• 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.

• Food Science of Animal Resources
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• v.27 no.4
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• pp.457-462
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• 2007

Effects of sonication on water-solubilization of myofibril from breast muscle of spent hen effects investigated in this study. To evaluate effect of salt concentration and pH, salt concentration was varied with range from 0.1 to 0.8 M, and pH was varied with range from 6.0 to 8.0. Solubility, SDS-PAGE, viscosity and ATPase activity of sonicated myofibril were measured. Solubility of myofibrillar protein containing 0.1 M NaCl at pH 8.0 after sonication was above 90%. Main components of soluble protein by SDS-PAGE were myosin heavy chain and actin. That is, it indicated breaking of myofibril structure by sonication. Also, viscosity of soluble protein increased, but Ca- and Mg-ATPase activities decreased by increasing sonication time. From these results, we concluded that most of myofibrillar proteins were denatured by sonication.

• Food Science of Animal Resources
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• v.23 no.2
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• pp.122-127
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• 2003

A surimi like material was made from fresh pig hearts and used to manufacture emulsion-type sausages for the improvement of quality characteristics. The heart muscles were diced and frozen at -60$^{\circ}C$ until processed. Then, the frozen diced heart muscles were thawed, chopped, filtered, and washed to extract myofibrillar proteins. The residue was centrifuged to take a surimi-like material. Emulsion-type sausages were made different levels of surimi-like material(5∼15%) and compared to the control. Cooking loss(CL, %) and water-holding capacity (WHC, %) were measured on raw meat batter, whereas shear force, hardness, color and panel test were measured after cooking. The addition of the surimi-like material up to 15% level in the sausage formulation reduced CL and increased WHC, as compared to the control. Shear force and hardness values of the control had the highest value, however sausages containing 15% surimi-like material had the lowest value(p<0.05). Increased surimi-like material became darker in color. Although no differences in panel scores of flavor and off-flavor were observed, panellists prefer to select sausages having 15% surimi-like material(p<0.05). These results indicated that a surimi-like material, which was a myofibrillar protein extracted from pig hearts, could be used to manufacture emulsion-type sausage up to 15% to improve cooking yield and textural characteristics without color and flavor defects.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.16 no.3
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• pp.190-196
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• 1983

This experiment was carried out to compare the change of muscle protein compositions, amino acid compositions of muscle protein, and free amino acid compositions by age of the Israeli strain of common carp, Cyprinus carpio nudus. Protein compositions of the muscle were: sarcoplasmic protein $25.8-27.2\%$, myofibrillar protein $62.3-56.2\%$, residual intracellular protein $9.6-13.2\%$ and stroma $2.3-2.9\%$. In between 1 year and 3 years, there were differences as follows; myofibrillar protein in 1 year was much than 3 years, and other proteins in 3 years were much than 1 year. By SDS-polyacrylamide gel electrophoresis, sarcoplasmic protein of the samples in 1 year an 3 years were composed of 11 subunits and 10 subunits, respectively. And appeared 210,000 dalton component in 1 year but did not appeared in 3 years. Myofibrillar protein was composed of 23 subunits in both 1 year and 3 years but the differences of subunits by age were not observed. No differences were observed by age in the composition of myofibrillar protein and residual intracellular protein. Amino acid composition of muscle protein in both 1 year and 3 years were no differences to each other, but the contents of glutamic acid, aspartic acid, lysine were higher than other amino acids. The amount of total free amino acid in 1 year was much than in 3 years.

• Biomedical Science Letters
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• v.9 no.4
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• pp.231-240
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• 2003

Deciphering the molecular interactions of proteins forming Z-lines is pivotal for understanding the regulation of myofibril assembly, sarcomeric organization, and mechanical properties of striated muscle. The purpose of this study is to searched for potential novel ligands of the Z-line portion of nebulin. In this study interacting proteins with intra-Z-line region of nebulin were screened using a yeast two-hybrid approach. The interaction was conformed by GST pull-down assay. We identified 269 residues within villin/gelsolin homology domain of supervillin that intreacts with the serine rich region of nebulin. The specific interactions of nebulin and supervillin were confirmed in vitro by GST pull-down experiments. Our data suggest that supervillin attaches directly to the Z-line through its interaction with the serine rich domain of nebulin in skeletal muscles. This interaction may link myofibrillar Z-discs to the membrane-associated complexes, costameres.

• Journal of Animal Science and Technology
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• v.63 no.2
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• pp.405-416
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• 2021

The aim of the study was to determine the effect of whole milk powder (WMP) as heterologous proteins on chicken breast emulsion-type sausages. The quality properties of WMP on such chicken breast emulsion-type sausages were investigated by measuring the proximate composition, pH, color, cooking yield, protein solubility, and by applying other methods, such as texture profile analysis (TPA), microphotograph, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and electronic nose. The crude fat, protein, and ash contents of 15% WMP samples were significantly higher than the control samples (p < 0.05). The redness of the cooked samples significantly increased with an increase in the WMP contents (p < 0.05). The cooking yield of WMP treated samples was significantly higher than the control sample (p < 0.05). Additionally, the hardness, gumminess, and chewiness of WMP treated samples were significantly higher than the control sample (p < 0.05). The sarcoplasmic and myofibrillar proteins of samples containing 15% WMP were significantly higher than the control samples (p < 0.05). The result of SDS-PAGE showed that the C protein, sarcoplasmic protein, actin, and tropomyosin increased with an increase in the WMP contents. The principal component analysis plot of WMP-treated samples was clearly different from that of the control samples. Based on these results, it was predicted that WMP could be useful as heterologous protein on emulsion-type sausage.

• Food Science of Animal Resources
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• v.42 no.2
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• pp.266-279
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• 2022

This study was conducted to evaluate the proteolysis trends and change in meat quality during 10 days of cold storage in duck M. pectoralis major (PM) and M. iliotibialis (IL). Duck IL had a higher pH and greater degree of lightness but lower cooking loss than PM (p<0.05). During the 10-day cold storage, the pH value of PM declined significantly (p<0.05), while the meat quality traits of IL were not affected by cold storage (p>0.05). In PM, the redness increased from day 1 to day 5, while cooking loss was lower on day 10 compared to day 5 (p<0.05). There were no significant differences in the activities of cathepsin B and proteasome 20S during cold storage (p>0.05). The activity of calpains declined gradually during 10 days of storage (p<0.05), and the activity of calpains in PM was higher than that in IL (p<0.05). A total of 5,155 peptides were detected and derived from 34 proteins of duck PM muscle, whereas 4,222 peptides derived from 32 proteins were detected from duck IL muscle. Duck PM muscle was composed only of fast type of muscle fiber, whereas IL muscle was composed of both slow and fast types. The proteins responsible for glycolysis or myofibrillar proteins were closely related to changes in meat color or water-holding capacity during cold storage. These results suggest that changes in meat quality characteristics during cold storage are closely related to protein degradation, which is also related to the distribution of muscle fiber types.

• 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 $61.96{\pm}7.41%$.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.1
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• pp.60-66
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• 1986

The muscles of wild and cultured eel, Anguilla japonica, were analyzed for the protein composition and amino acid profile. The differences of the subunit distribution for the sarcoplasmic and myofibrillar proteins were discussed with sodium dodecylsulfate(SDS) polyacryamide gel electrophoresis. The muscle protein in wild eel was composed of $30.78\%$ of sarcoplasmic, $59.02\%$ of myofibrillar, $9.73\%$ of residual intracellular and $2.47\%$ of stroma fraction. That in cultured eel was composed of $31.81\%,\;58.37\%,\;8.16\%\;and\;1.80%$, respectively, The sarcoplasmic and myofibrillar proteins were composed of 16 and 14 subunits in wild eel, and 22 and 15 subunts in cured eel. The sarcoplasmic protein between wild and cultured muscles showed a similar trend in the subunits, except a few subunits such as 36,500, 46,000, 58,500, 75,000, 170,000 and 235,000 daltons in cultured eel. Only the existence of 45,000 dalton subunit was the difference between wild and cultured eel in myofibrillar protein. The distribution patterns of total amino acid in muscles of wild and cultured eel were found to be very similar trend, although glycine content in wild eel was slightly higher than that in cultured one.

• Korean Journal of Environmental Biology
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• v.33 no.1
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• pp.7-18
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• 2015

In this study, we studied the effect of dissolved cement powder on Carassius auratus by analysis of the morphophysiological changes. The gill exposed to dissolved cement powder showed the thickened primary lamellae and the activity of chloride cells and mucous cells was also significantly increased and the proliferation, separation and clubbing of gill filament was observed in the secondary lamellae. In the kidney tissue, the space in Bowman's capsule was widen and the arrangement of dermis was irregular due to the thinned epidermis in the integument tissue. The activities of antioxidant enzymes and LDH tended to increase with the duration of cement exposure. It was confirmed that the up-regulated proteins were identified as involved in glycolysis and energy metabolism and down-regulated proteins were myofibrillar proteins which were involved in muscle contraction by the cement exposure to the integument. With these results, dissolved cement powder was thought to be a big threat to the survival of the fish because it causes the morphological changes and weakens the physiological activity in C. auratus tissues.