• Korean Journal of Fisheries and Aquatic Sciences
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• v.29 no.6
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• pp.754-760
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• 1996

Effects of washing and additives on the texture of squid surimi gel which has been known to hard to gelation due to high protease activities and many water solubles were studied by SDS-PAGE, compression test, jelly strength and transmission electron microscopy analysis (TEM). Myosin (205 kDa) heavy chain was the major protein in water soluble fractions. It was impossible to make a gel after washing of the minced squid meat. These results suggested that squid (Todarodes pacificus) minced meat does not need a washing for good jelly products. $3.0\%$ of bovine plasma protein (BPP) produced the hardest gel ($16\%$ harder than the control) among the additives including egg white (EW), potato extracts (PE) and transglutaminase-K (TG-K) by compression test (P>0.05). Microstructure of control, $2\%$ EW and $4\%$ TG-K treated gels showed a sponge-like structure with more vacant space. Gels containing $3\%$ BPP formed the most rigid and arranged networks. Those results indicates that poor gel-network formation Was due to the degradation of myofibrillar proteins by proteases contained in the minced meat, which result in non-interlinkage.

• Korean Journal of Poultry Science
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• v.25 no.2
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• pp.55-64
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• 1998

This study was carried out to investigate the postmortem changes in physico-chemical characteristics of chicken meat with different breeds. Thigh and breast meats from Korean Native Chicken(KNC, 15-wk old), Wangchoo(15-wk old), and broiler(7-wk old) were stored at 5 ˚C. Differences in postmortem pH changes were not recognized among breeds, and pH showed by the lowest value at the 1st day of postmortem in all breeds. Breast meat had tendency to drop pH faster than thigh meat. Heme pigment contents showed no differences among breeds. KNC showed the lowest cholesterol contents in all breeds, total collagen contents showed the lowest value at the 1st day of postmortem, and thereafter it was gradually increased. Heat soluble collagen contents was lowest in Wangchoo. Water soluble and salt soluble protein showed the lowest extractability at the 1st day of storage. Broiler showed the highest extractability of these proteins and Wangchoo showed the lowest. Water holding capacity(WHC) had increasing tendency whilst cooking loss had decreasing tendency by the ageing. WHC of breast and thigh meat showed the highest values in KNC and broiler, respectively. Myofibrillar fragmentation index (MFI) was significantly increased in all breeds by the ageing. Breast and thigh meat showed almost same MFI in KNC and broiler, and in KNC and Wangchoo, respectively. Hardness of breast meat showed decreasing tendency by the ageing.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.173-180
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• 1986

To investigate on the biochemical characteristics of muscle fiber, myofibrils and actomyosins were prepared front red muscle and white muscle, and their ATPase activities and SDS-polyacrylamide gel electrophoretic patterns were compared. Also biochemical characteristics of bovine muscle were compared with those of chicken muscle for the detection of species characteristics. SDS-polyacrylamide gel electrophoretic analysis indicated that red muscle contained nlore 30K component of myofibril than white muscle. Differences in KCI concen-tration dependency of actomyosin ATPase activities and ATPase activity-pH cone were observed, when bovine muscle were compared with chicken muscle.

• Food Science of Animal Resources
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• v.42 no.5
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• pp.723-743
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• 2022

Beef muscles from mature cows and bulls, especially those originating from the extremities of the carcass, are considered as underutilized due to unsatisfactory palatability. However, beef from culled animals comprises a substantial proportion of the total slaughter in the US and globally. Modern consumers typically favor cuts suitable for fast, dry-heat cookery, thereby creating challenges for the industry to market inherently tough muscles. In general, cull cow beef would be categorized as having a lower extent of postmortem proteolysis compared to youthful carcasses, coupled with a high amount of background toughness. The extent of cross-linking and resulting insolubility of intramuscular connective tissues typically serves as the limiting factor for tenderness development of mature beef. Thus, numerous post-harvest strategies have been developed to improve the quality and palatability attributes, often aimed at overcoming deficiencies in tenderness through enhancing the degradation of myofibrillar and stromal proteins or physically disrupting the tissue structure. The aim of this review is to highlight existing and recent innovations in the field that have been demonstrated as effective to enhance the tenderness and palatability traits of mature beef during the chilling and postmortem aging processes, as well as the use of physical interventions and enhancement.

• Food Science of Animal Resources
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• v.43 no.5
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• pp.877-888
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• 2023

We studied the proteolysis and conducted a sensory evaluation of fermented sausages using strains derived from Kimchi [Pediococcus pentosaceus-SMFM2021-GK1 (GK1); P. pentosaceus-SMFM2021-NK3 (NK3)], Doenjang [Debaryomyces hansenii-SMFM2021-D1 (D1)], and spontaneous fermented sausage [Penicillium nalgiovense-SMFM2021-S6 (S6)]. Fermented sausages were classified as commercial starter culture (CST), mixed with GK1, D1, and S6 (GKDS), and mixed with NK3, D1, and S6 (NKDS). The protein content and pH of GKDS and NKDS were significantly higher than those of CST on days 3 and 31, respectively (p<0.05). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the NKDS had higher molecular weight proteins than the GKDS and CST. The myofibrillar protein solubility of the GKDS and NKDS was significantly higher than that of the CST on day 31 (p<0.05). The GKDS displayed significantly higher pepsin and trypsin digestion than the NKDS on day 31 (p<0.05). The hardness, chewiness, gumminess, and cohesiveness of the GKDS were not significantly different from those of the CST. The GKDS exhibited the highest values for flavor, tenderness, texture, and overall acceptability. According to this study, sausages fermented using lactic acid bacteria (GK1), yeast (D1), and mold (S6) derived from Korean fermented foods displayed high proteolysis and excellent sensory evaluation results.

• Journal of Animal Science and Technology
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• v.65 no.6
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• pp.1151-1168
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• 2023

Tenderness and taste characteristics of meat are the key determinants of the meat choices of consumers. This review summarizes the contemporary research on the molecular mechanisms by which postmortem aging of meat improves the tenderness and taste characteristics. The fundamental mechanism by which postmortem aging improves the tenderness of meat involves the operation of the calpain system due to apoptosis, resulting in proteolytic enzyme-induced degradation of cytoskeletal myofibrillar proteins. The improvement of taste characteristics by postmortem aging is mainly explained by the increase in the content of taste-related peptides, free amino acids, and nucleotides produced by increased hydrolysis activity. This review improves our understanding of the published research on tenderness and taste characteristics of meat and provides insights to improve these attributes of meat through postmortem aging.

• Biomedical Science Letters
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• v.13 no.4
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• pp.251-261
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• 2007

A myofiber of skeletal muscle is composed of myofibrils, sarcolemma (plasma membrane), and constameres, which anchor the myofibrils to the sarcolemma. Achvillin is a recently identified F-actin binding muscle protein, co-isolates with dystrophin and caveolin-3 in low-density sarcolemma of striated muscle, and colocalizes with dystrophin at costameres, the specialized adhesion sites in muscle. Archvillin also binds to nebulin and localizes at myofibrillar Z-discs, the lateral boundaries of the sarcomere in muscle. However other roles of archvillin on the dynamics of myofibrillogenesis remain to be defined. The goal of this study is, by using siRNA-mediated gene silencing technique, to investigate the effect of archvillin on the dynamics of myofibrillogenesis in cell culture of a mouse skeletal myogenic cell line (C2C12), where presumptive myoblasts withdraw from the cell cycle, fuse, undergo de novo myofibrillogenesis, and differentiate into mature myotubes. The roles of archvillin in the assembly and maintenance of myofibril and during the progression of myofibrillogenesis induced in skeletal myoblast following gene silencing in the cell culture were investigated. Fluorescence microscopy demonstrated that the distribution of archvillin was changed along the course of myofibril assembly with nebulin, vinculin and F-actin and then located at Z-lines with nebulin. Fluorescence microscopy demonstrated that knockdown of mouse archvillin expression led to an impaired assembly of new myofibrillar clusters and delayed fusion and myofibrillogenesis although the mouse archvillin siRNA did not affect those expressions of archvillin binding proteins, such as nebulin and F-actin. This result is corresponded with that of RT-PCR and western blots. When the perturbed archvillin was rescued by co-transfection with GFP or Red tagged human archvillin construct, the inhibited cell fusion and myotube formation was recovered. By using siRNA technique, archvillin was found to be involved in early stage of myofibrillogenesis. Therefore, the current data suggest the idea that archvillin plays critical roles on cell fusion and dynamic myofibril assembly.

• Asian-Australasian Journal of Animal Sciences
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• v.33 no.3
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• pp.501-505
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• 2020

Objective: The purpose of this study was to investigate the effects of aging methods (AM) i.e. dry-aging (DA) and wet-aging (WA) on the physicochemical properties and in vitro digestibility of proteins in beef short loin. Methods: Short loins (M. longissmus lumborum), were trimmed and boned-out on the fifth day postmortem, from a total of 18 Hanwoo, which were purchased from a commercial slaughterhouse. Short loins were separated randomly grouped into one of the three treatments: control, WA (1℃, 7 days), and DA (1℃, 0.5 m/s, 85% relative humidity [RH], 30 days). Results: Dry-aged beef (DAB) exhibited higher pH, water holding capacity (WHC), myofibrillar fragmentation index (MFI), and digestibility, however lower lightness, redness, and yellowness values, cooking loss, and shear force (SF), than those of wet-aged beef (WAB) (p<0.05). The myosin light chain band intensity of DAB was higher than that of control and WAB in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The in vitro digestibility of aged beef was highly (p<0.001) correlated to physicochemical properties except WHC. The correlation coefficient between AMs and WHC was higher than that between AM and SF (p<0.05) or MFI (p<0.001). A high correlation was observed between SF and MFI (p<0.001). Conclusion: Thus, we believe that DAB is more advantageous than WAB owing to its high digestibility and WHC and low SF.

• Asian-Australasian Journal of Animal Sciences
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• v.21 no.6
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• pp.903-911
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• 2008

The effects of salt and bicarbonate solution on overall meat quality in beef biceps femoris muscle were investigated with the application of chilling and freezing conditions. Muscles were injected to a target of 120% of original meat weight with a solution containing 1.2 M sodium chloride, 0.25 M sodium bicarbonate and 0.1% ascorbic acid (pH 7.2). Half of the meat samples, considered as chill treatment and chill control, were stored at $4^{\circ}C$ up to five days; while the other half, frozen treatment and frozen control, were kept in a freezer at $-20^{\circ}C$ for seven days. Compared with untreated control, treated meats had higher water holding capacity (p<0.05), lower drip loss (p<0.05) and lower shear force (p<0.07) with higher overall acceptability (p<0.05) in sensory evaluation. Morphological observations demonstrated smooth and gummy meat surface due to the solubilization of myofibrillar proteins and the distortion of connective tissue in treated raw meats; and in the case of cooked meat, treatment caused the fragmentation of myofibrils, which might be responsible for a lower shear value in salt-bicarbonate treated beef biceps femoris muscle.

• Journal of Ginseng Research
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• v.28 no.1
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• pp.18-26
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• 2004

The effect of Panax ginseng administration in muscle inflammatory process induced after eccentric exercise, that causes myofibrillar disruption, was studied. Changes in lipid peroxidation, inflammation, glycogen levels in muscle and release of myocellular proteins to blood were measured. The analyses were performed immediately after eccentric exercise and over week since this period are necessary for the muscle damage-repair cycle. The ginseng extract (100 mg kg$^{-1}$ ) was orally administered to rats for three months, before the eccentric exercise performance. The results showed the protective role of ginseng against skeletal muscle damage. This effect could be associated with their membrane stabilising capacity since creatine kinase (CK) activity was significantly decreased 96 h post-exercise from 523$\pm$70 to 381$\pm$53 and 120 h post-exercise from 443$\pm$85 to 327$\pm$75 in treated animals. $\beta$-glucuronidase activity, as indicator of inflammation, showed a significant reduction of about 15-25% in soleus, vastus and triceps in these post-exercise times. The lipid peroxidation, measured by malondyaldehyde levels, was significantly decreased in the 24 h post-exercise period in soleus and vastus intermedius muscles and on the recovery period. Finally ginseng administration reduced significantly the decrease of the glycogen levels immediately after exercise and when the regenerative process took place (72-168 h post exercise). Collectively, the results have showed that ginseng did not inhibit the vital inflammatory response process associated with the muscle damage-repair cycle but presumably ameliorate the injury.