• Korean Journal of Poultry Science
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• v.15 no.1
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• pp.45-51
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• 1988

This experiment was conducted to determine yolk addition level for manufacturing the seasoned yolk Products. They were Prepared with 0, 10, 20, 40% yolk content in conduction with fish meat faste and spices. Yolk mixture was cooked at $90^{\circ}C$ for 1 hour and then dried with hot air at 5511 for 5 hours. The texture of non-dried seasoned product added with 10% yolk was remarkably increased as compared with any other treatment. For the drying process of seasoned yolk product, the more addition of egg yolk to the mure resulted in a slight difficulties on drying. As yolk level increased in dried seasoned product (egg jerky), moisture and fat content increased whereas protein and total amino acid content decreased. Most of amino acid except leucine, isoleucine and phenylalanine decreased by increasing level of egg ye The Predominant amino acids were glutamic acid, aspartic acid and lysine but only small amount of proline was detected in each treatment. Results of experiment indicated that yolk could be used up 20% level in view of physicochemical and sensory quality in seasoned products.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.1
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• pp.27-35
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• 1986

In succession to the previous paper, the present study was directed to investigate the effect of keeping freshness of conger eel (Astroconger myriaster) and yellowtail (Seriola quinqueradiata) by partial freezing, and the changes in the physical properties of fish meat paste product prepared with the muscle of conger eel during storage were also examined. The results obtained are summarized as follows: The period of keeping freshness (days in which k value reaches $20\%$) of conger eel and yellowtail by partial freezing was 10 days and 6 days, respectively. VBN content in the conger eel muscle showed 39.5 mg/100g by icing for 15 days, and did not show a great change by partial freezing and freezing, while that of yellowtail muscle reached at 32 mg/100g by icing, 20 mg/100g by partial freezing and 18 mg/100g by freezing for 15 days. The lipids extracted from the muscles of both fishes by icing were remarkably oxidized than those by partial freezing. The myofibrillar protein in the conger eel muscle during storage for 9 days decreased $3\%,\;10%\;and\;11\%$ by icing, partial freezing and freezing, respectively, and that of yellowtail muscle did $16\%,\;10%\;and\;4\%$ by icing, partial freezing and freezing, respectively. On the other hand, the alkali-soluble protein in both fishes increased with storage time. Gel strength of fish meat paste product prepared with the muscle of conger eel decreased to $35\%$ by icing, $74\%$ by partial freezing and $76\%$ by freezing for 10 days compared to control, and the expressible water increased 1.6 times, 1.2 times and 1.1 times by icing, partial freezing and freezing, respectively, as much as that of control product.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.20 no.5
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• pp.431-440
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• 1987

In order to develop a new type of food source for the effective utilization of fish protein, plastein reaction was applied to improve the functional properties of filefish protein. Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, pepsin, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper). Also, L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. And, General composition, yield, molecular weight, amino acid composition, color and IR spectrum of plasteins were measured. The protein, ash and lipid content of the plasteins were $72\~78\%,\;7.4\~11.8\%\;and\;0.3\~0.9\%$ respectively. The yield of plasteins were papain $55.0\%,\;pepsin\;47.6\%,\;\alpha-chymotrypsin\;38.3\%,\;protease\;23.6\%$, glutamic acid-incorporated plastein (Glu-Plastein) $35.0\%$, and leucine-incorporated plastein (Leu-plastein) $45.7\%$. The glutamic acid and leucine content in Glu-plastein and Leu-plastein were $38.7\%,\;41,7\%$, respectively, while the contents in the peptic filefish protein hydrolysate were $16.01\%\;and\;8.16\%$, respectively. The amino acid compositions were similar to that of the original filefish muscle protein. The major molecular weights of the peptic hydrolysate estimated by gel filteration were 2,000 and 310, and those of plasteihs were 21,000 and 4,900 for papain, 24,000 for pepsin, 18,500 for $\alpha-chymotrypsin$ 6,700 for protease, 24,000 for Glu-plastein and 17,000 for Leu-plastein. The structural changes in freeze-dried filefish meat, the FPC and hydrolysate were not observed on the IR spectrum. But plasteins showed amide I band in $1,600\~l,700cm^{-1}$ range and resulted in a strong band in $800\~850\;cm^{-1},\;700\~750\;cm^{-1}\;and\;650\~700\;cm^{-1}$. The amide I band of Glu-plastein was wider than those of other plasteins and had also a small band at $1,440\;cm^{-1}$.