• Korean Journal of Fisheries and Aquatic Sciences
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• v.45 no.4
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• pp.358-366
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• 2012

A novel neuropeptide was isolated from the skin of the conger eel Conger myriaster using hagfish Eptatretus burgeri intestine as a bioassay system. The sequence of the purified peptide was analyzed using automated amino acid sequencing and MALDI-TOF mass spectrophotometry. The molecular ion peak in the MALDI-TOF mass spectrum of the peptide was at m/z 962.89 $(M+H)^+$. The sequence of the peptide was determined to be L-P-M-L-E-T-Q-M, and was tentatively named comyrin. To investigate the complete primary structure of comyrin, comyrin-OH and comyrin-$NH_2$ were synthesized and the chemical and pharmacological properties of the synthetic peptides were compared with those of the native peptide. However, the elution time of synthetic peptides did not match that of the native peptide on the reverse-phase HPLC chromatogram. In addition, the synthetic peptides did not cause contractile activity in the intestinal smooth muscle of the hagfish. Based on these results, one possible reason for this disagreement may be the presence of a D-amino acid in comyrin.

• 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.

• Applied Biological Chemistry
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• v.39 no.4
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• pp.274-281
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• 1996

To prepare edible skin gelatin of conger eel such as material fur quality improvement of surimi gel, the defatted skin was limed with 1% calcium hydroxide at $5^{\circ}C$ for 2 days, washed thoroughly with tap water, extracted with 8 volumes of distilled water to dehydrated skin for 2 hours at $50^{\circ}C$. The gelatin extract was centrifuged, filtered and then passed through anion(Amberlite 200C) and cation (Amberlite IR 900) resins. The purified gelatin solution was evaporated and dried by hot-air blast$(40^{\circ}C)$. The gelatin prepared by above condition had the highest quality as revealed by physical property values i.e. 240.5 g in gel strength, $28.0^{\circ}C$ in melting point and $28.0^{\circ}C$ in gelling point. Funtional property values were 56.8% in solubility, 1.8 ml/g in oil binding capacity, 55.0% in emulsifying capacity and 48.5% in emulsifying stability. jelly strength and senso교 evaluation of surimi gel from fish with red muscle were not improved by addition of emulsifying curd from conger eel skin gelatin as emulsifier. Therefore, the conger eel skin gelatin requires a suitable modification of functional group and improvement of processing operation to utilize as a material for quality Improvement of surimi gel.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.11 no.4
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• pp.189-195
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• 1978

Using the skins of conger eel, Astroconger myriaster, and hagfish, Eptatretus burzeri, from fillet manufactory, the optimum conditions of skin glue processing were investigated and physical ana chemical properties of the product were also determined. The yields of conger eel and hagfish skin to the total body weight were $10.6\%$ and $11.4\%$, respectively. The optimum processing conditions for conger eel skin glue were the extraction of skins which were previously tinted with $0.3\%$ calcium hydroxide solution for one hour, in water at pH 5.5 and $60^{\circ}C$ for four hours. The additional water was six times sample weight. In case of the hagfish skin glue, the liming time with $0.3\%$ calcium hydroxide solution was suitable for three hours, and the skins were extracted with water as much as nine times sample weight at pH 5.0 and $60^{\circ}C$ for three hours. The contents of crude protein of conger eel and hagfish skin glue were $91.5\%$ and $90.2\%$, respectively. The content of crude lipid was slightly higher than that of chemical grade gelatin. Relative viscosity, melting point, gelation temperature and jelly strength of conger eel skin glue were 13.6, $15.2^{\circ}C$, $6.2^{\circ}C$ and 13.0g respectively and those of hagfish skin glue were 12.9, $14.8^{\circ}C$, $4.3^{\circ}C$ and 23.3g respectively. The turbidity of conger eel skin glue and hagfish skin glue were slightly superior to those of dry glue.

• Applied Biological Chemistry
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• v.39 no.4
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• pp.282-286
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• 1996

To effectively utilize fish skin gelatin as a material for quality improvement in surimi gel from fish with a red muscle, conger eel skin gelatin was modified with succinic anhydride, and funtional properties such as emulsifying activity and emulsifying stability were determined. The degree of chemical modification incresed up to 0.3 g of succinic anhydride/g of gelatin, above this adding ratio a nearly constant value was reached. The maximum amount of modification was about 90%. The emulsifying activity and emulsifying stability of gelatin gradually increased up to 89.8% of succinylation extent, little changed above of succinylation extent. The other functional properties as solubility, water holding capacity, foam expansion and foam stability were improved following succinylation with 0.3 g of succinic anhydride/g of gelatin. Amino acid composition of succinylated gelatin was similar to that of unmodified gelatin. Heavy metal contents such as cadmium, lead, copper and zinc of succinylated gelatin were lower than those of unmodified gelatin.

• Applied Biological Chemistry
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• v.39 no.5
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• pp.361-367
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• 1996

As a part of investigation for quality improvement of surimi gel from fish with a red muscle by addition of emulsion curd, we investigated the processing conditions of emulsion curd contained succinylated gelatin from conger eel skin as an emulsifier and emulsion curd-added surimi gel. Activity and stability of emulsion curd on standing at room temperature, chilled temperature and vibration were remarkably improved by the addition of 15 tunes of soybean oil and 5 times of water to succinylated gelatin from conger eel skin. The proximate composition of the emulsion curd was moisture 18%, protein 5%, lipid 76% and ash 0.5% and its appearance was white. Peroxide value and fatty acid composition of emulsion curd contained succinylated gelatin as an emulsifier were similar to these of soybean oil. By the addition of 6% of emulsion curd to mackerel surimi, gel strength, appearance and texture of the resulting surimi gel were improved, while its peroxide value and brown pigment revealed minor change. From the results of volatile basic nitrogen, viable cell counts and histamine content, the emulsion curd-added mackerel surimi gel can be safe In the sense of food sanitation.