• 생명과학회지
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• 제7권4호
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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.

• 한국식품영양과학회지
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• 제28권2호
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• pp.292-298
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• 1999

Myofibril and actomyosin were prepared from red muscle and white muscle of fresh water fish and sea water fish, and their biochemical characteristics and SDS PAGE patterns of myofibril were compared. SDS PAGE analysis showed that electrophoretic patterns of myofibril were similar be tween white muscle and red muscle, while difference of 30kDa component of myofibril was detected between fresh water fish and sea water fish. When myofibril were treated with trypsin, difference in hydrolysis of heavy chain was observed between white muscle and red muscle. In activities of Ca ATPase, Mg ATPase, EDTA ATPase and ATPase activity pH curve, myofibrillar protein from fresh water fish showed higher specific activity than those from sea water fish.

• 한국축산식품학회지
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• 제42권5호
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• pp.849-860
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• 2022

The myofibril protein (MP) isolate-saccharide graft reactions was prepared using the Maillard reaction with saccharides. The effects of various saccharides on protein functionality and quality of the Maillard reaction were investigated and compared with those of MP. The grafting degree of the MP isolate-saccharide graft reaction was significantly higher in the reducing sugar-treated groups (lactose, glucose, fructose, and palatinose). The browning intensity of the MP isolate-saccharide graft reaction with fructose, sucrose, and erythitol was higher than that observed in the control reaction (p<0.05). MP that reacted with reducing sugars (glucose, fructose, palatinose, and lactose) had fainter bands than MP that reacted with non-reducing sugars (sucrose, erythitol, trehalose, sorbitol, and xylitol). MPs conjugated with glucose exhibited higher protein solubility. The palatinose and lactose treatments were maximum in water binding capacity, though no significant difference in oil binding capacity among the saccharide treatments was observed. The emulsion stability of the MP isolate-saccharide graft reaction with palatinose and erythitol was higher than that of the control reaction. Therefore, reducing sugars have good protein functionality in the MP isolate-saccharides graft reaction.

• 한국식품영양과학회지
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• 제14권1호
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• pp.82-87
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• 1985

닭의 가슴부위 및 다리부위의 골격근(骨格筋)에서 myofibril, actomyosin 및 myosin을 추출하고 ATPase activity(${\mu}mole$ pi/mg protein/min)로서 나타낸 몇가지 생물학적(生物學的) 활성(活性)을 비교하였다. 가슴부위에서 추출한 actomyosin, myofibril 그리고 myosin의 $Mg^{+2}$-ATPase 활성(活性)은 0.05M KCl에서 0.80, 0.42, 0.40으로서 다리부위에서 추출한 단백질(蛋白質)의 활성(活性)인 0.69, 0.33, 0.28 보다 높았다. 가슴부위와 다리부위의 myosin의 ATPase 활성(活性)은 EDTA 농도보다 $Mg^{+2}$농도가 높아지면서 ATPase 활성(活性)을 1/10정도 저해(沮害)시켰고, $Ca^{+2}$ 농도는 $10^{-3}M$에서 400%까지 활성(活性)을 증가시켰다. 가슴부위와 다리부위에서 추출한 actomyosin의 용해되는 시점(始點)은 각각 0.1M KCl 및 0.15 M KCl이었고 myosin인 경우는 각각 0.25 M KCi 및 0.30 M KCl이었다.

• 한국식품과학회지
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• 제16권3호
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• pp.353-357
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• 1984

PSE돈육에서 근원섬유를 추출하고, 무수석시닐산으로 수식하여 석시닐화하고, 그 조제물의 화학적, 기능적 특성을 검토하였다. 석시닐화근원섬유는 석시닐화율에 상관없이 효소적 기능이 완전히 상실하였고, 무처리근원섬유의 등전점이 pH 5.0인데 비하여 석시닐화근원섬유는 pH 3.0정도에서 침전하였다. 염농도에 따른 용해도는 무처리근원섬유가 염농도의존성이 있음에 비하여 석시닐화근원섬유는 염농도에 관계없이 용해도의 변화가 거의 없었다. 석시닐화근원섬유의 기능적 특성중 열응고성은 현저히 감소하였고, 흡수성은 개선되지 않았으며, 유화용량은 다소 향상되었다.

• 생명과학회지
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• 제7권4호
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• pp.329-335
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• 1997

This study was conducted to investigate the effect of dietary fiber(DF) levels on the meat quality in colored broiler. Colored broiler were fed on containing corn-soy basal diet(DF 5%) and high level(DF 6,7 and 8%) of dietary fiber diets for 7 weeks. Dietary fiber level of diet was make up by adding some alffalfa meal. Colored broiler meats were stored at 3$\circ$ for 24hr after skaughter, and used to analyze physico-chemical properties. Proximate component, pH, shear force value, myofibril fragmentation index, water holding capacity, cooking loss, protein extractability, fatty acid composition, Hunter's L, a value and palatability of cooked meat were not significantly affected by dietary fiber levels, whereas the Hunter's value of meat was significantly affected bty dietary fiber levels for the final period of feeding. Crude protein content, myofibril fragmentation index, water holding capacity, protein extractability and Hunter's b value of breast meat's were higher than thigh meat's, but crude fat content, pH, shear force value, cooking loss, palmitoleic acid, linolenic acid, and Hunter's a value were lower, regardless of dietary fiber level.

• 한국축산식품학회지
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• 제27권4호
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• pp.457-462
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• 2007

본 연구에서는 노계 가슴육의 단백질 식품 소재로서 활용도를 높이기 위하여 초음파를 이용한 근원섬유 단백질의 수용화에 대하여 검토하였다. 근원섬유에 0.1-0.8 M NaCl, pH 6.0-8.0이 되도록 조절한 후 20 kHz에서 초음파 처리를 하였다. 그런 다음 이들의 용해도, SDS-PAGE, 점도, Ca- 및 Mg-ATPase 활성을 측정하였다. 각각의 처리 조건에서 용해도를 검토한 결과 초음파에 의해서 용해도는 증가하였으며 0.1 M NaCl, pH 8.0에서 약 90%를 나타내었다. 용해된 성분을 SDS-PAGE를 이용하여 검토한 결과 대부분 myosin heavy chain 및 actin에 상당하는 성분이 검출되었으며, 초음파에 의한 단백질의 분리는 근원 섬유 구조의 붕괴에 의한 것으로 사료되었다. 한편, 초음파에 의한 점도의 변화는 용해도가 높을수록 점도도 증가하였다. 그러나, Ca- 및 Mg-ATPase 활성은 초음파에 의해서 급격히 저하하였으며, 초음파에 의해서 분리되는 단백질은 대부분 변성이 진행된 상태인 것으로 사료되었다.

• 한국식품과학회지
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• 제6권4호
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• pp.199-208
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• 1974

근육의 수축 및 사후강직은 myosin 과 actin 그리고 ATP 와의 상호작용에 의한 것임은 널리 알려진 정설(定說)이다. 최근 myosin 과 actin 및 ATP 의 상호작용이 근조절단백질의 지배를 받고 Ca ion 이 관여하고 있다는 것이 알려졌다. 그런데 이들 조절단백질은 수용성단백질로써의 성질을 가지고 있음에도 불구하고 염용성단백질 구분에 들어 있다. 본 연구의 목적은 염용성단백질 구분에 들어 있는 이들 조절단백질의 새로운 분리정제방법을 연구하는 데 있었다. 이를 위하여 본 연구에서는 새로운 정제방법의 flow sheet 를 작성하였다. 이 제안된 새로운 정제방법은 근원섬유중의 조절단백질의 함량을 정량적으로 추적할 수 있는 장점을 가지고 있다는데 그 특색이 있다.

• 대한의생명과학회지
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• 제13권4호
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• pp.251-261
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• 2007

A myofiber of skeletal muscle is composed of myofibrils, sarcolemma (plasma membrane), and constameres, which anchor the myofibrils to the sarcolemma. Achvillin is a recently identified F-actin binding muscle protein, co-isolates with dystrophin and caveolin-3 in low-density sarcolemma of striated muscle, and colocalizes with dystrophin at costameres, the specialized adhesion sites in muscle. Archvillin also binds to nebulin and localizes at myofibrillar Z-discs, the lateral boundaries of the sarcomere in muscle. However other roles of archvillin on the dynamics of myofibrillogenesis remain to be defined. The goal of this study is, by using siRNA-mediated gene silencing technique, to investigate the effect of archvillin on the dynamics of myofibrillogenesis in cell culture of a mouse skeletal myogenic cell line (C2C12), where presumptive myoblasts withdraw from the cell cycle, fuse, undergo de novo myofibrillogenesis, and differentiate into mature myotubes. The roles of archvillin in the assembly and maintenance of myofibril and during the progression of myofibrillogenesis induced in skeletal myoblast following gene silencing in the cell culture were investigated. Fluorescence microscopy demonstrated that the distribution of archvillin was changed along the course of myofibril assembly with nebulin, vinculin and F-actin and then located at Z-lines with nebulin. Fluorescence microscopy demonstrated that knockdown of mouse archvillin expression led to an impaired assembly of new myofibrillar clusters and delayed fusion and myofibrillogenesis although the mouse archvillin siRNA did not affect those expressions of archvillin binding proteins, such as nebulin and F-actin. This result is corresponded with that of RT-PCR and western blots. When the perturbed archvillin was rescued by co-transfection with GFP or Red tagged human archvillin construct, the inhibited cell fusion and myotube formation was recovered. By using siRNA technique, archvillin was found to be involved in early stage of myofibrillogenesis. Therefore, the current data suggest the idea that archvillin plays critical roles on cell fusion and dynamic myofibril assembly.

• 한국식품과학회지
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• 제18권6호
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• pp.443-449
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• 1986

근원섬유구성단백질의 SDS-polyacrylamide gel 전기 영동상으로 부터 돼지근육의 red muscle과 while muscle의 근원섬유단백질사이에는 30K성분함량의 특징적 차이가 나타났으며, 생물활성에서도 red muscle쪽이 white muscle쪽보다 높은 ATPase 활성을 나타내었다. 근원섬유단핵질의 열안정성은 D값에서 확실한 차이를 보여 white muscle쪽이 red muscle쪽보다 높은 열안정성을 나타냈고, 열역학량에서도 근섬유 type간의 차이를 보였다. 한편 근원섬유단백질의 열안정성은 생체조직에 가까운 형태일수륵 안정하다는 사실도 확인되었다.