• 제목/요약/키워드: myofibrillar

검색결과 229건 처리시간 0.023초

담수어와 해수어의 근원섬유단백질의 특성 비교 (Comparison of Biochemical Characteristics of Myofibrillar Protein from Fresh Water Fish and Sea Water Fish)

  • 신완철;송재철;홍상필;김영호
    • 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.

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Tetramethylpyrazine Protects Oxidative Stability and Gelation Property of Rabbit Myofibrillar Proteins

  • Wang, Jianping;Liu, Ning;Zhang, Feike
    • 한국축산식품학회지
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    • 제39권4호
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    • pp.623-631
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    • 2019
  • Tetramethylpyrazine (TMP), an alkaloid rich in Ligusticum wallichii and fermented products, possesses multiple pharmacological activities in antioxidant, antiinflammatory, and antibacterial. This study aimed to investigate the effect of TMP (15 mg/L) on the physicochemical and gelation properties of rabbit myofibrillar proteins (MPs) with/without oxidative stress. Results showed that compared to the control, oxidative stress to MPs decreased free thiol content, gel yield, whiteness, water-holding capacity, bounder water, immobilized water, and endogenous tryptophan fluorescence intensity, but increased surface hydrophobicity, dityrosine content, and free water content (p<0.01). Without oxidative stress, MPs treated with TMP increased free thiol content, whiteness, and bound water, but decreased dityrosine content and free water (p<0.05). Under oxidative conditions, all parameters were conversely affected by TMP (p<0.01). The results suggest that TMP can be an antioxidant to decrease the concern on oxidative deterioration during meat processing and storage by improving the oxidative stability, water retention, and gel forming property of rabbit MPs.

근위축 발생전의 지구력 운동이 쥐의 위축뒷다리근의 질량, 근원섬유 단백질 함량 및 근섬유 단면적에 미치는 영향 (Effect of Endurance Exercise Prior to Occurrence of Muscle Atrophy on the Mass, Myofibrillar Protein Content and Fiber Crossectional Area of Atrophied Hindlimb Muscles of Rats)

  • 최명애
    • 대한간호학회지
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    • 제27권1호
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    • pp.96-108
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    • 1997
  • The purpose of this study was to determine the effect of endurance training prior to occurrence of muscle atrophy on the mass, myofibrillar protein content and fiber crossectional area of atrophied hindlimb muscles of rats. Adult female Wistar rats were trained prior to occurrence of muscle atrophy induced by hindlimb suspension. Training began on the 1st day for 10min /day at 15m /min on a 0% grade, training exercise increased daily in time and intensity so that by the 4th week rats were running 60min /day, at 34m /min on a i3.5% grade. Wet weight and relative weight of soleus, plantaris and gastrocnemius muscle decreased significantly after seven days of hindlimb suspension. Wet weight and relative weight of soleus tended to increase and that of plantaris and gastrocnemius tended to decrease in the exercise group as compared to the control group. Myofibrillar protein content of soleus and gastrocnemius tended to increase and that of plantaris tended to decrease in the endurance trained group as compared to the control group. Fiber crossectional area of Type I, II fiber in soleus and plantaris muscle tended to increase in the exercise group as compared to the control group. Wet weight and relative weight of soleus. plantaris and gastrocnemius decreased significantly, myofibrillar protein content of soleus, plantaris and gastrocnemius increased in hindlimb suspended rats following endurance training as compared to the control group. There was no change in fiber type percentage and crossectional area of type I and II fiber in soleus muscle and that of type I and IIfiber in plantaris muscle decreased in the hindlimb suspended rats following endurance training as compared to the control group. Wet weight and relative weight of soleus and plantaris tended to increase, that of gastrocnemius increased significantly, myofibrillar protein content of soleus and plantaris muscle increased significantly and that of gastrocnemius tended to increase in the hindlimb suspended rats following endurance training as compared to sedentary rats following endurance training. Crossectional area of type I fiber of soleus muscle tended to increase. that of type I fiber of plantaris muscle increased significantly and that of type II fiber tended to increase in hindlimb suspended rats following endurance training as compared to sedentary rats following endurance training. The results suggest that endurance training prior to occurrence of muscle atrophy can attenuate the decrease of mass, myofibrillar protein content and fiber crossectional area induced by hindlimb suspension.

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산란노계육(産卵老鷄肉)의 냉장 및 동결저장 중 물리화학적 특성 변화 (Changes in the Physicochemical Properties of Spent-hen Meat during Cold and Frozen Storage)

  • 공양숙;문윤희
    • 한국식품영양과학회지
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    • 제16권3호
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    • pp.55-61
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    • 1987
  • 산란노계육(産卵老鷄肉)(Arbor Acres, 72주령(週齡))의 가슴근육과 다리근육을 냉장 및 동결저장하면서 pH, 단백질의 추출성, 근원섬유단백질의 ATPase 활성, 소편화, 냉동감량 및 드립량의 변화를 비교하였다. 가슴근육과 다리근육의 pH는 각각 냉장 1일 및 동결저장 1주에 가장 낮았다. 근원섬유단백질의 추출성은 냉장기간이 경과하면서 점차 증가하였으며, 동결저장에서는 1주에 가장 높은 수준을 보였다. 근원섬유단백질의 $Mg^{2+}-ATPase$활성은 냉장 1일 및 동결저장 1주에 각각 높게 나타났다. 근원섬유의 소편화 정도는 냉장 1일 및 동결저장 1주에 크게 변화하였으며 냉동감량과 드립량은 동결저장 기간이 경과하면서 점차 많아졌다. 냉장 및 동결저장 중 가슴근육은 다리근육에 비하여 pH가 낮았고, 근원섬유단백질의 추출성, $Mg^{2+}-ATPase$활성, 드립량 및 소편화 정도가 높았으나 저장기간 중 변화되는 양상은 비슷하였다.

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명태 근육단백질의 아세틸화에 따른 기능성의 변화 (Acetylation of Fist Protein form Alaska Pollack)

  • 홍정화;최진호;변대석
    • 한국식품영양과학회지
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    • 제19권3호
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    • pp.219-223
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    • 1990
  • Myofibrillar protein from Alaska pollack was modified with acetic anhydride at pH 7.5 and $25^{\circ}C$ and changes in functional properties as affected by the degree of modification were determined. Acetylation of myofibrillar protein resulted in protein with unique functional properties dependent upon the degree of acetylation. By selecting appropriate degree of modification it was possible to control protein solubility heat coagulability calcium precipitability foaming and emulsion capa-city.

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간접면역형광법(間接免疫螢光法)을 이용(利用)한 숙성중(熟成中) 식육(食肉)의 연화정도(軟化定度) 측정(測定) (Measurement of Meat Tenderization during Post-mortem Aging by the Indirect Immunofluorescence Method)

  • 안동현
    • 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.

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Porcine Myofibrillar Protein에 대한 비교생화학적 연구 (Comparative Biochemical Study on the Myofibrillar Proteins from Porcine Muscle)

  • 양융;박현주;김영호;진홍승;신완철
    • 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.

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스테로이드치료 전 운동이 스테로이드 치료에 의해 유발된 쥐의 위축 Type I, II 뒷다리근육에 미치는 효과 (Effects of Exercise before Steroid Treatment on Type I and Type II Hindlimb Muscles in a Rat Model)

  • 최명애;안경주
    • 대한간호학회지
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    • 제37권1호
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    • pp.81-90
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    • 2007
  • Purpose: The purpose of this study was to examine the effects of daily exercise before steroid treatment on mass, the type I and II fiber cross-sectional area, and myofibrillar protein content of hindlimb muscles in a rat model. Method: Adult male Sprague-Dawley rats were randomly assigned to one of three groups: a control group(n=10) that had a normal saline injection for 7days, a steroid group(n=10) that had a steroid injection for 7days, and an exercise-steroid group(n=10) that ran on the treadmill for 7days before a steroid treatment. Body weight and food intake were measured every day. At 15 days all rats were anesthetized and the soleus, plantaris and gastrocnemius muscles were dissected. Result: The exercise-steroid group showed significant increases as compared with the steroid group in body weight, muscle weight of the soleus and gastrocnemius, type II muscle fiber cross-sectional area of plantaris, and myofibrillar protein content of the soleus, plantaris, and gastrocnemius. As compared with the control group, the steroid group showed significant decreases in body weight and diet intake, muscle weight, the type II fiber cross-sectional area and myofibrillar protein content of the soleus, plantaris, and gastrocnemius muscles. Conclusion: Daily exercise before steroid treatment attenuates hindlimb muscle atrophy, with type II muscle changes more apparent than type I muscle changes.

Leucocyte lysosomal proteinase에 의한 닭의 근섬유(筋纖維) 단백질(蛋白質) 분해(分解)에 미치는 NaCl과 pH의 영향(影響) (Influence of NaCl and pH on Hydrolysis of Chicken Myofibrillar Proteins by Leukocyte Lysosomal Proteinases)

  • 신승이;이종욱
    • 한국식품과학회지
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    • 제22권5호
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    • pp.569-574
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    • 1990
  • 닭의 근섬유(筋纖維) 단백질(蛋白質) 돼지의 백혈구(白血球)에서 추출(抽出)한 lysosomal proteinase에 의해서 분해(分解)될 때 미치는 NaCl과 pH의 영향(影響)에 대해서 연구(硏究)하였다. Leucocyte lysosomal proteinase에 의한 근섬유(筋纖維) 단백질(蛋白質)의 분해(分解)는 다른 pH를 갖는 Tris-maleate buffer에서 partial hydrolysis로 진행(進行)하였다. 분해(分解)는 높은 pH에서 더욱 심화(深化)되었으며, 여기에 NaCl이 첨가(添加)되었을 때 proteinase의 activity는 pH의 고저(高低)에 관계(關係)없이 더욱 증가(增加)함을 보여주었다.

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Optimisation of Calcium Alginate and Microbial Transglutaminase Systems to form a Porcine Myofibrillar Protein Gel

  • Hong, Geun-Pyo;Chin, Koo-Bok
    • 한국축산식품학회지
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    • 제29권5호
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    • pp.590-598
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    • 2009
  • The aim of this study was to model and optimize the calcium alginate (CA) and microbial transglutaminase (TG) systems to form a cold-set myofibrillar protein (MP) gel containing 0.1 M or 0.3 M NaCl using a response surface methodology. The gel strengths of cold-set and heat-induced MP gels, and cooking yields were measured. All measured parameters showed determination coefficients ($R^2$) above 0.7 without a lack-of-fit. The CA system had the best results with component ratios of 1.0:0.3:1.0 corresponding to sodium alginate, calcium carbonate and glucono-$\delta$-lactone, respectively, and was favourable at 0.1 M NaCl. In contrast, the TG system only had an effect on cold-set MP gelation at 0.3 M salt, and the optimal ratio of TG to sodium caseinate was 0.6:0.5. By combining the two systems at 0.3 M NaCl, an acceptable cold-set MP gel with an improved texture and high cooking yield could be formed. Therefore, these results indicated that the functionality of the cold-set MP gel could be enhanced by combining these two optimized gelling system.