• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.763-770
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• 1993

To investigate the quality changes during frozen storage, top shell, Omphalius pfeifferi capenteri, was stored at -18$^{\circ}C$, -$25^{\circ}C$ and -3$0^{\circ}C$ immediately after shelling and water holding capacity, protein composition and histological features were examined with the lapsed period of the storage. During the storage period, amount of free drip was increased with higher frozen temperature and longer frozen period, but with the longer storage period, the lower water holding capacity was observed. The extractability and composition of muscle protein, sarcoplasmic protein and stroma protein were rather stable regardless of frozen temperature and frozen storage period. However, the extractability of myofibrillar protein was decreased with higher frozen temperature and longer frozen storage period. On the changes of muscle tissue structure, following points were observed. 1) In the muscle tissue structure of fresh sample, fine muscle fiber was closely distributed all over the tissue regardless of cross and longitudinal section. 2) In tissue structure under frozen state, it was observed that ice crystals apparently grew with the higher storage temperature. Empty spaces between muscle bundles which wee formed by aggregations of muscle fiber were observed after 3 months storage at -18$^{\circ}C$ . 3) Tissue structure in thawed state was restored satisfactorily after 1 month storage regardless of storage temperature. After 3 months storage at -3$0^{\circ}C$, muscle tissue was well restored, but at -18$^{\circ}C$, empty spaces were apparent due to incomplete restoration.

• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.1
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• pp.123-130
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• 1989

Myofibrillar protein(myofibil) was prepared from Yellowtail fish (Seriola quinqueradiata), and then, it was stored at $0^{\circ}C$(ice-cooling), $-3.5^{\circ}C$(partial freezing) and $-20^{\circ}C$(freezing). Another myofibrils were prepared from the fish stored with ice-cooling, partial freezing and freezing for a week as the maximum. Denaturation of muscle protein during the storage was investigated by the measurement of $Ca^{2+}-$ and $Mg^{2+}-ATPase$ activity. Specific activity of $Ca^{2+}-\;and\;Mg^{2+}-ATPase$ associated with Yellowtail myofibrils was 0.155 and $0.149\;{\mu}\;mole$ Pi/min/mg of protein, respectively, before storgae. ATPase activity of myofibils did not show any significant difference between $0^{\circ}C$ and $-3.5^{\circ}C$ whereas it was decreased faster at $-20^{\circ}C$ than at $0^{\circ}C$ or $-3.5^{\circ}C$. ATPase activity of myofibirls extracted from the fish stored for a week was 1.2-1.8 times higher than myofibils stored with ice-cooling or partial freezing while it was 2.5-3 times higher than that with freezing. Apparent denaturation constant of $Ca^{2+}-ATPase$ of myofibrils was between 0.48-0.65, and it was 2-3 times higher than that of $Mg^{2+}-ATPase$. The constant of myofibrils extracted from the fish did not show significant difference between $Ca^{2+}-\;and\;Mg^{2+}-ATPase$.

• Food Science of Animal Resources
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• v.31 no.5
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• pp.663-667
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• 2011

This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

• Asian-Australasian Journal of Animal Sciences
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• v.33 no.4
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• pp.662-669
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• 2020

Objective: This study was conducted to evaluate the effect of red glasswort (RG) (Salicornia herbacea L.) curing on the physicochemical, textural and sensory properties of cooked pork loin ham (M. longissimus thoracis et lumborum). Methods: All treatments were cured with different salt and RG powder levels. RG0 treatment was prepared with only 4% NaCl (w/w) as a control, and RG25, 3% NaCl:1% RG (w/w); RG50, 2% NaCl:2% RG (w/w); RG75, 1% NaCl:3% RG (w/w); RG100, 0% NaCl:4% RG (w/w) treatments were prepared sequentially. All samples were individually vacuum packaged in polyethylene bags and stored for 7 d at 3℃±1℃. Results: The results showed that as the rate of RG substitution increased, pH value, redness, myofibrillar protein solubility, and myofibrillar fragmentation index increased (p<0.05), but salt concentration and shear force decreased (p<0.05). However, there were no significant differences in cooking loss and moisture content. In terms of sensory evaluation, RG100 exhibited higher scores in tenderness and juiciness than RG0 (p<0.05). Conclusion: The partial substitution of NaCl by RG could improve the physicochemical properties, textural and sensory characteristics of cooked pork loin. Therefore, it is suggested that RG as a natural salt replacer could be an effective ingredient for developing low-sodium cured hams.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.2
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• pp.214-219
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• 1998

This study was carried out to investigate the changes of physicochemical and sensory characteristics according to cold storage period of the vacuum-time beef loin. The pH was decreased for 10 days, and then was increased gradually during storage time. The lactic acid content during the initial storage was 483mg/100g, after storage for 10 days it was increased significantly (p<0.05) to 625mg/100g, and then was decreased with storage time. Regarding of color difference, the L values were 41.0~42.5, but after storage for 40 days they were increased significantly(p<0.05) to 46.2, the a and b values wee 17.3~14.3 and 7.2~5.8, respectively, they were no significant differences depending n storage time. The shear force values showed 584 and 560g for 0 and 10 days, respectively but after storage for 20 days it was decreased significntly(p<0.05) to 299g. The myofibrillar protein extractability was no significant difference for 20 days, howener, it was increased remarkably at 30 days(p<0.05). The myofibrillar fragmentation index was increased significantly (p<0.05) on 20 and 40 days, and the Mg-ATPase activity of myofibrils was increasd to 30 days. The free amino acid was increased during storage periods. The composition of amino acid was composed of glutamic acid, alanine, valine and lysine, which were predominant amino acids as 45%. The total free amino acid was increased 182.18mg/100g to 40 days. The raw meat aroma showed no significant changes during storage time, but the tenderness was increased until 30 days(p<0.05). The color was superior from 20 to 30 days. The taste of cooked meat indicated significant changer to 30 days, but was significantly inferior(p<0.05) at 40 days, the aroma was superior until 30 days(p<0.05). The palatability was superior between 20 and 30 days.

• Food Science of Animal Resources
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• v.43 no.2
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• pp.269-281
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• 2023

In this study, we evaluate the effect of gelatin coating and sonication of wet-aged pork loin on quality. The moisture content of wet-aged pork loin with sonication and gelatin coating was the highest in the G5S sample (5% gelatin coating and sonication), while the moisture content of wet-aged pork loin with sonication was higher than that without sonication. The pH of wet-aged pork loin with sonication was lower than that without sonication. The aging loss of 5% gelatin coating with sonication was significantly lower than that of G0 (control), while the cooking loss was the lowest in G0 wet-aged pork loin. The water holding capacity of the wet-aged pork loin was the highest in G1. The thiobarbituric acid reactive substances value of wet-aged pork loin was significantly decreased with coating and not affected by sonication. The gelatin coating and sonication treatment significantly increased the myofibrillar fragmentation index of the samples. Shear force of wet-aged pork loin significantly decreased as the samples were gelatin-coated and sonicated. The myofibrillar and total protein solubilities were not significantly different between samples. In conclusion, the 1% gelatin coating with sonication can enhance the quality of wet-aged pork loin.

• The Korean Journal of Food And Nutrition
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• v.10 no.4
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• pp.468-474
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• 1997

This study was designed to investigate the changes in meat quality of beef shank, rib and loin during storage at 8$^{\circ}C$. The shear force value(SFV) of beef shank and loin decreased significantly after 6days storage, beef loin was no significant difference during storage. The SFV in early storage period was high in the order of beef rib, loin and shank, but the SFV of beef rib and loin was similar in course of storage period. The Myofibrillar fragmentation index(MFI) of beef shank increased significantly after 6 days storage, but beef rib and loin early storage was high in the order of beef rib, loin and shank. The actomyosin extractability after 3days storage increased in all parts of beef, but beef loin decreased after 6 days storage. In case of Mg2+-ATPase activity of actomyosin, beef shank increased to 3 days storage, and this reached the level of 0 day after 6days. The MG2+-ATPase activity of beef rib and loin was similar, but beef rib in early storage was higher than beef loin. The Ca2+-TPase activity of beef shank increased to 3 days and decreased after 6 days storage, beef rib was not different during storage and beef loin decreased slightly during storage.

• Journal of Animal Science and Technology
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• v.58 no.6
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• pp.23.1-23.17
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• 2016

Background: The functionality of myofibrillar proteins is a major factor influencing the quality attributes of muscle foods. Nonetheless, the relationships between muscle type and oxidative changes in chevon during ageing are meagrely elucidated. Postmortem changes in antioxidant status and physicochemical properties of glycolytic gluteus medius (GM) and oxidative infraspinatus (IS) muscles in goats were compared. Methods: Twenty Boer bucks (9-10 months old, body weight of $36.9{\pm}0.725kg$) were slaughtered and the carcasses were subjected to chill storage ($4{\pm}0.5^{\circ}C$). Analyses were conducted on GM and IS muscles sampled on 0, 1, 4 and 7 d postmortem. Results: Chill storage did not affect the antioxidant enzyme activities in both muscles. The IS had greater (P < 0.05) superoxide dismutase and catalase activities than GM. Carotenoid and tocopherol contents did not differ between muscles but decreased (P < 0.05) over storage. The IS had higher (P < 0.05) glycogen and ultimate pH and lower (P < 0.05) shear force and cooking loss than GM. The carbonyl content, % metmyoglobin, drip loss and TBARS increased (P <0.05) while free thiol, metmyoglobin reducing activity (MRA), shear force and myoglobin decreased (P < 0.05) over storage. Muscle type had no effect (P > 0.05) on free thiol, MRA and TBARS. The GM had lower (P < 0.05) redness on d 0 and 1 than IS while the IS had greater carbonyl, % metmyoglobin and drip loss than GM on d 7. The reflective density of slow myosin heavy chain (MHC) was higher (P < 0.05) while the density of fast MHC and actin was lower (P < 0.05) in IS than GM. Regardless of muscle type, the density of MHC decreased (P < 0.05) while that of actin was stable over storage. Nonetheless, the degradation of fast and slow MHC was greater (P < 0.05) in IS than GM. Muscle type had no effect (P > 0.05) on consumer preference for flavour, juiciness and overall acceptability. However, IS had higher (P < 0.05) tenderness score than GM on d 1 and 4 postmortem. Intramuscular fat was higher (P< 0.05) in IS compared with GM. Fatty acid composition did not differ between the muscles. However, GM had lower (P < 0.05) n-6/n-3 ratio than IS. The n-3 and n-6 PUFA declined (P < 0.05) while the SFA increased (P < 0.05) over storage. Conclusion: The changes in myofibrillar proteins and physicochemical properties of goat meat during postmortem chill storage are muscle-dependent.

• Korean Journal of Food Science and Technology
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• v.22 no.6
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• pp.640-645
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• 1990

Changes of the electrophoretic patterns of myofibrillar proteins by sugar audition and heat treatment was studied. In the electrophoretic patterns of myofibrills prepared from no sugar added meat, as the intensity of higher molecular weight band such as myosin heavy chain showed a remarkable decrease by heating, that of lower molecular weight band such as actin showed no change. That from sugar added meat showed more remarkable decrease in the intensity of higher molecular weight band than that from no sugar added meat and this tendency was most noticeable in case of glucose addition. The effect of digestion with proteases after sugar addition and heat treatment on the electrophoretic patterns exhibited the descending order of trypsin >chymotrypsin >peptidase. By digestion with these three enzymes at one time myosin produced 27.000 dalton and 32.000 dalton components, and actin showed 16,000 dalton component. in the case of heat treatment, a part of actin was not digested. And in the case of glucose addition the myosin aggregates was not digested with these three enzymes at a time.

• 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.