• Korean Journal of Food Science and Technology
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• v.29 no.3
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• pp.395-399
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• 1997

Meat model emulsions ware prepared with salt-soluble protein and soybean oil. Effects of water-soluble protein (WSP) on the meat model emulsion treated with/without BHT during 8 day storage $5^{\circ}C$ under both dark and light illumination were studied by measuring POV and TBA. An emulsion without BHA and WSP was used as a control. Under light storage, there was no significant difference in peroxide values between the control and the sample treated with BHA except the 2nd day of storage. However, TBA values of the sample treated with BHA were significantly (p<0.05) lower than those of control except the 4th day of storage. TBA and POV of the samples treated with WSP and WSP + BHA were higher than control after 4th day of storage under light. That is, water soluble protein, which was composed mainly of myoglobin, increased lipid oxidation under light storage. The similar trends were also shown in the samples stored under dark. These results suggested that acceleration of lipid oxidation of the meat model emulsions by water soluble protein (WSP) under both light and dark might not be due to the singlet oxygen formation, but due to superoxide anion formed.

• 한국전기화학회:학술대회논문집
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• 2005.07a
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• pp.115-122
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• 2005

• Korean Journal of Food Science and Technology
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• v.9 no.2
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• pp.153-156
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• 1977

We have investigated for amino acid composition and molecular weight of the sunflower main protein which was purfied by Sephadex column. The results were obtained as fellow. 1. The salt-soluble sunflower proteins were highly dispersible in 0.02M sodium phosphate buffer, containing 10% sodium chloride. 2. The sunflower proteins were characterized by comparatively high levels of essential amino acids. 3. Seven bands of component of sunflower proteins were found in disc electrophoretic gel column. 4. The sunflower main protein was purified by Sephadex G-150 and A-25 column chromatography 5. The molecular weight was estimated 86,000 for the sunflower main protein.

• 한국전산유체공학회:학술대회논문집
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• 2009.11a
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• pp.8-12
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• 2009

In this study the performance of the nozzle of a rocket system is evaluated using a CFD code. The main emphasis of the investigation is placed on the effects of the number (9 and 12) and the depth of fluted edge in the rocket nozzle. It is observed that as the depth increases the rolling moment of the nozzle increases while the thrust of the nozzle decreases.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.05a
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• pp.246-249
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• 2004

겔 강도와 경도는 사후강직 후 근육이 강직 전 근육에 비해 단단한 것으로 나타났지만, 수분결합력과 관능적인 탄력성을 고려해볼 때 사후강직 전 근육이 더 훌륭한 겔 형성력을 보였다. 따라서 돈육을 이용한 수리미유사물 제조시 사후강직 전 근육을 이용하는 것이 바람직할 것으로 사료되었는데, 사후강직 전 근육은 염용성단백질 추출성과 수분결합력이 다른 상태의 근육에 비해 높게 나타났기 때문이다.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.18 no.5
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• pp.401-408
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• 1985

In order to develop new types of product which can offer a sanitary and preservative duality, and convenience to consumers in marketing and cooking particularly in urban area, two processing methods of ready-to-cook food materials with dark fleshed fishes like sardine and mackerel were investigated. A method applied, in this work, is processing of ready-to-cook sardine meat "surimi" in which sardine meat is treated with alkaline solution to stabilize myofibrillar proteins, washed thoroughly with water to remove soluble components, and added with a proper amount of polyphosphate and sorbitol to enforce the functional property of meat such as water holding capasity, elasticity, and gel strength. The textural properties of fish meat paste made from the "surimi" meat were greatly dependent upon the stability of myofibrillar proteins and the elimination of water soluble components. The salt soluble proteins of sardine meat were so unstable in post-mortem stage that the gel forming ability was lost within 3 days at $5^{\circ}C$ storage and 2 to 3 weeks even at $-20^{\circ}C$ although the freshness was well kept for a week at $5^{\circ}C$ and several months of storage at $-20^{\circ}C$. A proper way of treatment to keep the proteins stable was that fish meat must be washed with $0.4\%$ sodium bicarbonate solution followed by 3 to 4 times washing with water. This resulted in removal of $80\%$ water soluble proteins and 50 to $60\%$ lipids. The addition of polyphosphate and sorbitol affected the stability of proteins during the storage of "surimi" meat. When phosphate and sorbitol were added in the ratio of $0.3\%:\;0.3\%,\;0.6\%:\;3\%,\;0.6\%:\;6\%,\;0:\,0.3\%\;and\;0.3\%:\;0$, the gel forming ability terminated in 35 days, 21 days, 14 days, 14 days, and 14 days of storage at $-30^{\circ}C$, respectively, while that of the control was 7 days. And it was also noteworthy that at least 8.0 mg/g of salt soluble protein nitrogen content was required for gel formation.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.21 no.3
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• pp.177-183
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• 1988

The Present study has been carried out to investigate the effect of refrigerated seawater (RSW) at $-1^{\circ}C$ in order to delay spoilage and extend the shelf-life in Sardine(Sardinops melanosticta). The result obtained are summarized as follows : In case of freshness, K-value was shown above $30\%$ at 1 day of storage by icing, but in RSW system was shown $20\%$ until 2 days by storage. VBN and TMA were also shown the similar tendency when compared to K-value. The lipids extracted from sardine muscle held in ice was oxidized much more than those in RSW system by way of chemical test such as TBA and POV. The myofibrillar protein extracted from sardine stored in RSW system was denaturized more slowly compared with those by ice. $Ca^{2+}-ATPase$ activity indicated that myofibrillar protein held in RSW system was more stable than those held in ice. Total viable counts for sardine in RSW system showed an overall lower values. By TPA(Textural Porfile Analysis) , sardine meat pastes held in RSW system have a higher value than those held in ice.

• Korean Journal of Food Science and Technology
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• v.20 no.3
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• pp.447-452
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• 1988

In order to study effect of freezing rates on the quality changes such as pH, TBA value, free fatty acids and protein extractability, cylindrical chopped beef logs with 10cm of diameter and 10cm of height were frozen at three freezing rates(0.97cm/hr, 2.05cm/hr, 3.71cm/hr)using air blast freezer. Physicochemical changes of frozen meat were investigated during forzen storage at $-20^{\circ}C$ for 16weeks. Results on pH change showed $0.1{\sim}0.2unit$ increase at the 16th week of the frozen storage and the change was smaller with the increasing freezing rates. Free fatty acids content and TBA value also were increased during forzen storage, but they were minimal at 3.71cm/hr freezing rate. Correlation coefficient between TBA value and free fatty acids content were highly significant(r=0.804). After 16weeks of storage, extractibilities of salt soluble protein were decreased by 17.7%, 6.1% and 1.6% at freezing rates of 0.97, 2.05 and 3.71cm/hr, respectively. On the other hand, extractabilities of water soluble protein were decreased by 26.0%, 21.2% and 18.5%, respectively. The effect of freezing rates on the protein extractability appeared to be greater in salt soluble protein than in water soluble protein, but freezing denaturation was more rapid in water soluble protein.

• Korean Journal of Food Science and Technology
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• v.23 no.5
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• pp.532-537
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• 1991

Effect of storage temperature fluctuation on quality of frozen breaded raw shrimp was studied. Storage experiments were undertaken as follows; First, after storage at $-20^{\circ}C$ for 20 days or 40 days, storage temperature of materials were raised to $-15^{\circ}C\;or\;15^{\circ}C$, and then stored at these temperatures, And second, by repeating for 5, 10 and 15 times by 3 conditions ($-20{\rightarrow}-15^{\circ}C{\rightarrow}-20^{\circ}C,\;-20{\rightarrow}-10^{\circ}C{\rightarrow}-20^{\circ}C\;-20{\rightarrow}-5^{\circ}C{\rightarrow}-20^{\circ}C$) with temperature fluctuation during storage. Quality changes were measured by determining extractability of salt-soluble protein, volatile basic nitrogen, thiobar-bituric acid, pH and microbiological changes at regular intervals. Rise in storage temperature from $-20^{\circ}C\;to\;-15^{\circ}C$ had not caused significant change on it's quality, but rise up to $-5^{\circ}C$ caused some change in quality without relationship with storage period before temperature rise. Fluctuation of storage temperature from $-20^{\circ}C\;to\;-15^{\circ}C$ of frozen breaded raw shrimp did not cause noticeable changes on it's quality. But temperature fluctuation from $-20^{\circ}C\;to\;-10^{\circ}C\;or\;-5^{\circ}C$ caused remarkable changes of it's quality, according to the increase of fluctuation times and temperatures.

• Korean Journal of Food Science and Technology
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• v.6 no.4
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• pp.199-208
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• 1974

An attempt was made to study on new method for the extraction of the regulatory proteins from myofibrils, and the procedures for the preparation of desensitized actomyosin and for complete extraction of troponin-tropomyosin complex were developed. When myofibrils were treated through the procedures developed in this study, actomyosin obtained had no Ca-sensitivity, indicating that Ca-sensitizing protein factor had been removed completely from myofibril. Consequently, it was concluded that the procedures developed in this study were convenient to test whether Ca-sensitizing proteins has been removed or not. When Mg-activated ATPase activity of myofibril were measured, the myofibrillar ATPase turned into the actomyosin type ATPase with the progress of the treatment. This result was interpreted to show that the regulatory proteins of the myofibril seems to play a cementing role on the structure of myofibril. When supernatant containing the regulatory proteins were fractionated with $(NH_4)_2SO_4$ saturation solution, regulatory proteins, ${\alpha}-actinin$ and troponia-tropomyosin complex, could be obtained and they showed their typical phyoislogical activity which modify the actin-myosin interaction. The amount of troponin-tropomyosin complex in myofibril was 72 mg per g myofibril. This result was in good agreement with the results reported by many investigators, and therefore it was concluded that our procedures for the extraction of troponin-tropomyosin complex were desirable to study on the quantitative analysis of troponin-tropomyosin complex.