• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.7 no.3
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• pp.405-411
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• 1994

Purified myofibrils were prepared from ante-mortem stress and control lots of Taiwan country chicken breast and thigh muscles at death and afler storage at $4^{\circ}C$ for 0, 1, 2, 3, and 7 days post-mortem. Sodium dodecyl sulfate polycrylamide gel electrophoresis (3.2%) and densitometer were used to examine the effect of ante-mortem stress and control storage of muscle on titin and nebulin. Results indicated that titin and nebulin were more rapidly degraded in the control and the ante-mortem stress light muscles than in the control and ante-mortem dark muscles of Taiwan country chicken. In contrast, nebulin was shown to be more resistance to degradation in the ante-mortem stress dark muscle than in the control light muscle.

• Korean journal of food and cookery science
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• v.23 no.2 s.98
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• pp.221-226
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• 2007

This study was carried out to investigate the optimun conditions for the isolation of low molecular weight peptides containing histidine, and to evaluate the antioxidant effects of skipjack boiled extracts(SBE). The results are summarized as follows : L-histidine contents of the ordinary muscle and dark muscle extracts were $ 83.1{\pm}1.75{\mu}M/g\;and\;11.0{\pm}2.39\;{\mu}M/g$, respectively. The L-histidine level of the dark muscle was much lower than that of ordinary muscle in the SBE. The extracts were treated with alcalase and neutrase under different pH levels, temperatures, and times. The optimum hydrolysis conditions of SBE were pH 7.0 and a $60^{\circ}$C temperature for 2 hr in the batch reactor, which hydrolyzed 63% of the SBE. HPLC analysis showed a removing effect of the ultrafiltration permeate (UFP) to high molecular weight impurities in SBE. SBE and pure carnosine participated as inhibiting agents to, which was confirmed through the autoxidation processing of linoleic acid. UFP treatment improved the inhibiting ability of SBE to the autoxidation of linoleic acid. The reducing power of the UFP-treated ordinary muscle extracts were 10-fold higher than the dark muscle extracts, and 0.7-fold higher than 20 mM pure carnosine. The UFP-treated ordinary muscle extracts had greater reducing power activity than pure carnosine. The scavenging activities on DPPH radical of the different treated-SBE and pure carnosine were also investigated. Scavenging activities of the ordinary and dark muscle extracts and the pure carnosine were 90%, 70%, and 45%, respectively. In summary, Skipjack boiled extracts (SBE) demonstrated that low molecular weight peptides containing histidine are capable of inhibiting lipid oxidation. They also possessed effective abilities as free radical scavengers and reducing agents, and these activities may increase with increasing concentrations.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.16 no.2
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• pp.117-124
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• 1983

Qualify changes of the precooked frozen sardine (Sardinops melanosticta) during frozen storage were investigated by measuring extractable protein, expressible drip, available lysine and lipid oxidation as peroxide value. Fresh sardine was dressed, washed in chilled water, cooked in boiling water to have $55^{\circ}C\;and\;70^{\circ}$ at the center of the body, frozen at $-40^{\circ}C$, and finally stored at $-20^{\circ}C$ for 84 days. The quality factor mentioned above were determined in both ordinary and dark muscle at 14 day intervals through the period of storage. When cooked at $70^{\circ}C$, the changes in expressible drip were less than that of raw and the one cooked at $55^{\circ}C$. In observation of the extractability of muscle protein, no great change in extractable sarcoplasmic protein was observed, the extractable myofibrillar protein, however, showed a tendency to decrease during the period of frozen storage, accompanying the increase of the alkali-soluble protein. That was more excessive in ordinary muscle than dark muscle. Lipid oxidation of dark muscle was faster than that of ordinary muscle. Acid value was not changed, and peroxide value of the samples cooked at $70^{\circ}C\;and\;55^{\circ}$ was higher than that of raw at the early stage of the storage, after 40-50 day storage, it became lower than that of raw muscle.

• Korean Journal of Ichthyology
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• v.23 no.1
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• pp.21-29
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• 2011

Expression analysis of development-related genes was conducted using differential screening of 6-month-old [18M(-), 6M-18M] specific and 18-month-old [6M(-), 18M-6M] specific subtracted cDNA libraries constructed by subtractive hybridization using skeletal muscle of 6- and 18-month-old dark-banded rockfish Sebastes inermis. A total 202 cDNA clones displaying different expression levels in each stage were obtained; among them, 32 clones showing up-regulation were finally selected for further expression analysis. We sequenced the clones and analyzed individual sequences. Genes expressed specifically in 6-month-old skeletal muscle were identified as myosin, adenylate kinase, calsequestrin, dystrobrevin beta, and diphosphate kinase-Z1. Genes showing strong expression in 18-month-old rockfish were identified as desmin, TGFBR2 (transforming growth factor-beta receptor), muscle-type creatine kinase, and cathepsin D. Expression of these genes was checked further in 6-18-30-42 month-old dark-banded rock fish. Rapid reduction of expression was observed in dystrobrevin beta and diphosphate kinase. However, expression of creatine kinase (muscle type) and cathepsin D increased as dark-banded rockfish grew, and remained even after 18 months. The results reported here demonstrate that genes related to muscles contract are expressed at an early stage of development, and genes controlling energy in muscles are predominantly expressed at a late developmental stage.

• Preventive Nutrition and Food Science
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• v.10 no.1
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• pp.11-16
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• 2005

Enzymatic hydrolysis of dark muscle of skipjack was optimized by using response surface methodology. Three factors of independent values were pH (4.2 to 9.8), time (0.6 to 3.4 hrs) and temperature (34℃ to 76℃), and independent values were optical density and brix. The optimum conditions for enzymatic hydrolysis were pH 7.0 to 8.0, 55℃ and 3 hrs. The headspace volatile compounds of reaction flavors using the enzymatic hydrolysate, cysteine and xylose were identified by using the combination of a canister system, gas chromatography and mass selective detector. Among 67 compounds, we identified 8 sulfur-containing compounds and 7 furans which were thought to be highly related to meat-like flavors.

• Food Science of Animal Resources
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• v.25 no.4
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• pp.423-429
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• 2005

Properties of pant surimi derived from porcine longissimus muscle were investigated Rapid glycolysis of muscle reduced yield $\%$ of water-washed pork and moisture $\%$ of pent surimi because of ie lower ultimate pH. Gel Hardness was significantly (p<0.05) higher in pork surimi from rapid glycolysis muscle, but springiness was higher (p<0.05) in pork surimi from normal glycolysis muscle. SDS-PAGE pattern showed denaturation of sarcoplasmic proteins onto myofibrillar proteins in rapid glycolysis muscle, resulted in dark color and hard texture of pork surimi. Color and texture of gels were related with water-holding capacity of muscle proteins and moisture $\%$ in gel matrix. Results imply that glycolysis rate of porcine muscle at postmortem could affect gel properties of pork surimi, and muscle with rapid glycolysis muscle could produce a hard texture of pork surimi and dark color.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.15 no.3
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• pp.185-190
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• 1982

In utilization of small size red muscled fishes like mackerel, sardine, and filefish, mechanical dressing is usually required. The removal of dark muscle is also necessary to improve qualify of the product, which could hardly be done by mechanical process. As a method of separating dark muscle, specific gravity method using sugar solution was investigated in this study. And the effects of the level of specific gravity, the size and density of meat particles, and stability of meat particle float on the separation of dark muscle were discussed. From the results, effective specific gravity, in case of sucrose solution, ranged 1.067 to 1.072 for mackerel, 1.062 to 1.070 for sardine, and 1.072 to 1.077 for filefish, respectively. The maximum separation of more than $90\%$ was obtained at specific gravity of 1.075, 1.070, and 1.075 in cases of mackerel, sardine and filefish, respectively. The size of meat particles which were ground with 0.2cm orifice plate was adequate to yield $90\%$ separation or above. The meat particle float in the glucose solution began to precipitate within 5 minutes after separation while 25 minutes in case of sucrose solution. Lipids were also fairly removed by the dark muscle separation process.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.17 no.4
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• pp.313-320
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• 1984

In order to elucidate the oxidative stabilities of mackerel lipids, lipids were extracted from ordinary muscle, dark muscle, skin (including subcutaneous adipose tissue) and viscera, and then stored at $30^{\circ}C$. The changes of lipids were examined periodically by measuring peroxide value (POV), thiobarbituric acid (TBA), weighing method, acid value (AV) and iodine value (IV), Fatty acid composition of lipids was analyzed by GLC. The results obtained are summerized as follows: The velocity of lipid oxidation during the storage was differ from the extracting part of the sample. It was laster in skin, viscera, dark muscle and ordinary muscle in the order. Ratio of polar lipid fractions in total lipids was ranged from 5 to $15\%$, and the highest result was observed in dark muscle. Main fatty acids of the lipids were $C_{16:0}$ acid ($22.0{\sim}25.9\%$), $C_{18:1}$ acid ($22.3{\sim}26.7\%$) and $C_{22:6}$ acid ($9.6{\sim}13.4\%$), and $C_{22:6}$ acid content ($\%$) was the highest in lipid from dark muscle, and the lowest in lipid from skin. Monoenoic acid content ($\%$) was higher in the non-polar lipid than in the polar lipid, on the contrary. polyenoic acid content ($\%$) was higher in the polar lipid than in the non-polar lipid. Polyunsaturated fatty acids of the lipids, $C_{20:5}$ acid and $C_{22:6}$ acid, decreased predominantly with oxidation during storage, while saturated acids, $C_{14:0}$ acid and $C_{16:0}$ acid, increased predominantly. The polar lipid fractions were oxidized much faster than the non-polar lipid fractions.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.5
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• pp.469-476
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• 1986

Proteolytic activity of the tissue extracts from the muscle of mackerel, Scomber japonicus, and sardine, Sardinops melanostcta, was comparence with referenced to the optimum reaction condition. Thermal stability and change of proteolytic activity of the tissue extracts during storage were investigated. The existence of acid, weak acid and alkaline proteinase was identified in the ordinary and dark muscle of the mackerel and sardine. Specific activity of acid proteinase was stronger than weak acid or alkaline proteinase in the both fish. The proteolytic activity of the tissue extracts on the optimum reaction condition was: ordinary muscle of mackerel, 0.12 nM-Tyr. eq./mg-prot. /min. at pH 3.0 and $50^{\circ}C$; dark muscle of mackerel, 0.36 nM-Tyr. eq./mg-prot. /min. at pH 3.0 and $45^{\circ}C$; ordinary muscle of sardine, 0.45 nM-Tyr. eq./mg-prot. /min. at pH 2.4 and $45^{\circ}C$; dark muscle of sardine, 0.24 nM-Tyr. eq./mg-port. /min. at pH 2.4 and $45^{\circ}C$. The proteinases distributed in the muscle of mackerel and sardine were stable with the heat treatment at $45^{\circ}C$ for 5 minutes, but those in the dark muscle of mackerel was stable with the treatment at $5^{\circ}C$ for 5 minutes. The proteinases from the muscle were slowly inactivated with the whole storage days at $5^{\circ}C\;and\;-15^{\circ}C$, those were more stable at $-15^{\circ}C\;than\;5^{\circ}C$ storage.