• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.3
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• pp.349-354
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• 1997

Myotibrillar ATPase activity, thermostability and composition of muscle protein were investigated to elucidate biochemical properties regard with rearing period and sex of olive flounder. Myofibrillar ATPase activity of male olive flounder reared for 6, 12 and 20 months was stronger than that of female one. $Mg^{2+}\;(+Ca^{2+})-ATPase$ activity of both female and male fish decreased with the elapse of rearing period, and the activity of male was higher than that of female far beyond the rearing periods. The high correlationship between the weight gain and myofibrillar ATPase activity was observed. The thor mostability of male myofibrillar protein was higher than that of female. Subunit composition of the myofibrillar and sarcoplasmic protein did not show difference between the both sex of the fish.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.226-233
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• 1986

Myofibrillar proteins were prepared from red muscle and white muscle, and their thermostabilities were compared. Rate constants of inactivation of myofibrillar proteins were increased as the ionic strength of reaction mixture increased and also dielectric constant of reaction mixture decreased. Thermodynamic data forinactivation of myofibrillar proteins, such as $D-value,\;{\Delta}H^{\ddag},\;{\Delta}G{\ddag}\;and\;{\Delta}S^{\ddag$, revealed that thermostabilities of myofibrillar proteins from white muscle were higher than those from red muscle, and that myofibrillar proteins from chicken muscle were more heatlabile than from bovine muscle.

• Korean Journal of Food Science and Technology
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• v.25 no.3
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• pp.295-298
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• 1993

This study was carried out to investigate the effects of heating temperature, heating time and protein concentration on the gel properties and heat stability of a mixed system of pork plasma and myofibrillar to increase the utility of porcine blood as protein resources of the food industry, especially meat processing industry. The solubility of plasma protein and mixture (plasma + myofibrillar protein) decreased significantly at $70^{\circ}C\;to\;90^{\circ}C$ when heating temperature rised, whereas myofibrillar protein decreased slightly at $40^{\circ}C\;to\;60^{\circ}C$, and the gel strength and the turbidity of those increased significantly at these heating temperatures. The solubility of plasma protein and mixture decreased when the heating time increased at $75^{\circ}C$, whereas the gel strength and turbidity increased, and the solubility, the gel strength and the turbidity of myofibrillar protein showed no changes.

• Journal of Korean Biological Nursing Science
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• v.13 no.1
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• pp.1-7
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• 2011

Purpose: The purpose of this study was to compare the hypertrophic effects of low-intensity exercise on weight, myofibrillar protein content and Type I, II fiber cross-sectional area of hindlimb muscles of rats between every other day exercise and every day exercise. Methods: Adult male Sprague-Dawley rats were assigned to 1 of 3 groups: control group (C, n=6), experimental group 1 (E1, n=7) and experimental group 2 (E2, n=7). Rats in E1 group had 7 sessions (every other day) and those in E2 group had 14 sessions (every day) of exercise in which they ran on a treadmill for 30 min/day at 10 m/min. Results: Muscle weight, cross-sectional area of type I fiber and myofibrillar protein content of soleus and myofibrillar protein content of plantaris in E1 group, and myofibrillar protein content of soleus and cross-sectional area of type I fiber of plantaris in E2 group were greater than those in C group. Cross-sectional area of type I fiber of soleus of E1 group was higher than E2 group while cross-sectional area of type I fiber of plantaris of E2 group was higher than E1 group. Conclusion: Hypertrophy of hindlimb muscles occurs from every other day exercise similar to every day exercise.

• Proceedings of the Korea Society of Poultry Science Conference
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• 2006.11a
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• pp.69-72
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• 2006

To investigate the manufacturing methods of surimi-like materials (SLM) from breast muscle of spent hen, the muscles were diced, chopped and washed with distilled water or sodium chloride solution at 0.1, 0.5 and 1% level and then washed with distilled water to extract myofibrillar protein. When used only distilled water to extract myofibrillar protein, washing was repeated 3 times followed by homogenization and centrifugation of breast muscle after each washing (CM; conventional method). Whereas, to extract myofibrillar protein using sodium chloride solution had sufficient to do 2 times washing by distilled water after 1 time washing by sodium chloride followed by homogenization and centrifugation of breast muscle after each washing (NM; new method). The both batter and cooked SLM gel from NM had significantly (p<0.05) lower redness compared with CM. Again, SDS-PAGE with sarcoplasmic protein fractions showed that the bands of phosphorylase had increased staining intensity in NM compared with CM. These results indicated that the brightness was related to sarcoplasmic protein fractions. SDS-PAGE with myofibrillar protein showed that the bands of myosin had increased staining intensity in NM compared with CM. Data implied that myofibrillar protein extraction with sodium chloride solution had the better adaptability for the breast muscle of spent hen then the commonly used distilled water method.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.28 no.5
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• pp.557-568
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• 1995

Proteolytic properties of enzymes from the muscle and viscera of anchovy have been examined. Cathepsin L, chymotrypsin, and trypsin showed similar Km values for casein. However, they had higher Km values for myofibrillar proteins than those for casein. The $k_cat$ of cathepsin L and chymotrypsin for myofibrillar proteins were higher than that of trypsin, and also cathepsin L and chymotrypsin caused higher hydrolysis in myofibrillar proteins of anchovy and yellowtail. In the presence of sodium chloride$(0-25\%)$, proteolytic activity for myofibrillar proteins from yellowtail was higher than that for casein. Proteolytic activity was decreased with the increase of sodium chloride concentration. Cathepsin L had been less affected by NaCl concentration and temperature on the hydrolysis of myofibrillar proteins than chymotrypsin and trypsin. Cathepsin L and chymotrypsin were move responsible to the autolysis of muscle proteins from fish than trypsin.

• Food Science of Animal Resources
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• v.34 no.3
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• pp.307-315
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• 2014

pH adjustment would be of advantage in improving the water holding capacity of muscle proteins. The objective of this study was to evaluate the addition of fish sarcoplasmic protein (SP) solution, which was adjusted to pH 3.0 or 12.0, neutralized to pH 7.0, and lyophilized to obtain the acid- and alkaline-treated SP samples, on the functional properties of the chicken myofibrillar protein induced by microbial transglutaminase (MTG). The solubility of alkaline-treated SP was higher than that of the acid counterpart; however, those values of the two pH-treated samples were lower than that of normal SP (p<0.05). All SP solutions were mixed with myofibrillar proteins (MP) extracted from chicken breast, and incubated with MTG. The shear stresses of MP with acid- and alkaline-treated SP were higher than that of normal SP. The thermal stability of MP mixture reduced upon adding SP, regardless of the pH treatment. The breaking force of MP gels with acid-treated SP increased more than those of alkaline-treated SP, while normal SP showed the highest value. The MP gel lightness increased, but cooking loss reduced, with the addition of SP. Smooth microstructure of the gel surface was observed. These results indicated that adjusting the pH of SP improved the water holding capacity of chicken myofibrillar proteins induced by MTG.

• Journal of the Korean Society of Food Science and Nutrition
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• v.9 no.1
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• pp.45-50
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• 1980

Myofibrilar Protein from Korean Duck Muscle was extracted and ATPase activities were studied. The results were as follows: 1. Mg-activated ATPase activity of Myofibril from Korean Duck, muscle exhibited a biphasic response, ATPase activity was high at a low ionic strength and low activity was showed at high ionic strength. 2. Effect of EDTA on the Myofibrillar protein ATPase activity was studied, it was investigated that the EDTA inhibition was showed at the concentration of $6.9{\mu}g$ and it above. 3. It showed that the effect of Ca++ on ATPase activity was decreased at the lower than $3{\mu}g$. Inhibition showed at the concentration of $6.9{\mu}g$ and it above. 4. It showed that the effect of Mg++ on ATPase activity was decreased at the lower than $3.6{\mu}g$. Inhibition showed at the concentration of $3.9{\mu}g$ and it above.

• Korean Journal of Food Science and Technology
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• v.26 no.2
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• pp.110-116
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• 1994

In order to study the effects of enzyme modification on the physico-chemical and functional properties of myofibrillar protein prepared from the frozen sardine, Sardinops melanostica, the protein was hydrolyzed with pepsin under the enzyme-substrate ratio 1:100 at $37^{\circ}C$ and pH 1.65 for 1, 4, 8, 12, and 24 hr, respectively. The properties of pepsin-modified sardine myofibriliar protein were determined. The extents of proteolysis with pepsin as a fuction of time was showed a typical enzyme hydorlysis curve with an initial region of 4 hour period followed by plateau region. The SDS-acrylamide slab gel electrophoresis patterns of pepsin-modified proteins showed mainly disappearances of minor protein bands, but no changes of main protein bands. The gel filtration patterns through Sephadex G-75 of sardine myofibrillar protein showed two big peaks and three small peaks. All the small peaks were disappearanced by proteolysis with pepsin in one hour. and during the period of proteolysis the fast big peak became gradually smaller and the late big peak eluted more slowly. By proteolysis, the emulsifying activity and emulsifying capacity of sardine myofibrillar protein were all decreased. The effects of pepsin-modification on emulsifying capacity were greater than those on emulsifying activity of protein. The aeration capacity of the protein was increased about 1.9 folds and the foam stability decreased to 0.6 folds of control by pepsin-modification. The pepsin-modified sardine myofibrillar proteins showed about 0.6 folds of heat coagulation and 1.4 folds of viscosity of control. The pH dependence of solubilities of sardine myofibrillar protein showed two isoelectric areas of pH 5 and 9. The pepsin-modified protein showed more clear pH dependences at the early stage but not at the late stage of proteolysis.

• Food Science of Animal Resources
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• v.30 no.5
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• pp.746-754
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• 2010

Response surface methodology was adopted to model and optimize the effects of microbial transglutaminase (TG) and calcium alginate (CA) systems of various ratios on the gelation characteristics of porcine myofibrillar protein (MP) at various salt levels. The CA system consisting of sodium alginate (SA), calcium carbonate (CC) and glucono-$\delta$-lactone (GdL) showed no remarkable changes in the salt-soluble fraction, and only minor effects on electrostatic interactions were observed. Increasing CA concentration caused acid-induced hydrophobic interactions in MPs, resulting in increased MP gel strength. The TG system, containing TG and sodium caseinate (SC), induced cold-set MP gelation by formation of covalent bonding. The main advantage of the combined system was a higher cooking yield when the MP gel was heated. These results indicated that 0.7% TG combined with 0.8% CA system can form a viscoelastic MP gel, regardless of salt levels.