• Food Science of Animal Resources
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• v.44 no.5
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• pp.1055-1068
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• 2024

The differences in the proteolytic patterns and shear force of pork and beef during aging were evaluated. Pork and beef semitendinosus muscles were obtained at 24 and 48 h postmortem, respectively, and aged at 4℃ for 0 (Day 0), 7 (Day 7), and 14 days (Day 14). Changes in the electrical conductivity were observed in pork on Day 7 and beef on Day 14. The calpain activity increased in pork (p<0.05) after 14 days of aging, whereas that of beef decreased on Day 7 (p<0.05). The cathepsin B activity in pork and beef increased between Day 7 and 14 (p<0.05). The content of α-amino group in the 10% trichloroacetic acid-soluble fraction increased between Day 7 and 14 in pork (p<0.05), but increased steadily in beef throughout aging (p<0.05). The electrophoretogram of the myofibrillar proteins revealed a 30 kDa protein band only in the beef lane on Day 14. The cooked pork had no significant changes in the shear force during aging periods (p>0.05), while the gradual decrease in the shear force with the increasing aging periods was shown in the cooked beef (p<0.05). Circular dichroism analysis of myosin extracts from pork and beef revealed thermal denaturation temperatures of 55℃ and 58℃, respectively. This study highlights the different post-mortem proteolytic patterns and thermal denaturation temperatures of myosin in pork and beef semitendinosus muscles, which contribute to distinct changes in the shear force during aging between pork and beef.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.2
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• pp.73-78
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• 1992

To investigate the desirable index for evaluation of frozen surimi's grades, the relationship between indices for grading of surimi, such as ATPase activity $(Ca^{2+}-,\;Mg^{2+}-\;and\;EDTA-)4, solubility, viscosity and K-value of frozen surimi and jelly strength of kamaboko was studied. The myofibrillar $Ca^{2+}-ATPase$ activity and solubility from frozen surimi of grades SA, FA, A, RA and B gave values of $1.184\pm0.2,\;0.956\pm0.14,\;0.766\pm/0.07,\;0.453\pm0.07\;and\;0.227\pm0.08$(umoles Pi/min/mg) for $Ca^{2+}-$ATPase activity and $93.19\pm5,\;84.62\pm4,\;70.63\pm5,\;41.21\pm4\;and\;32.82\pm4(\%)$ for solubility, respectively. Therefore, the myofibrillar $Ca^{2+}-$ATPase activity and solubility of surimi were closely related to the jelly strength of kamaboko from same material, as the correlation coefficient were 0.9584 and 0.9849, respectively. K-value, the index of freshness, was related to the jelly strength of frozen surimi as the correlation coefficient 0.9053 and shown as SA $15.67\pm1.4,\;FA\;14.94\pm 3,\;A\;28.00\pm5,\;RA\;32.16\pm3\;and \;B\;48.68\pm 5(\%)$. $Mg^{2+}-$ and EDTA-ATPase activity and viscosity were not related to the jelly strength. The $Ca^{2+}-$ATPase activity and solubility were found to be useful index for evaluating the quality of frozen surimi.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.5
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• pp.493-501
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• 1986

The present work aims to estimate the effect of heat treatment on the in vitro protein digestibility and formation of trypsin inhibitor or trypsin indigestible substrate(TIS) of raw and defatted flounder. It was also carried out to assess the formation of lipid-protein complexes under the conditions of different ratio of lipid addition. The in vitro protein digestibility increased when steamed for 5 min showing $88.09\%$ in raw and $90.56\%$ in defatted samples, respectively. After 40 min steaming, the digestibility decreased by $2{\sim}4\%$. As for microwaving, heating for 1 min resulted in slight increase of digestibility, however, heating for 7 min did decrease of digestibility by $3{\sim}4\%$ for both raw and defatted materials. There was no difference in fatty acid composition found with heat treatment. The major fatty acids of flounder meat were $C_{16:0},\;C_{16:1},\;C_{18:1},\;C_{20:5},\;C_{22:6}$ and the ratio of the unsaturated to saturated was 67.3:32.6. Fat oxidation and nonenzymatic browning were enhanced by heat treatment and protein solubility decreased necessarily as the brown pigment formation increased. On the other hand, the effects on the digestibility and TIS of the complexes formed from interaction of lipid and myofibrillar or meat protein of flounder were examined. The interaction of protein with lipid was considered to mostly contribute to the drop of digestibility of fish products. The digestibility of myofibrillar protein was $93.72\%$ for flounder, and it generally decreased as the amount of lipid added to protein and reaction time increased. Also mixed and heated samples were more active in digestibility decline than those mixed after heating. The result probably indicated that lipid-protein interaction was involved in the drop of digestibility which coincided with protein denaturation.

• The Korean Journal of Food And Nutrition
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• v.16 no.3
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• pp.209-217
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• 2003

The composition of muscle proteins and free amino acids in the mudskipper (hibernant fish) were investigated before and after hibernation (maturity period: August, hibernation period: November thru. April). It was found that crude proteins were 17.6% in August, 17.5% in November and 16.9% in April, while among the muscle proteins, sarcoplasmic proteins were constituted up to 19.2～20.4%, 58.8～61.3% for myofibrilla proteins, 11.2～13.2% for intracellular proteins and 7.5～8.3% for stroma proteins. Composition changes of the muscle proteins were hardly noted until November but during the hibernation(from Nov. to Apr.) the amount of the sarcoplasmic proteins and the myofibrillar proteins decreased pronouncedly. As for the sarcoplasmic proteins, 14 subunits were found and among them, the amount of 30 kDa and 46 kDa subunits were found to increase slightly in April compared with those in November, while the amount of 35 kDa and 65 kDa subunits were decreased slightly. As for the myofibrilla proteins, 13 subunits were found and detectable changes in their composition were not observed until November but in April the amount of myosin heavy chain was increased by 3%, while the amount of actin decreased by 3% when those are compared with the results in November. The composition of amino acids in the muscle proteins was hardly changed during the observation period. But there were considerable changes of composition of free amino acids. Glycine and alanine were found to be the major free amino acids. The most striking feature was the changes in the glycine and arginine content: the former, which is a dominant free amino acid, was increased by two-fold in April compared with that in August and the latter was increased by two-fold in November and by four-fold in April. It was also found that the amount of essential amino acids (i.e., lysine and histidine) and others (alanine, glutamic acid, serine, aspartic acid and valine) increased significantly during the hibernation period.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.18 no.5
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• pp.401-408
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• 1985

In order to develop new types of product which can offer a sanitary and preservative duality, and convenience to consumers in marketing and cooking particularly in urban area, two processing methods of ready-to-cook food materials with dark fleshed fishes like sardine and mackerel were investigated. A method applied, in this work, is processing of ready-to-cook sardine meat "surimi" in which sardine meat is treated with alkaline solution to stabilize myofibrillar proteins, washed thoroughly with water to remove soluble components, and added with a proper amount of polyphosphate and sorbitol to enforce the functional property of meat such as water holding capasity, elasticity, and gel strength. The textural properties of fish meat paste made from the "surimi" meat were greatly dependent upon the stability of myofibrillar proteins and the elimination of water soluble components. The salt soluble proteins of sardine meat were so unstable in post-mortem stage that the gel forming ability was lost within 3 days at $5^{\circ}C$ storage and 2 to 3 weeks even at $-20^{\circ}C$ although the freshness was well kept for a week at $5^{\circ}C$ and several months of storage at $-20^{\circ}C$. A proper way of treatment to keep the proteins stable was that fish meat must be washed with $0.4\%$ sodium bicarbonate solution followed by 3 to 4 times washing with water. This resulted in removal of $80\%$ water soluble proteins and 50 to $60\%$ lipids. The addition of polyphosphate and sorbitol affected the stability of proteins during the storage of "surimi" meat. When phosphate and sorbitol were added in the ratio of $0.3\%:\;0.3\%,\;0.6\%:\;3\%,\;0.6\%:\;6\%,\;0:\,0.3\%\;and\;0.3\%:\;0$, the gel forming ability terminated in 35 days, 21 days, 14 days, 14 days, and 14 days of storage at $-30^{\circ}C$, respectively, while that of the control was 7 days. And it was also noteworthy that at least 8.0 mg/g of salt soluble protein nitrogen content was required for gel formation.

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.229-237
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• 1975

An attempt was made to utilize the enzyme produced by Asp. oryzae as meat tenderizer. The production, purification, and various properties of proteinase produced by Asp. oryzae were investigated. Results obtained are as follow; 1. A strain which had the highest proteolytic activity was selected among 9 Aspergillus species. 2. Culture medium consisted of wheat bran 10g, 2% glucose, 0.03% urea and 0.1% $MgSO_4$ (pH 6.5). Mold was incubated at $30^{\circ}C$ for 3 days. 3. Enzyme extract from culture medium were fractionated with ammonium sulfate and purified by Sephadex G-75 column chromatography. 4. When pH of reaction mixture was controlled, maximal activity of proteinase by Asp. oryzae was obtained at pH 3, pH 6.6, $8.4{\sim}8.5$ and pH 10.0 to 10.5. Those results were interpreted to show that enzyme consists of acid proteinase, neutral proteinase and alkaline proteinase. Enzyme was stable at pH 6 to 10. 5. Opt. temperature for proteinase activity was $50^{\circ}C$, but enzyme was stable up to $40^{\circ}C$. 6. The proteinase was inhibited by $Ag^+$. It was also inhibited by EDTA. 7. When myofibrillar proteins were treated by proteinase from Asp. oryzae, ATPase activities of myofibrillar proteins changed remarkably. Accordingly, it was concluded that proteinase produced by Asp. oryzae were able to be used as meat tenderizer.

• Food Science of Animal Resources
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• v.33 no.1
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• pp.119-124
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• 2013

This study was conducted to investigate meat quality and sensory characteristics between castrated and non-castrated dairy goats. Dairy goat of Saanen breeds was slaughtered at an age of 6 mon. Then, characteristics of dairy goat meat were analyzed to chemical compositions, collagen content, pH, meat color, cooking loss, water-holding capacity, shear force, protein solubility, and myofibrillar protein fractions by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Also, odor from dairy goat meats was analyzed by sensory evaluation and volatile substances by gas chromatography-mass spectrometry (GC-MS). As a result, the chemical compositions and physicochemical characteristics were not significantly different between castrated and non-castrated dairy goats meat. Also, there is no difference protein solubility (sarcoplasmic, myofibrillar and total protein) and protein fraction by SDS-PAGE. Sensory evaluation results in odour scores are highly (p<0.05) non-castration dairy goat meat better than castration. As a result, overall palatability was higher (p<0.05) in castrated goat meat when compared with non-castrated one. The indole and octadecanoic acid by GC-MS based on sensory evaluation results were only detected in non-castrated dairy goat meat. Therefore, distribution for goat meats castrated compared to non-castrated dairy goat meat is expected to be able to get a good response to the Korean consumer.

• Food Science and Preservation
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• v.31 no.3
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• pp.423-432
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• 2024

In this study, a vacuum tumbler with 4 impellers (DVT) was designed and applied for thawing frozen pork (vacuum -60 kPa, jacket 35℃, 1 rpm). Quality characteristics of the thawed pork were compared with those of industrially thawed meat by natural air at room temperature (NAT) and imported vacuum tumbler (IVT). The thawing time for frozen pork (303.36 kg) using DVT (165 min) was much shorter than that of NAT (4,200 min). DVT-thawed pork had lower drip loss (0.85%) than NAT (2.08%). DVT-thawed pork showed a pH of 5.92, a total bacterial count of 1.96±0.02 log CFU/g and no coliforms. Deteriorations in fat (TBARS 0.31±0.01 MDA mg/kg) and protein (VBN 5.67±1.98 mg%) in DVT-thawed pork were significantly lower than those of NAT (p<0.05). DVT-thawed pork had a high water-holding capacity (WHC, 97.5%). The hardness (34.59±0.46 N) and chewiness (188.21±0.17) of cooked DVT-thawed pork were about 5-6 times lower than those of NTA. Microstructure (SEM) showed myofibrillar damage in NAT-thawed pork, whereas dense myofibrillar structure was observed in DVT-thawed pork. DVT was better or similar to IVT in all evaluation parameters. The designed DVT is expected to be used as an efficient thawing method in terms of processing time and yield and to produce thawed meat with high WHC, soft texture, and low spoilage by minimizing tissue damage.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.1
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• pp.82-87
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• 1985

Some biological activities showed as ATPase activity of myofibril, actomyosin and myosin extracted from chicken leg and pectoral skeletal muscle were investigated. The $Mg^{+2}$-ATPase activity at 0.05 M KCl were 0.82, 0.38 and 0.11 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle while 0.71, 0.32 and 0.08 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from leg muscle. EDTA-ATPase activity at 0.6M KCl were 0.80, 0.42 and 0.40 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle. In case of leg muscle, that activity was noted as 0.69, 0.33 and 0.28 ${\mu}mole$e Pi/mg protein/min in proteins. ATPase activity of myosin from leg and pectoral muscle were inhibited in 10% at a higher concentration of $Mg^{+2}$ than molar concentration of EDTA, and the ATPase activity was increased to 400% compared with control at $10^{-3}M$ of $Ca^{+2}$. Actomyosin from pectoral muscle was solubilized at 0.1 M KCl above and that from leg muscle was solubilized at 0.15 M KCl above. In case of myosin, pectoral muscle was solubilized at 0.25M KCI above and leg muscle was solubilized at 0.30M KCl above.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.1
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• pp.77-81
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• 1985

It was investigated about extractability and biological property(ATPase activity) of actomyosin from skeletal muscle of chi(:ken differed feeding period. The extractabilities of actomyosin from pectoral muscle were increased from 184.5 to 1020.1 mg per 100g muscle as feeding period prolonged from 3 weeks to 8 weeks. In case of leg-muscles, extractability was revealed the similar tendency as pectoral muscles. EDTA ATPase activity of actomyosin in various chicken muscles for 3 weeks feeding was 0.6 Brmole Piimg Protein/min., 0.59 for 6 Iveeks feeding and 0.50 for 8 weeks. The Ma^{+2}$-ATPase of actomyosin in various chicken muscles was showed inverted relationship with ionic strength. EGTA ($125\;{\mu}mole$)inhibited Ma^{+2}$-ATPase activity to below $0.1\;{\mu}mole$ Pi/mg protein/min. regardless the feeding period.