• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.5
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• pp.827-831
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• 1994

Investigation on the extractability, Mg2+-, Ca2+ , EDTA-ATPase activity and solubility of actomyosin prepared from leg and breast muscle of silky fowol were as follows. The extractability of actomyosin in leg and breast muscle was 779mg/100g and 1, 318mg/100g respectively, breast muscle was higher than leg muscle . Mg2+-ATPase activity of actomyosin was high inionic strength 0.02-0.10 and Mg2+ATPase activity of low ionic strength was higher than high ionic strength not related to the part. Ca2+ ATPase activity was high in ionic strength 0.05-0.13, the activity of leg muscle was higher that breast muscle. And EDTA-ATPase activity showed low in low ionic strength and showed high in high ionic strength, and increased greatly depend ionic strength up to 0.4. The solubility of actomyosin was not different in leg and breast muscle , the solution started in KCI concentration of 0.3M and ended in DCI concentration of 0.4M.

• Food Science of Animal Resources
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• v.23 no.3
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• pp.193-199
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• 2003

In order to investigate the meat tenderizing effects of pear, pineapple and kiwifruit, crude protease was prepared from each fruit and treated with actomyosin in a single manner or mixed type in several combination. Actomyosin was incubated with various proteases for 24 hrs under three different pH condition, and its degrading performance was evaluated by the SDS-PAGE. Pear extract showed an active degrading activity for actomyosin at pH 5.3 and 7.0. But, little actomyosin degradation was observed at pH 8.0. Actomyosin was strongly degraded by the treatment of protease from pineapple at all different pHs(5.3, 7.0 and 8.0). Kiwifruit protease extract has shown actomyosin degradation activity 1hr after treatment at pH 5.3 and pH 7.0. Meanwhile, the mixture of pear and pineapple extracts(l:l, w/w) showed much more degradation than the results of singular manner treatment at pH 5.3 and 7.0. When the pear protease was mixed with kiwifruit protease(l:l, w/w), the performance of actomyosin degradation was similar to the results of each single protease treatment. When the mixture was made of pineapple and kiwifruit extracts, actomyosin degradation was almost the same as the result of treatment of pineapple protease only. When those three proteases were mixed together(l:l:l, w/w/w), actomyosin degrading activities was in time dependent manner at pH 5.3. In summary, pear protease can be used potentially as a meat tenderizer when it was mixed with pineapple or kiwifruit rendering proper tenderization of the meat.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.4
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• pp.348-352
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• 1992

Investigation on the characteristics of actomyosin was prepared from leg and breast muscle of duck treated by hard scalding and subscalding method and their extractability , ATPase activity , solubility and SDS polyacrylamide gel electrophoresis were compared. The extractability of actomyosin in leg and breast muscle of duck by hard scalding was 7.84 and 39.84mg/g, whereas 4.79 and 28.04mg/g by subscalding respectively. Ca-ATPase activity of breast muscle wash higher than that of leg muscle. In case of leg muscle, hard scalding was higher tan subscalding. Breast muscle showed that subscalding was higher than hard scalding in less than ionic strength 0.08, and was lower than hard scalding in over ionic strength 0.08.Mg-ATPase was great in ionic strength and subcalding was relatively higher than hard scalding. Without regard to be treated method and part, the start point and end point of solubility were like. Hard scalded muscle and breast muscle showed that proteins in thin filament produced many extraction.

• Journal of Nutrition and Health
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• v.11 no.3
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• pp.37-42
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• 1978

Actomyosin and myofibril were extracted from Korean native Goat muscle with the Weber-Edsall solution. ATPase activities and physiochemical properties were measured. The results obtained were as follows; 1) Mg-activitied ATPase activity of actomyosin and myofibrill from Korean native Goat muscle exhibited a common biphasic response, a typical ATPase pattern, that is high at a low ionic strength and low at a high ionic strength. Actomyosin showed high activity than myofibrill. 2) Mg-activited ATPase activity of actomyosin from muscle increased extraction time 24 hours. 3) EDTA-enhanced ATPase activity of actomyosin was greater than myofibrill and low at the low ionic strength, high at the high ionic strength. The difference of the activity were shown great broad pattern at the after 0.3M KCI concentration. 4) Effect of EGTA on-ATPase activity of myofibrill and actomyosin from muscle was measured, the Mg-ATPase activity was markedly depressed. 5) Solubility of actomyosin from muscle began to solubilize at KCI concentration of 0.28M and solubilized completely at the KCI concentration of 0.3M.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.4
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• pp.349-355
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• 1990

Actomyosine prepared from Yellowtail fish(seriola quinqueradiata) were stored at $0^{\circ}C$(ice-cooling) -3.5$^{\circ}C$(partial freeaing) and -2$0^{\circ}C$(freezing) Another actomyosin samples were prepared from the fish previously stored at the temperatures for a week as the maximum .Remaining activity of {{{{ {Ca }^{2+ } }}}}-and {{{{ {Mg }^{2+ } }}}}- dependent adenosine triphosphatase(ATPase) activity was measured fronm the actomyosin preparations. Specific activity of {{{{ {Mg }^{2+ } }}}}-ATPase of actomy-osin before storagew was 0.253$\mu$ mole pi/min/mg of protein and it was 1.5 times higher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. The enzyme activities were markedly decreased during early period of storage. However no significant differences in the enzyme activity were revealed among the samples stored at different temperature. The enzyme of actomyosin prepared from the fish previously stored at the temperatures for a week revealed an acitivity of 2-3 times higher than that of freezing. Apparent denaturation constant of {{{{ {Mg }^{2+ } }}}} -ATPase of actomyosin was between 0.810-1.139 per day and it was about 1.5 times hgiher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. But the constant of {{{{ {Mg }^{2+ } }}}} ATPase of actomyosin extracted from the fist stored for a week at each temperature was between 0.176-0.356 per day. This constant was 4 times higher than that of {{{{ {Ca }^{2+ } }}}}- ATPase in frozen stored fish. It was presumed from these results that denaturation of ATPase is largely accorded to the structural changes of actomyosin.

• The Korean Journal of Physiology
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• v.11 no.2
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• pp.1-7
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• 1977

The activity of the $Ca^{++}$ activated adenosinetriphosphatase (Ca-ATPase) of actomyosin systeme of rabbit and frog skeletal muscle has been studied at varying pH and temperature. The PH optima of the Ca-ATPase activity of the rabbit actomyosin was rather broad. Over the temperature range of $16-36^{\circ}C$ activity of the enzyme was not appreciably changed between pH 6.4-8.5; below and above which it rapidly reduced. The pH at the inflection point of the enzyme activity increased as temperature decreased, showing the ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ of approximately $-0.018\;unit/^{\circ}C$. Consequently, $(OH^-)/(H^+)$ ratio at the inflection point was constant regardless of assay temperature. In the frog actomyosin systems the Ca-ATPase activity was not apparently altered between PH 6.4-7.0 when the incubation temperature was $15{\sim}30^{\circ}C$. Outside of this range of pH, however, the enzyme activity was dramatically decreased. The pH of the inflection point changed inversely with temperature. ${\bigtriangleup}pH\;inflection/{\bigtriangleup}T$ at the acidic side was approximately $-0.018\;unit/^{\circ}C$, whereas that at the alkaline side it was about $-0.037\;unit/^{\circ}C$. The Arrhenius Plot on the Ca-ATPase activity at constant $(OH^-)/(H^+)$ ratio of 1.0 was not linear, but showed break at arround $20^{\circ}C$ for both rabbit and frog actomyosin Preparations. From these results it was speculated that pH dependence of Ca-ATPase activity of rabbit actomyosin systems might reflect titrations of histidine-imidazole and -SH groups, and that of the frog actomyosin represents titrations of histidine-imidazole and lysyllysine ${\alpha}-NH_2$ groups.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.5 no.2
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• pp.57-62
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• 1972

Natural actomyosin was extracted from the dorsal muscle of carp (Cyprinus carpio), and some Physico-chemical properties were determined. The sedimentation constant ($s_{20},\;_\omega$) of the purified skeletal muscle actomyosin was about 24.76s and the ATP sensitivity 147-176. The specific viscosity was rapidly ascended with the increase of protein concentration as other vertebrate actomyosins. ATPase activating site under the effect of pH variation was showed on the both sides of acid and base resembling with the tendency of rabbit skeletal muscle actomyosin, and found at 6.0 on the acidic side and at 9.5 on the basic side.

• The Korean Journal of Food And Nutrition
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• v.10 no.2
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• pp.160-165
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• 1997

The actomyosin and myosin of the squid at 3$0^{\circ}C$ showed the highest Vmax and the actomyosin and myosin of the clam at 35$^{\circ}C$ and HMM at $25^{\circ}C$ showed the highest Vmax the thermostability of myofibrillar proteins is changed greatly according to the difference of KCI concentration. The myofibrillar proteins of the clam showed a higher thermostability than the myofibrillar proteins of the squid. When 3% ethanol solution was added and heated myofibrillar proteins, denaturation was accelerated and it was shown that there was a difference between animals in the denaturation velocity.

• Journal of the East Asian Society of Dietary Life
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• v.16 no.4
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• pp.453-457
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• 2006

This study investigated the extractability, solubility, Mg$^{2+}$-, Ca$^{2+}$- and EDTA-ATPase activity of actomyosin prepared from leg and breast muscle of dog meat. The actomyosin extractability of breast muscle(2,100.6 mg/l00 g) was higher than that of leg muscle(500.8 mg/l00 g). The Mg$^{2+}$-ATPase activity of actomyosin had a high ionic strength of 0.02$\sim$0.05 M KCI and did not differ between leg and breast muscle. The Ca$^{2+}$-ATPase activity of actomyosin had a high ionic strength of 0.02$\sim$0.10 M KCI and leg muscle had a higher level of Ca$^{2+}$-ATPase activity than breast muscle did. The EDTA-ATPase activity was lower in low ionic strength and showed higher in high ionic strength, and increased sharply with increasing ionic strength up to 0.3 M KCI. The solubility of actomyosin did not differ between leg and breast muscle, and the solubility started and ended at KCI concentrations of 0.35 M and 0.4 M, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.1
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• pp.77-81
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• 1985

It was investigated about extractability and biological property(ATPase activity) of actomyosin from skeletal muscle of chi(:ken differed feeding period. The extractabilities of actomyosin from pectoral muscle were increased from 184.5 to 1020.1 mg per 100g muscle as feeding period prolonged from 3 weeks to 8 weeks. In case of leg-muscles, extractability was revealed the similar tendency as pectoral muscles. EDTA ATPase activity of actomyosin in various chicken muscles for 3 weeks feeding was 0.6 Brmole Piimg Protein/min., 0.59 for 6 Iveeks feeding and 0.50 for 8 weeks. The Ma^{+2}$-ATPase of actomyosin in various chicken muscles was showed inverted relationship with ionic strength. EGTA ($125\;{\mu}mole$)inhibited Ma^{+2}$-ATPase activity to below $0.1\;{\mu}mole$ Pi/mg protein/min. regardless the feeding period.