• Journal of Fisheries and Marine Sciences Education
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• v.3 no.2
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• pp.47-72
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• 1991

To obtain the principal data for useful treatment and processing of Korean geoduck (Panope japonica A. ADAMS) which inhabit mostly at Dong-Hae coastal area in Korea, changes of $NH_2$-N, TMAO, TMA, total creatinine, protein composition and fatty acid composition in raw and blanched geoduck muscle during storage at $-20^{\circ}C$ were investigated. In addition, its chemical composition variation in the whole year was elucidated. The moisture content in geoduck muscle meat was 78.1% to 82% in the whole year. Particularly, in July its moisture content was maximum as 82% and in September minimum as 78.1%. Crude protein was in the range of 12.3-16.4%, crude lipid the average was 1.5%, crude ash on the average was 1.4%. The abundant fatty acids in geoduck muscle oil were $C_{16}$ : 0, $C_{16}$ : 1, $C_{18}$ : 0, $C_{18}$ : 1, $C_{20}$ : 5, and $C_{22}$ : 6 acids. During storage at $-20^{\circ}C$, content of unsaturated fatty acid such as eicosapentaenoic acid (EPA, $C_{20}$ : 5) and docosahexaenoic acid (DHA, $C_{22}$ : 6)in raw geoduck muscle decreased somewhat and the raw geoduck was slightly oxidized. Trimethylamine (TMA), volatile basic nitrogen (VBN)and $NH_2$-N of raw muscle increased compared to blanched muscle. Trimethylamine oxide (TMAO) was slightly decreased during the storage period. The muscle protein was approximately composed of 37% sarcoplasmic, 29% myofibrillar, 22% alkali soluble, and 12% stroma protein. Among several proteins, myofibrillar protein content decreased mostly, while the alkali-soluble and stroma protein content increased slightly during storage at $-20^{\circ}C$.

• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.17 no.4
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• pp.280-290
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• 1984

An extensive study has been made on the relationship between the freshness and the compositions of the muscle protein of prawn, Pandalus japonica during the storage under partially frozen condition. The variations of the subunit distribution for sarcoplasmic protein and myofibrillar protein extracted from the samples by changes of freshness were discussed by sodium dodecylsulfate-poly-acrylamide gel (SDS-PAG) electrophoresis. On the other hand, the denaturation constant ($K_D$) of the myofibrillar protein extracted from the prawn stored at $-3^{\circ}C\;and\;-20^{\circ}C$ were successively compared. The prawn muscle contained about $18\%$ of protein with the composition of $32\%$ in sarcoplasmic protein, $56\%$ in myofibrillar protein, $10\%$ in residual intracellular protein and $2\%$ in stroma. The indices for estimating freshness of the muscle were approached to the early stage of putrefaction on the 26th day of the storage with $25.29mg\%$ of total volatile basic nitrogen, $31.36\%$ of K-value and 8.83 of pH. The content of the myofibrillar protein was remarkably decreased with the time during the storage while that of residual intracellular protein was increased. The $K_D$ values of the myofibrillar protein were $9.03{\times}10^{-6}sec^{-1}\;at\;-3^{\circ}C\;and\;4.42{\times}10^{-6}sec^{-1}\;at\;-20^{\circ}C$. The results of the analysis of SDS-PAG electrophoretograms indicated that the sarcoplasmic protein and the myofibrillar protein were composed of 12 subunits and 17 subunits in the muscle of instantaneously killed prawn ana were changed into 8 subunits and 22 subunits in the muscle stored for 26 days, respectively. It is noticeable that 30,000, 41,000, 107,000, 136,000, 170,000 173,000, 185,000, and 198,000 daltons of the newly appeared 8 subunits were found in the myofibrillar protein from the prawn muscle stored for 26 days. The amino acid composition of the muscle protein showed that the most of amino acids were slightly decreased with the days of the storage. With respect to the free amino acid composition of the muscle of instantaneously killed prawn, glycine, proline, arginine, alanine and taurine comprised $93\%$ of the total free amino acids. Taurine, valine, leucine, phenylalanine, serine, lysine, methionine, isoleucine and histidine were increased during the storage period but exceptionally proline was decreased.

• Food Science and Preservation
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• v.16 no.5
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• pp.686-698
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• 2009

We sought basic data for product development and storage improvement of abalone. We explored drying methodologies, such as shade drying, cold air drying, and vacuum freeze drying. We also examined various physicochemical features of both meat and viscera. Raw abalone meat had $78.88{\pm}1.01%$ moisture, $9.24{\pm}0.27%$ crude protein, and $10.05{\pm}0.81%$ carbohydrate (all w/w). The moisture level of dried abalone meat was highest after cold air drying, at $18.38{\pm}0.91%$, and lowest after vacuum freeze drying, at $1.05{\pm}0.05%$. The total amino acid content of raw abalone meat was $17,124.05{\pm}493.18\;mg%$, and fell after shade-drying to $12,969.92{\pm}583.65\;mg%$, and to $13,328.78{\pm}653.11\;mg%$ after cold air drying. The total free amino acid content of raw abalone meat was $4,261.99{\pm}106.55\;mg%$, and rose after shade-drying to $6,336.50{\pm}285.15\;mg%$, to $5,072.04{\pm}248.53\;mg%$ after cold air drying, and to $4,638.85{\pm}218.03\;mg%$ after vacuum freeze drying. The fatty acid proportions in raw abalone meat were $47.00{\pm}0.99%$ saturated, $22.18{\pm}1.05%$ monounsaturated, and $30.82{\pm}1.45%$ polyunsaturated. In the viscera, however, the proportions were $36.72{\pm}0.74%$ saturated, $25.44{\pm}1.12%$ monounsaturated, and $37.84{\pm}1.67%$ polyunsaturated. The contents of chondroitin sulfate in raw abalone were $11.95{\pm}0.35%$ in meat and $7.71{\pm}0.19%$ in viscera (both w/w). After shade-drying, the chondroitin sulfate content was $16.57{\pm}0.90%$ in meat and $9.24{\pm}0.50%$ in viscera. The figures after cold air drying were $16.17{\pm}0.79%$ and $12.44{\pm}0.61%$, and those after vacuum freeze drying $25.17{\pm}1.16%$ and $15.22{\pm}0.70%$ (thus including the highest meat content). The level of collagen in raw abalone was $69.80{\pm}3.07\;mg/g$ in meat and $40.62{\pm}1.79\;mg/g$ in viscera. Meat and viscera dried in the shade had $144.05{\pm}7.78\;mg/g$ and $44.16{\pm}2.39\;mg/g$ collagen, respectively, whereas the figures after cold air drying were $133.29{\pm}6.53\;mg/g$ and $69.20{\pm}3.39\;mg/g$, and after vacuum freeze drying $137.51{\pm}6.33\;mg/g$ and $60.61{\pm}2.79\;mg/g$. Volatile basic nitrogen values of raw abalone showed a higher content in viscera, at $19.01{\pm}0.84\;mg%$, compared to meat ($10.10{\pm}0.44\;mg%$). The value for shade-dried abalone meat was $136.77{\pm}7.37\;mg%$ and that of viscera $197.97{\pm}10.69\;mg%$. After cold air drying the meat and visceral values were $27.32{\pm}1.34\;mg%$ and $71.37{\pm}3.50\;mg%$, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.4
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• pp.464-469
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• 2006

This study was conducted to evaluate a knowledge on food components of muscle and adductor muscle of pearl oyster (Pinctada fucata martensii) as pearl processing byproducts. The concentrations of mercury and chromium as heavy metal were not detected in both pearl oyster muscle and adductor muscle, and those of cadmium and lead were 0.06 ppm and 0.11 ppm in only pearl oyster muscle, respectively. Thus, the heavy metal levels of pearl processing byproducts were below the reported safety limits. The volatile basic nitrogen (VBN) content and pH of pearl oyster muscle were 11.6 mg/100g and 6.31 and those of abductor muscle were 8.6 mg/100 g and 6.33, respectively. It was concluded that pearl oyster muscle and adductor muscle might not invoke health risk in using food resource. The contents of crude protein (16.5%) and total amino acid (15,691 mg/100 g) of adductor muscle were higher than those of muscle (11.2% and 10,131 mg/100 g) and oyster (12.1% and 11,213 mg/100 g) as a control. The contents of calcium and phosphorus were 95.4 mg/100 g and 116.0 mg/100 g in muscle, 75.2 mg/100g and 148.1 mg/100 g in adductor muscle, respectively. The calcium level based on phosphorus was a good ratio for absorbing calcium. The free amino acid contents and taste values were 635.5 mg/100 g and 40.2 in muscle, and 734.9 mg/100 g and 24.1 in adductor muscle, respectively, but that (882.8 mg/100 g and 40.2) of oyster was higher than those of pearl processing byproducts. Based on the results of physicochemical and nutritional properties, pearl oyster muscle and adductor muscle can be utilized as a food resource.