• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.10
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• pp.1676-1684
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• 2004

Gel properties of recovered protein from mackerel, frozen blackspotted croaker, chicken breast and pork leg using acidic and alkaline processing were evaluated. Myofibrillar protein from mackerel by acidic processing did not form a heat-induced gel. However, the recovered protein including sarcoplasmic protein formed heatinduced gel. Breaking force of gel from mackerel processed at pH 10.5 was the lowest. A deformation value of frozen blackspotted croaker was the highest, followed by chicken breast, pork leg and mackerel. Whiteness of frozen blackspotted croaker was the highest among heat-induced gel. Breaking force, deformation and whiteness were decreased by addition of recovered protein from mackerel, but price was increased. A breaking force and whiteness of heat-induced gel added recovered protein from chicken breast were increased, and the price was greatly decreased. When the constraint of breaking force, deformation and price of raw material were set up above 110 g, 4.5 mm and below 2,000 won/kg. A optimum formulation for blending protein was 36∼50% for frozen blackspotted croaker, 34∼40% for chicken breast, 14∼25% for pork leg. The heat-induced gel of recovered protein from frozen blackspotted croaker showed compact structure compared to that of recovered protein from mackerel. A formulation of chicken breast and pork leg based on blackspotted croaker can be used in surimi based seafood products having various texture.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.28 no.2
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• pp.157-162
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• 1995

When fish meat is washed for the processing of surimi, about 50ff of lipid in the fish meat is removed from the fish meat to the effluent. The removed lipid was easily recovered by centrifugation or filteration of wastewater washed fish meat. Then, the recovered lipid was utilized as a material of mayonnaise sauce processing. The major fatty acids in the recovered lipids are $C_{16:0},\;C_{18:0},\;C_{16:1},\;C_{20:5},\;and\;C_{22:6}$ Polyenoic fatty acids were composed of $33.6\%$ to total fatty acids. When the recovered lipid was substituted for soybean oil in processing of mayonnaise sauce, the maximum percentage of substitution ratio presumed to be $30\%$ according to viscosity, color difference, and emulsion stability evalution for the substituted ones.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.44 no.1
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• pp.8-17
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• 2011

To identify and examine the distribution of proteolytic inhibitory activity in crude extracts from fish eggs, and to determine the applicability of these protease inhibitors as anti-degradation agents in surimi-based products and fish meat, we compared the inhibitory activities of various extracts from fish eggs to those of commercial proteases, such as trypsin and papain. We used the optimal conditions for the screening of trypsin activity: 30 ug/uL of 0.1% trypsin and 0.6 mM Na-benzoyl-L-arginine-p-nitroanilide (BAPNA) with a pH of 8.0 at $40^{\circ}C$ for 60 min. The activities of papain and four commercial proteases were investigated after mixing with 100 ug/uL enzymes and 0.3% casein with a pH of 8.0 at $40^{\circ}C$ for 60 min. We performed a screening assay to detect the inhibitory activity (%) of crude extracts from eight species of fish eggs against the target proteases trypsin and papain. The assay revealed a wide distribution of trypsin and papain inhibitors in fish eggs. The specific inhibitory activities (11.6.28.6 U/mg) of crude extracts from fish eggs against trypsin and BAPNA substrate were higher than that (0.64 U/mg) of egg whites, used as a commercial inhibitor. The inhibitory activities of crude extracts from fish eggs against trypsin, and of egg whites against casein substrate (1.94.4.51 U/mg), were higher than those of papain (0.24.1.57 U/mg) and commercial protease (0.04.0.32 U/mg). The extracts from fish eggs were rich in protease inhibitors that exhibited strong inhibitory activity against trypsin, a serine protease, and papain, a cysteine protease.

• Applied Biological Chemistry
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• v.39 no.2
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• pp.134-139
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• 1996

In order to effectively utilize marine animal skin wastes in marine processing manufacture, conger eel skin, file fish skin and arrow squid skin as raw material of edible gelatin were screened. Conger eel skin was the highest in the collagen content, followed by Ole fish skin and arrow squid skin, in the order named. In the fish skins, the soluble and insoluble collagens occupied $67.4%{\sim}72.3%\;and\;27.7{\sim}32.6%$, respectively, and in the arrow squid skin, 30.4ft and 69.6ft, respectively. No difference in the amino acid composition between soluble and insoluble collagens was detected. Collagen from the marine animal skin catched in coasted and offshore water in Korea consisted ${\alpha}$ chain and ${\beta}$ chain, and ${\alpha}$ chain were hetero type. The sum of proline and hydroxyproline contents in conger eel skin collagen was higher than that in the other skin collagens, while was lower than that pork skin collagen. Conger eel skin collagen exhibited a higher denaturation temperature in solution and a higher degree of proline hydroxylation, compared with skin collagen of the respective species. The physical properties such as gel strength, melting point and gelling point of conger eel skin gelatin were superior to those of file fish skin and arrow squid skin gelatins.