• Ocean and Polar Research
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• v.36 no.1
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• pp.39-47
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• 2014

The black scraper Thamnaconus modestus was a commercially important fish species in the 1980s, but suddenly its commercial significance decreased in the 1990s mainly due to continuous overfishing. Recently, in order to reverse the depleted stocks of the black scraper and help the species recover, seed production technology has emerged. This has led to the farming of the black scraper in several parts of the southern coast of Korea. Since detailed research on its metabolism in relation to water temperature has been scanty, this was the investigative focus of the present study. The standard metabolism rates of the black scraper (9-10 months old, total length=$22.6{\pm}0.8cm$, wet weight=$140.3{\pm}13.9g$) were measured at seven different water temperature settings (12, 15, 17, 20, 23, 26, $28^{\circ}C$) to understand the relationship between metabolism and water temperature. Relationships between water temperature (WT) and oxygen consumption rate (OCR) were obtained as SOCR (weight-specific oxygen consumption rate) = 0.0117WT - 0.0135 ($r^2=0.9351$) and IOCR (oxygen consumption rate per individual) = 1.8160WT - 5.4007 ($r^2$ = 9428). The $Q_{10}$ (temperature sensitivity), an indicator of the sensitivity of biological function to temperature, was analyzed. In our experiment, when the water temperature increased, the $Q_{10}$ value decreased. The $Q_{10}$ value was 6.27 in waters where the temperature ranged from $12-15^{\circ}C$ and this was much higher than the values obtained in waters where temperatures ranged between (1) $15-23^{\circ}C$ and (2) $23-28^{\circ}C$. Consequently, it was shown that the black scraper is a warm water species and inhabiting waters in the temperature range from $15-28^{\circ}C$ is deemed appropriate.

• 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.