm}0.5^{\circ}C$). Analyses were conducted on GM and IS muscles sampled on 0, 1, 4 and 7 d postmortem. Results: Chill storage did not affect the antioxidant enzyme activities in both muscles. The IS had greater (P < 0.05) superoxide dismutase and catalase activities than GM. Carotenoid and tocopherol contents did not differ between muscles but decreased (P < 0.05) over storage. The IS had higher (P < 0.05) glycogen and ultimate pH and lower (P < 0.05) shear force and cooking loss than GM. The carbonyl content, % metmyoglobin, drip loss and TBARS increased (P <0.05) while free thiol, metmyoglobin reducing activity (MRA), shear force and myoglobin decreased (P < 0.05) over storage. Muscle type had no effect (P > 0.05) on free thiol, MRA and TBARS. The GM had lower (P < 0.05) redness on d 0 and 1 than IS while the IS had greater carbonyl, % metmyoglobin and drip loss than GM on d 7. The reflective density of slow myosin heavy chain (MHC) was higher (P < 0.05) while the density of fast MHC and actin was lower (P < 0.05) in IS than GM. Regardless of muscle type, the density of MHC decreased (P < 0.05) while that of actin was stable over storage. Nonetheless, the degradation of fast and slow MHC was greater (P < 0.05) in IS than GM. Muscle type had no effect (P > 0.05) on consumer preference for flavour, juiciness and overall acceptability. However, IS had higher (P < 0.05) tenderness score than GM on d 1 and 4 postmortem. Intramuscular fat was higher (P< 0.05) in IS compared with GM. Fatty acid composition did not differ between the muscles. However, GM had lower (P < 0.05) n-6/n-3 ratio than IS. The n-3 and n-6 PUFA declined (P < 0.05) while the SFA increased (P < 0.05) over storage. Conclusion: The changes in myofibrillar proteins and physicochemical properties of goat meat during postmortem chill storage are muscle-dependent.

저장기간에 따른 한국산 토종닭고기의 품질 특성 (Postmortem Changes in the Physico-Chemical Characteristics of Korean Native Chicken)

  • 성삼경;권연주;김대곤
    • 한국가금학회지
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    • 제25권2호
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    • pp.55-64
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    • 1998
  • This study was carried out to investigate the postmortem changes in physico-chemical characteristics of chicken meat with different breeds. Thigh and breast meats from Korean Native Chicken(KNC, 15-wk old), Wangchoo(15-wk old), and broiler(7-wk old) were stored at 5 ˚C. Differences in postmortem pH changes were not recognized among breeds, and pH showed by the lowest value at the 1st day of postmortem in all breeds. Breast meat had tendency to drop pH faster than thigh meat. Heme pigment contents showed no differences among breeds. KNC showed the lowest cholesterol contents in all breeds, total collagen contents showed the lowest value at the 1st day of postmortem, and thereafter it was gradually increased. Heat soluble collagen contents was lowest in Wangchoo. Water soluble and salt soluble protein showed the lowest extractability at the 1st day of storage. Broiler showed the highest extractability of these proteins and Wangchoo showed the lowest. Water holding capacity(WHC) had increasing tendency whilst cooking loss had decreasing tendency by the ageing. WHC of breast and thigh meat showed the highest values in KNC and broiler, respectively. Myofibrillar fragmentation index (MFI) was significantly increased in all breeds by the ageing. Breast and thigh meat showed almost same MFI in KNC and broiler, and in KNC and Wangchoo, respectively. Hardness of breast meat showed decreasing tendency by the ageing.

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Postmortem Proteolysis of Breast and Leg Muscles from Taiwan Colored Chickens and Silkie Bantams

  • Tsai, Shih-Fen;Lin, Chia-Ying;Lu, Jin-Jenn;Chou, Rong-Ghi R.
    • 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.

Comparison of Postmortem Proteolysis between Breast and Leg Muscles in Chiayi Native Chickens

  • Cha, Shih-Ting;Tseng, Tsai-Fuh;Ho, Sy-Shyan;Chou, Rong-Ghi R.
    • 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.

사후강직형태에 따른 근원섬유 단백질의 이화학적 성질변화 (Postmorten Changes in the Myofibrillar Proteins of Alkaline and Acid Rigor Rabbit Muscle during Storage)

  • 김대곤;성삼경
    • 한국식품영양과학회지
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    • 제21권6호
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    • pp.712-718
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    • 1992
  • 산 강직근과 알카리 강직근의 사후 자장중 물리, 화학적 변화를 비교 검토하였다. 근섬유의 소편화도는 산강직근이 알카리 강직근에 비하여 저장 3일째부터 월등히 높았다. $Mg^{2+}$-ATPase 활성은 알카리 강직근이 저장 전기간 동안 산 강직근 보다 높았으며, 산 강직근은 저장 1일째, 알카리 강직근은 저장 3일째에 가장 높았다. $Ca^{2+}$-ATPase 활성에 있어서 산 강직근과 알카리 강직근 모두 전 저장기간 동안 약간 증가하는 경향이었으나 산 강직근은 알카리 강직근 보다 전기간 동안 활성도가 낮았다. Actomyosin의 용해성이나 myofibril의 전기영동상은 강직 형태에 따른 유의한 차이가 없었다.

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Postmortem changes in physiochemical and sensory properties of red snow crab (Chionoecetes japonicus) leg muscle during freeze storage

  • Jun, Joon-Young;Jung, Min-Jeong;Kim, Dong-Soo;Jeong, In-Hak;Kim, Byoung-Mok
    • Fisheries and Aquatic Sciences
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    • 제20권7호
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    • pp.13.1-13.7
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    • 2017
  • In order to evaluate the maximal storable period of the raw crab for a non-thermal muscle separation, the quality changes of the leg meat of red snow crab (Chionoecetes japonicus) during freeze storage were investigated. Fresh red snow crabs were stored at $-20^{\circ}C$ for 7 weeks, and the leg muscle was separated by a no heating separation (NHS) method every week. During the storage, considerable loss of the leg muscle did not occur and microbiological risk was very low. In contrast, discoloration appeared at 2-week storage on around carapace and the leg muscle turned yellow at storage 3-week. In physiochemical parameters, protein and free amino acids gradually decreased with storage time, expected that proteolytic enzymes still activated at $-20^{\circ}C$. At 4-week storage, the sensory acceptance dropped down below point 4 as low as inedible and notable inflection points in pH and acidity were observed. The volatile base nitrogen was low, though a little increase was recorded. These results suggested that the maximal storable period at $-20^{\circ}C$ of the raw material was within 2 weeks and it was depended on external factor such as the discoloration. The present study might be referred as basic data for approaches to solve quality loss occurred in non-thermal muscle separation.

저장기간에 따라 추출된 쇠고기 Actomyosin의 생물활성 변화 (Changes in Actomyosin ATPase Activities Extracted from Beef Meet during Postmortem Storage)

  • 정인철;김미숙;강세주
    • 한국식품영양학회지
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    • 제10권3호
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    • pp.401-406
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    • 1997
  • 소의 도체로부터 사태, 갈비 및 등심을 분리하고 8$^{\circ}C$에 저장하면서 actomyosin을 추출하여 부위별 저장기간에 따라 추출성 및 ATPase활성을 비교하였다. Actin과 myosin이 유리되어 형성된 actomyosin의 추출성은 저장초기 사태, 갈비 및 등심이 각각 36.74, 72.55 및 56.77mg/g이었으며, 저장기간에 의한 추출양상은 갈비와 등심이 비슷하였고, 사태는 이들과 다르게 진행되었다. 사태의 Mg- 및 Ca-ATPase활성은 저장 3일까지 상승하다가 6일째 감소하였고, 갈비는 저장기간 동안 비슷하였으며, 등심은 저장기간에 따라 조금씩 낮아지는 경향이었다. 그리고 Mg- 및 Ca-ATPase활성은 사태, 등심 및 갈비의 순으로 크게 나타났다. 사태와 갈비의 EDTA-ATPase활성은 저장기간과 이온강도에 따라 차이를 보였지만 등심은 이온강도가 커짐에 따라 계속 상승하였다.

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