• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.19 no.4
• /
• pp.333-338
• /
• 1986

Compositions of protein and amino acid in the muscle of crucian carp, Carassius carassius, and snakehead, Channa argus, were determined by amino acid autoanalyzer, and the protein subunits composed of sarcoplasmic and myofibrillar proteins were also analyzed by sodium dodecylsulfate (SDS) polyacrylamide gel electrophoresis. The crucian carp muscle contained about $14.7\%$ of protein, and the protein was composed of $32.6\%$ in sarcoplasmic, $62.0\%$ in myofibrillar, $4.9%$ in alkali soluble and $0.6\%$ in stroma protein. The snakehead muscle, on the other hand, contained about $16.1\%$ of protein, and $30.7\%,\;64.1\%,\;4.7\%\;and\;0.4\%$ in the above order. The sarcoplasmic and myofibrillar proteins were composed of 10 and 19 subunits respectively, in the crucian carp, and 12 and 18 subunits in the snakehead. The total amino acid compositions in the muscle of the crucian carp and snakehead were found to be very similar except lysine and glutamic acid. The major amino acids of their muscle protein were lysine, glutamic acid, arginine and aspartic acid in order. In free amino acid content of the crucian carp, histidine occupied $52\%$ of the total free amino acid, and glutamic acid, glycine and taurine did $85\%$ in case of snakehead.

• Food Science of Animal Resources
• /
• v.31 no.5
• /
• pp.782-790
• /
• 2011

The effects of soy protein isolate (SPI) and red bean protein isolate (RBPI) on gelling properties of pork myofibrillar protein (MP) in the presence of microbial transglutaminase (MTG) were studied at 0.45 M NaCl. MP paste was incubated with MTG (0.1%) at various levels (0.1, 0.3, 0.5, and 1%) of SPI and RBPI before incubating at $4^{\circ}C$ for 4 h. The rheological property results showed that MP gel shear stress increased with increasing RBPI concentration. Cooking yield (CY) of the MP gel increased with increasing RBPI and SPI, whereas gel strength (GS) was not affected by adding RBPI or SPI. Thus, effects of incubation time (0, 4, 8, 10, and 12 h) were measured at 0.1% SPI and RBPI. GS values of the MP gel at 10 and 12 h were similar and were higher than those of the others. CY values were highest when RBPI (0.1%) was added, regardless of incubation time. The protein patterns indicated that incubating the MP with MTG for 10 h resulted in protein crosslinking between MP and RBPI or SPI. Based on these results, RBPI and SPI could be used as an ingredient to increase textural properties and cooking yield of meat protein gel.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.19 no.1
• /
• pp.60-66
• /
• 1986

The muscles of wild and cultured eel, Anguilla japonica, were analyzed for the protein composition and amino acid profile. The differences of the subunit distribution for the sarcoplasmic and myofibrillar proteins were discussed with sodium dodecylsulfate(SDS) polyacryamide gel electrophoresis. The muscle protein in wild eel was composed of $30.78\%$ of sarcoplasmic, $59.02\%$ of myofibrillar, $9.73\%$ of residual intracellular and $2.47\%$ of stroma fraction. That in cultured eel was composed of $31.81\%,\;58.37\%,\;8.16\%\;and\;1.80%$, respectively, The sarcoplasmic and myofibrillar proteins were composed of 16 and 14 subunits in wild eel, and 22 and 15 subunts in cured eel. The sarcoplasmic protein between wild and cultured muscles showed a similar trend in the subunits, except a few subunits such as 36,500, 46,000, 58,500, 75,000, 170,000 and 235,000 daltons in cultured eel. Only the existence of 45,000 dalton subunit was the difference between wild and cultured eel in myofibrillar protein. The distribution patterns of total amino acid in muscles of wild and cultured eel were found to be very similar trend, although glycine content in wild eel was slightly higher than that in cultured one.

• Korean Journal of Food Science and Technology
• /
• v.9 no.4
• /
• pp.295-305
• /
• 1977

The procedures for the Preparation of regulatory proteins of myofibrill were developed and postmortem changes in the regulatory proteins of myofibrill were investigated. Both the physiological property and molecular shape of ${\alpha}-actinin$ from pre-rigor muscle did not differ from those of ${\alpha}-actinin$ from post-rigor muscle. On the other hand, although tropomyosin of myofibril changed negligibly during the post-mortem storage of muscle, troponin of myofibril changed remarkably.

• The Korean Journal of Food And Nutrition
• /
• v.16 no.3
• /
• pp.209-217
• /
• 2003

The composition of muscle proteins and free amino acids in the mudskipper (hibernant fish) were investigated before and after hibernation (maturity period: August, hibernation period: November thru. April). It was found that crude proteins were 17.6% in August, 17.5% in November and 16.9% in April, while among the muscle proteins, sarcoplasmic proteins were constituted up to 19.2～20.4%, 58.8～61.3% for myofibrilla proteins, 11.2～13.2% for intracellular proteins and 7.5～8.3% for stroma proteins. Composition changes of the muscle proteins were hardly noted until November but during the hibernation(from Nov. to Apr.) the amount of the sarcoplasmic proteins and the myofibrillar proteins decreased pronouncedly. As for the sarcoplasmic proteins, 14 subunits were found and among them, the amount of 30 kDa and 46 kDa subunits were found to increase slightly in April compared with those in November, while the amount of 35 kDa and 65 kDa subunits were decreased slightly. As for the myofibrilla proteins, 13 subunits were found and detectable changes in their composition were not observed until November but in April the amount of myosin heavy chain was increased by 3%, while the amount of actin decreased by 3% when those are compared with the results in November. The composition of amino acids in the muscle proteins was hardly changed during the observation period. But there were considerable changes of composition of free amino acids. Glycine and alanine were found to be the major free amino acids. The most striking feature was the changes in the glycine and arginine content: the former, which is a dominant free amino acid, was increased by two-fold in April compared with that in August and the latter was increased by two-fold in November and by four-fold in April. It was also found that the amount of essential amino acids (i.e., lysine and histidine) and others (alanine, glutamic acid, serine, aspartic acid and valine) increased significantly during the hibernation period.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
• /
• 2003.06a
• /
• pp.95-117
• /
• 2003

본 연구는 한우육의 육질등급과 저장기간에 따른 육질 및 저장특성과 맛성분의 차이를 조사하고자 실시하였으며, 도축 24시간 후 도체등급판정을 실시한 한우 36두의 등심부위를 시료로 취하여 $2^{\circ}C$ 냉장실에서 14일간 저장하면서 이화학적 특성 및 관능적 특성을 조사하였다. 그 결과를 요약하면 다음과 같다. 육질등급에 따른 도체 특성에 있어서 등급간의 지방두께, 배최장근 단면적 및 육량등급은 차이가 없었으며, 육색과 지방색, 성숙도 등도 차이가 없는 것으로 나타났으나 조직감은 1등급육이 3등급육에 비하여 좋은 것으로 나타났다. 1등급육은 3등급육에 비하여 지방함량(9.87${\pm}$2.23%)이 높았으며, 수분함량(67.75${\pm}$l.63%)이 낮았으나(p<0.05), 단백질함량은 육질등급간에 차이가 없었다. 도축 24시간후의 L, b, h-값은 등급간에 차이가 없었으며, a와 C-값은 2등급육이 다른 등급에 비하여 다소 높게 나타났다. L, a, b-값 모두 저장기간이 경과함에 따라 다소 증가하였다. pH는 육질등급간에 차이가 없었으며 저장기간에 따른 차이도 없었다. 1등급육은 3등급육에 비하여 드립감량은 다소 낮은 것으로 나타났으며, 가열감량은 등급간에 유의적인 차이는 없었으나 1등급육이 가장 적은 가열감량을 나타냈다. 보수력은 1등급육이 2, 3등급육에 비하여 유의적으로 높았으며, 근절길이와 콜라겐 함량은 등급간에 차이가 없었다. 전단력값은 3등급육이 1, 2등급육에 비하여 다소 높은 전단력값을 보였으나 유의적인 차이는 없으며, 근원섬유 소편화도는 등급간에 차이가 없었다. 저장기간이 경과합에 따라 전단력값은 점차적으로 낮아졌고 근원섬유 소편화도는 유의적으로 증가하였다. 1등급육이 2, 3등급육에 비하여 TBA가가 높았고, VBN함량은 낮았으나 유의적인 차이는 없었으며, 저장기간이 경과함에 따라 TBA가와 VBN함량은 증가하였다. 관능평가에서 풍미는 육질 등급간에 차이가 없었으나, 연도, 다즙성 및 전체적인 기호도는 1등급육이 3등급육에 비하여 다소 우수한 것으로 나타났다.

• Journal of Life Science
• /
• v.17 no.5 s.85
• /
• pp.728-734
• /
• 2007

In this study, we prepared surimi from pork leg and chicken breast by pH adjustments of 3.0 and 11.0. The content of crude protein, yield, water-holding capacity, redness, yellowness, myoglobin(Mb) and metmyoglobin(metMb) were significantly higher in the surimi manufactured from pork leg at adjustment pH 3.0 compared to the other surimi samples; whereas whiteness, myofibrillar protein, breaking force, deformation and gel strength were lower than other samples(P<0.05). The textural attributes were significantly higher in the surimi manufactured from pork leg at adjustment pH 11.0 compared to the other surimi samples; whereas Mb, metMb, cooking loss, breaking force, deformation and gel strength were lower than other samples(P<0.05). Again, the content of crude protein, yield, pH, breaking force, deformation, gel strength and lightness were significantly higher in the surimi manufactured from chicken breast at adjustment pH 3.0 compared to the other surimi samples; whereas myofibrillar protein, redness and metMb were higher than other samples(P<0.05). The content of myofibrillar protein, deformation, lightness and cohesiveness were significantly higher in the suriml manufactured from chicken breast at adjustment pH 11.0 compared to the other surimi samples; whereas Mb, cooking loss, yield and breaking force were higher than other samples(P<0.05). The chicken breast surimi had superior color and gel characteristics than manufactured from pork leg, and adjustment pH 11.0 had superior whiteness and cohesiveness than the pH 3.0 adjusted sample, however, there were no significant differences in sensory attributes among the surimi samples.

• Korean Journal of Food Science and Technology
• /
• v.18 no.6
• /
• pp.443-449
• /
• 1986

In order to investigate the general characteristics of ATPase and ATPase thermostability between porcine white muscle and red muscle, myofibrillar proteins were prepared and compared their physicochemical characteristics. SDS-polyacrylamide gel electrophoretic analyses showed that a protein band of 30,000 daltons was detected noticeably in myofibril from red muscle, but negligibly in myofibril from white muscle. The noticeable differences were found between porcine white muscle and red muscle for the activities of EDTA-ATPase, Ca-ATPase and Mg-ATPase. Myofibrillar proteins from white muscle showed higher thermostability than those from red muscle. Thermodynamic parameters, enthalpy $({\Delta}H^#)$, entropy $({\Delta}S^#)$, etc., showed characteristic variations between porcine white muscle and red muscle.

• Journal of Korean Academy of Nursing
• /
• v.27 no.1
• /
• pp.96-108
• /
• 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.

• Food Science of Animal Resources
• /
• v.25 no.4
• /
• pp.423-429
• /
• 2005

Properties of pant surimi derived from porcine longissimus muscle were investigated Rapid glycolysis of muscle reduced yield $\%$ of water-washed pork and moisture $\%$ of pent surimi because of ie lower ultimate pH. Gel Hardness was significantly (p<0.05) higher in pork surimi from rapid glycolysis muscle, but springiness was higher (p<0.05) in pork surimi from normal glycolysis muscle. SDS-PAGE pattern showed denaturation of sarcoplasmic proteins onto myofibrillar proteins in rapid glycolysis muscle, resulted in dark color and hard texture of pork surimi. Color and texture of gels were related with water-holding capacity of muscle proteins and moisture $\%$ in gel matrix. Results imply that glycolysis rate of porcine muscle at postmortem could affect gel properties of pork surimi, and muscle with rapid glycolysis muscle could produce a hard texture of pork surimi and dark color.