• 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 $1,440\;cm^{-1}$.

• Korean Journal of Food Science and Technology
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• v.17 no.2
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• pp.121-127
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• 1985

In studying the structural work on ciguatoxin, parrot fish collected were identified as Scarus sordidus, S. frenatus, S. scaber and S. pectarlis, in which only S. sordidus contained toxic materials. Crude toxins obtained by silicic acid column chromatography, could be separated on a DEAE-cellulose column into two fractions, ST-1(less polar) and ST-2(polar) eluted with chloroform and chloroform-methanol(1:1). Furthermore ST-1 could be changed into ST-2 by repeated chromatography on DEAE-cellulose. Rf values of ST-1 and ST-2 were 0.60-0.75 and 0.30-0.54 on TLC coated with silica gel 60F-254 developed by chloroform-methanol-water-acetic acid (90:9.5:0.2:0.3) mixture. The peaks of ST-1 and ST-2 were not observed on each HPLC chromatogram at low sensitivity(2X), but by bioassay they were detected in the fraction of 24-27ml(less polar toxin, 120ng) and 22-27 ml (polar toxin, 150 ng). Less polar ciguatoxin from morey eel viscera also showed its peak in the same elution volume(25ml). Being subjected to chromatography on basic aluminum oxide (activity grade I) or to alkaline treatment, followed by basic aluminum oxide (activity grade I) chromatography ST-1 toxin was remarkably converted into the polar toxic component supposed to be polar ciguatoxin in both cases. In the latter case, approximately 74% of the residual toxicity was changed into the polar component, accompanied by about 50% loss of the initial toxicity. More than 26% of ST-2 toxicity was transformed into the less polar toxic component supposed to be less polar ciguatoxin on a deactivated aluminum oxide (activity grade V) column.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.6
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• pp.547-557
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• 1986

The characteristics of the three alkaline proteinases, Enz. A, B and C, from the pyloric caeca of mackerel have been investigated. The optimum condition for the activity of the Enz. A, B and C was pH 9.4, 9.8 and 9.8 at $45^{\circ}C$ for $2\%$ casein solution, and was pH 9.2 10.2 and 9.8 at $45^{\circ}C$ for $5\%$ hemoglobin denatured by urea, respectively. Enz. A, B and C by heat treatment at $50^{\circ}C$ for 5 min were inactivated 90, 33 and $37\%$, respectively, over the original activity. The reaction rate of the three alkaline proteinases was constant to the reaction time to 40 min in the reaction condition of $2{\mu}g/ml$ of enzyme concentration and $2\%$ casein solution. The reaction rate equation and Km value against casein substrate determined by the method of Lineweaver and Burk were: Enz. A, Y=3.6X and $Km=5.0{\times}10^{-3}\%$; Enz. B, Y=6.0X and $Km=1.0{\times}10^{-3}\%$; Enz. C, Y=4.2X and $Km=3.6{\times}10^{-3}\%$. The three alkaline proteinases were inactivated by $Ag^+$ and $Hg^{2+}$, but activated by $Mn^{2+},\;Sn^{2+}\;and\;Pb^{2+}$, Enz. B and C were remarkably inhibited by the soybean trypsin inhibitor. Molecular weight of Enz. A, B and C determined by SDS-polyacrylamide gel electrophoresis and Sephadex G-100 gel filtration was in the range of $27,500{\pm}2,500,\;20,500{\pm}1,500\;and\;15,250{\pm}250$, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.36 no.11
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• pp.1458-1464
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• 2007

This study was conducted to develope a new type of ready-to-eat smoked Sebastes schlegeli product with high acceptability and extended shelf-life. A Sebastes schlegeli was salted at 4% salt concentration for 6 hr at $4^{\circ}C$. The cold smoking conditions for the salted Sebastes schlegeli consisted of drying for 2 hr at $22{\sim}24^{\circ}C$ followed by smoking for 2 hr at $22{\sim}24^{\circ}C$. The warm smoking conditions for the salted Sebastes schlegeli consisted of drying for 2 hr at $22{\sim}24^{\circ}C$, smoking for 2 hr at $22{\sim}24^{\circ}C$, and smoking again for 30 min at $47{\sim}50^{\circ}C$. The rancidity of the smoked Sebastes schlegeli did not change after 1 year storage at $-20^{\circ}C$ by monitoring the iodine value, peroxide value, and acid value. The number of viable cells in the cold and warm smoked samples were counted as $7.4{\times}10^5$ and $6.2{times}10^5$ CFU/g, respectively. Viable cells were not detected after 1 year of storage at $-20^{\circ}C$. The sensory evaluations of the processed Sebastes schlegeli showed that elastic texture increased with smoking as compared to with salting. There were no significant differences between cold and warm smoking in terms of sweetness, elastic texture, color, and smoke flavor. However, for overall acceptability, preference were in the oder of cold smoked, warm smoked, and salted.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.8
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• pp.1265-1273
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• 2005

The purpose of this study was to prepare accelerated salt-fermented anchovy sauce using a shrimp processing byproducts (head, shell and tail) as a fermenting accelerator, and to investigate its physicochemical and enzymatic properties. Four types of sauces were prepared with 0, 10, 20, and 30$\%$ (w/w) addition of shrimp byproduct and fermented at 24$\pm$2$^{\circ}C$ for 360 days. During fermentation, all four type sauces decreased moisture content (67.5$\%$68.0$\%$ to 64.0$\∼$64.8$\%$) and pH (5.52$\∼$7.10 to 5.03$\∼$6.58), but showed increase in their crude protein (7.0$\∼$8.2 to 10.8$\%$) and volatile basic nitrogen contents (40$\∼$75 to 180$\∼$200 mg/100 g of sauce). The ratio of amino nitrogen to total nitrogen contents of control (0$\%$) and sauce with 10$\%$ shrimp byproducts (10$\%$ sauce) were maximized at 270 days, whereas 20$ \% $ and 30$\%$ added sauces were at 180 days. Endoprotease and exoprotease activities of anchovy sauces added with 20$\%$ and 30$\%$ of shrimp byproducts tend to be higher than those of control (0$\%$) and 10$\%$ addition. Proteolytic activities of sauces at pH 9 were about 2 times higher than those at pH 6. Amidolytic activities for LeuPNA decreased remarkably during fermentation, and control (0$\%$) almost lost their activity at 180 days, while additional sauces were relatively stable. These suggest that alkaline pretense of anchovy and shrimp byproducts as a endoprotease mainly contributed to the fermentation of salt-fermented sauces. The protein molecular weight distribution of sauces indicated 2 groups of peaks (peak 1,>70,000 da and peak 2, 3,000$\∼$29,000 da). As the fermentation proceeded, peak 1 tended to decrease in all of sauces, but peak 2 increased rapidly from 30 to 270 days. Optimum fermentation periods of control and 10$\%$ sauces were 270 days and those of 20$\%$ and 30$\%$ sauce were 180 days. The results suggest that shrimp byproduct can be used as accelerator of salt-fermented sauce.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.15 no.2
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• pp.123-136
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• 1982

We investigated the changes in protein and free amino acid compositions of the muscles, and amino acid composition of the muscle proteins during postmortem storage of dorsal white and lateral dark muscles of Yellowtail, Seriola quinqueradita, which were kept at $2^{\circ}C$. We present an extensive discussion on the relationship between the changes of freshness and those of protein compositions in the white and the dark muscle of the red-fleshed fish by analyzing polyacrylamide gel electrophoretograms of $NaDodSO_4-solubilized$ sarcoplasmic and myofibrillar proteins extracted from the both muscles. By assessing K-value, total volatile basic nitrogen and pH value as a criterion of freshness, we found that the dark muscle undergoes a more rapid decrease in its freshness compared to that of the white muscle. The contents of the sarcoplasmic and the myofibrillar protein were decreased with postmortem aging of the muscles while those of the residual intracellular protein were increased, and these changes were somewhat faster in the dark muscle than in the white muscle. From the analysis of the electrophoretograms and their densitograms, we found that the sarcoplasmic proteins of the white and the dark muscle were respectively composed of 16 and 12 components. The sarcoplasmic protein of the white muscle lapsed for 10 days showed an increase of 18,000 and 41,000 dalton components, and a gradual decrease of 23,000 and 23,500 dalton components, whereas the sarcoplasmic protein of the dark muscle lapsed for 9 days showed a decrease of 49,000 dalton component, an appearence of a newly formed component of 47,000 dalton, and a disappearance of 26,000 dalton component. The electrophoretograms of the myofibrillar proteins shelved that the white and the dark muscle were composed of 17 and 16 components, respectively. Depending on the lapsed time of postmortem under the controlled condition, the myofibrillar proteins of the white muscle showed an increase of 40,000 dalton component, a gradual decrease of 37,500 dalton component, an appearance of a newly forming component of 32,000 dalton and a disappearance of 26,000 dalton component. On the other hand, the myofibrillar proteins of the dark muscle showed an increase of 58,000 and 64,000 dalton bands, a disappearance of light chain-2 protein and an appearance of a newly forming protein of 32,000 dalton. These changes on the electrophoretic patterns in the dark muscle were more rapid than those in the white muscle. In almost all of the cases, we observed that the changes in the sarcoplasmic protein were faster than those in the myofibrillar protein. The analysis of amino acid of the both muscle proteins showed that the white muscle was rich in glutamic acid, aspartic acid, leucine, arginine, lysine, etc. but was poor in proline and tryptophan. No significant difference was found in the amino acid composition of protein of both the white and the dark muscles. The sample of white muscle lapsed for 10 days shows a remarkable decrease in glutamic and aspartic acids, while that of the dark muscle lapsed for 9 days shows an appreciable decrease in alanine, glycine and arginine. The free amino acid compositions of the white and the dark muscles are respectively characterized with $63\%$ of histidine and $67\%$ of taurine with respect to the total free amino acids of the yellowtail at-death, respectively. The white muscle lapsed for 10 days showed an increase of histidine, valine and taurine, and a slight decrease of alanine, leucine and glycine. The dark muscle lapsed for 9 days shelved an increase of taurine, phenylalanine and glycine, and a decrease of histidine, alanine and serine.