• Food Science of Animal Resources
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• v.34 no.5
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• pp.656-664
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• 2014

The purpose of this study was to analyze myosin heavy chain (MHC) isoforms in bovine longissimus thoracis (LT) muscle by liquid chromatography (LC) and mass spectrometry (MS). LT muscles taken from Hanwoo (Korean native cattle) steer (n=3) used to separate myosin bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The peptide queries were obtained from the myosin bands by LC-MS/MS analysis following in-gel digestion with trypsin. A total of 33 and 43 queries were identified as common and unique peptides, respectively, of MHC isoforms (individual ions scores >43 indicate identity or extensive homology, p<0.05). MHC-1 (IIx), -2 (IIa), -4 (IIb), and -7 (slow/I) were identified based on the Mowse score (5118, 3951, 2526, and 2541 for MHC-1, -2, -4, and -7, respectively). However, more analysis is needed to confirm the expression of MHC-4 in bovine LT muscle because any query identified as a unique peptide of MHC-4 was not found. The queries that were identified as unique peptides could be used as peptide markers to confirm MHC-1 (14 queries), -2 (8 queries), and -7 (21 queries) in bovine LT muscle; no query identified as a unique peptide of MHC-4 was found. LC-MS/MS analysis is a useful approach to study MHC isoforms at the protein level.

• Food Science of Animal Resources
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• v.35 no.4
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• pp.533-540
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• 2015

The aim of this study was to investigate the effects of aqueous extract from Sarcodon aspratus on tenderization of the bovine longissimus dorsi muscles in comparison with commercial proteolytic enzymes. Furthermore, meat quality and muscle protein degradation were examined. We marinated meat with 2% Sarcodon aspratus extract, 2% kiwi extract, and 0.2% papain. Beef chunks (3×3×3 cm³) were marinated with distilled water (control), Sarcodon aspratus extract (T1), kiwi extract (T2) or papain (T3) for 48 h at 4℃. There were no significant differences in muscle pH and lightness between control and treated samples. T1 had the lowest redness (p<0.01), and higher cooking loss and water holding capacity than control and T2 (p<0.05). T1 and T3 exhibited lower shear force values than control (p<0.05). Total protein solubility did not differ significantly between T1 and control, but T1 had less myofibrillar protein solubility than control and T2 (p<0.001). The degradation of myosin heavy chain in T1 and T3 was observed. This degradation of myofibrillar protein suggests that Sarcodon aspratus extract could influence tenderization. These results show that aqueous extract of Sarcodon aspratus extract actively affect the tenderness of the bovine longissimus dorsi muscle.

• The Journal of the Acoustical Society of Korea
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• v.20 no.5
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• pp.76-82
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• 2001

Because the biological tissue with inhomogeneous acoustic properties does not keep a particular shape, the measurement of propagation characteristics of ultrasonic fields by the conventional scanning method with a miniature hydrophone is difficult. In this study, a two-dimensional may hydrophone was fabricated using the PVDF (Polyvinylidene fluoride) piezo-electric film and a ultrasonic field measurement system with it was established. For the acoustic field produced by a circular plan transducer with center frequency of 2.25㎒ and 13㎜ in diameter, it was possible to make a fairly accurate field measurement using the hydrophone system. The attenuation coefficients at 2.25 ㎒ for biological tissues were 0.7∼1.3 dB/cm(average; 1.0 dB/cm) in bovine liver, 1.0∼1.8 dB/cm (average; 1.6 dB/cm) in pig liver, 0.9∼2,9 dB/cm(average: 2.1 dB/cm) in bovine muscles, 1.7∼3.3 dB/cm (average; 2.5 dB/cm) in pig muscles.

• Asian-Australasian Journal of Animal Sciences
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• v.30 no.2
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• pp.254-261
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• 2017

Objective: The effects of aging and freezing/thawing sequence on color, physicochemical, and enzymatic characteristics of two beef muscles (Mm. gluteus medius, GM and biceps femoris, BF) were evaluated. Methods: Beef muscles at 3 d postmortem were assigned to four different combinations of aging and freezing/thawing sequence as follows; aging at $2^{\circ}C$ for 3 wk (A3, never-frozen control), freezing at $-28^{\circ}C$ for 2 wk then thawing (F2, frozen/thawed-only), aging at $2^{\circ}C$ for 3 wk, freezing at $-28^{\circ}C$ for 2 wk then thawing (A3F2), and freezing at $-28^{\circ}C$ for 2 wk, thawing then further aging at $2^{\circ}C$ for 3 wk (F2A3). Results: No significant interactions between different aging/freezing/thawing treatments and muscle type on all measurements were found. Postmortem aging, regardless of aging/freezing/thawing sequence, had no impact on color stability of frozen/thawed beef muscles (p<0.05). F2A3 resulted in higher purge loss than F2 and A3F2 treatments (p<0.05). A3F2 and F2A3 treatments resulted in lower shear force of beef muscles compared to F2 (p<0.05). Although there was no significant difference in glutathione peroxidase (GSH-Px) activity, F2A3 had the highest ${\beta}-N-acetyl$ glucominidase (BNAG) activity in purge, but the lowest BNAG activity in muscle (p<0.05). GM muscle exhibited higher total color changes and purge loss, and lower GSH-Px activity than BF muscle. Conclusion: The results from this present study indicate that different combinations of aging/freezing/thawing sequence would result in considerable impacts on meat quality attributes, particularly thaw/purge loss and tenderness. Developing a novel freezing strategy combined with postmortem aging will be beneficial for the food/meat industry to maximize its positive impacts on tenderness, while minimizing thaw/purge loss of frozen/thawed meat.

• Asian-Australasian Journal of Animal Sciences
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• v.33 no.10
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• pp.1642-1655
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• 2020

Objective: The aim of this study is to characterize the impact of additional electrical stimulation (AES) and various pre-rigor holding temperatures (for 3 h) on the ageing-potential of hot boned bovine M. longissimus lumborum (LL). Methods: Paired LL loins from 12 bulls were hot-boned within 40 min of slaughter, immediate AES applied and subjected to various holding temperatures (5℃, 15℃, 25℃, and 35℃) for 3 h. Results: AES did not accelerate the rate of rigor attainment, but the 3 h pre-rigor holding temperature did. Shear force values decreased as the pre-rigor holding temperatures increased. AES and holding for 3 h (at 25℃) resulted in higher water-holding capacity. Conclusion: Data confirmed that AES did not influence the various meat quality parameters in the present study, but pre-rigor holding temperature (25℃) alone or in combination with AES resulted in superior meat quality.

• Korean Journal of Veterinary Service
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• v.29 no.3
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• pp.317-330
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• 2006

This study was conducted to develop the analytical method about simultaneous determination for synthetic antimicrobials in muscle by high performance liquid chromatography - mass selective detector (HPLC- MSD). Solid phase extraction (SPE), matrix solid phase dispersion (MSPD) and liquid-liquid extraction (LLE) have been adapted as pretreatment procedures for HPLC- MSD. Among various solvent tested, methanol was chosen for extraction of synthetic antimicrobials in muscles. For the optimized response, the values of various MS parameters including fragment voltage, drying gas flow, nebulizer pressure, drying gas temperature were verified. The average recovery rates using MSPD and SPE for muscles of bovine and pork were 78.9-127.1% and 78.3-121.7%, respectively. This method was verified the satisfactory performance for fourteen synthetic antimicrobials excepting carbadox in muscle of pork as detection limit of $0.05{\mu}g/g$ on API/ES SIM mode.

• Korean Journal of Poultry Science
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• v.6 no.1
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• pp.24-30
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• 1979

1. The effects of heat stress (38$^{\circ}C$), cold stress (4$^{\circ}C$) and extreme cold stress (-20$^{\circ}C$) before slaughter on the tenderness and postmortem glycolysis if the excised chicken breast muscle were studied Heat stress significantly (p 0.05) increased the toughness of breast muscle. Though statistically not significant, cold stress also adversely affected the tenderness. The heat-stressed birds showed higher zero hr glycogen higher zero hr pH and significantly (p 0.05) love. ultimate pH then the controls. The cold-stressed birds showed intermediate values in these parameters. Highly significant correlations. were observed between shear value and each of these three parameters. Glycolysis rate ana final moisture content were minor factors which affected the muscle tenderness to a limited extent. The slightly elevated lactate-dehydrogenase and creatine phosphokinase activities in serum and breast muscle of stressed birds failed to account for any variations in tenderness. 2. Chicken breast and thigh muscles were subjected to different environmental temperatures to determine if the phenomenon of cold shortening exists in chicken muscle. For both breast and thigh muscles, minimum shortening was observed in the 4-10$^{\circ}C$t range. Muscles held at 0$^{\circ}C$ showed a slightly higher extent of shortening than at 4$^{\circ}C$; where as muscles held at above 20$^{\circ}C$ showed a severe shortening effect. It was concluded that no apparent cold shortening was detected in chicken muscle except at 0$^{\circ}C$ and even at 0$^{\circ}C$ and even at 0$^{\circ}C$ the extent of shortening was of a small magnitude compared to bovine muscles. Since high temperature induces a much greater shortening, muscle temperature must be lowered to below 20$^{\circ}C$ as early as possible to prevent excessive muse]e shortening.

• Asian-Australasian Journal of Animal Sciences
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• v.31 no.2
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• pp.218-224
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• 2018

Objective: This study evaluated the effects of different levels of protein concentrate supplementation on the growth performance of yak calves, and correlated the growth rate to changes occurring in the plasma- amino acids, -insulin profile, and signaling activity of mammalian target of rapamycin (mTOR) cascade to characterize the mechanism through which the protein synthesis can be improved in early weaned yaks. Methods: For this study, 48 early (3 months old) weaned yak calves were selected, and assigned into four dietary treatments according to randomized complete block design. The four blocks were balanced for body weight and sex. The yaks were either grazed on natural pasture (control diet) in a single herd or the grazing yaks was supplemented with one of the three protein rich supplements containing low (17%; LP), medium (19%; MP), or high (21%; HP) levels of crude proteins for a period of 30 days. Results: Results showed that the average daily gain of calves increased (0.14 vs 0.23-0.26 kg; p<0.05) with protein concentrates supplementation. The concentration of plasma methionine increased (p<0.05; 8.6 vs $10.1-12.4{\mu}mol/L$), while those of serine and tyrosine did not change (p>0.05) when the grazing calves were supplemented with protein concentrates. Compared to control diet, the insulin level of calves increased (p<0.05; 1.86 vs $2.16-2.54{\mu}IU/mL$) with supplementation of protein concentrates. Addition of protein concentrates up-regulated (p<0.05) expression of mTOR-raptor, mammalian vacuolar protein sorting 34 homolog, the translational regulators eukaryotic translation initiation factor 4E binding protein 1, and S6 kinase 1 genes in both Longissimus dorsi and semitendinosus. In contrast, the expression of sequestosome 1 was down-regulated in the concentrate supplemented calves. Conclusion: Our results show that protein supplementation improves the growth performance of early weaned yak calves, and that plasma methionine and insulin concentrations were the key mediator for gene expression and protein deposition in the muscles.

• Analytical Science and Technology
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• v.20 no.4
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• pp.347-354
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• 2007

A simple and rapid high-performance liquid chromatography assay for the determination of residual novobiocin levels in bovine, porcine, chicken, flatfish and japanese eel muscle has been developed and validated. The separation condition for HPLC/UV was optimized with phenyl hexyl ($4.6{\times}150mm$, $5{\mu}m$) column with 10 mM monobasic sodium phosphate buffer (pH 2.5)/acetonitrile (50/50, v/v) as the mobile phase at a flow rate of 1.0 mL/min and detection wavelength was set at 254 nm. Residues were extracted from tissue by blending with methanol and lipid materials were removed with n-hexane. Then, the methanol extract was evaporated to dryness under a nitrogen stream, reconstituted in the mobile phase. Aliquot of the organic extract was decanted and filtered through $0.45{\mu}m$ syringe filter. The $20{\mu}L$ of the resulting solution was injected into the HPLC system. The calibration ranges were $0.5{\sim}5{\mu}g/g$ and calibration curves were linear with coefficients of correlation better than 0.95. The limits of quantification were $0.5{\mu}g/g$ for all muscles. The recoveries of bovine, porcine, chicken, flatfish and japaneseel muscles were 99.8%, 102.4%, 91.0%, 104.0% and 93.0%, respectively. The procedures were validated according to the CODEX guideline, determining specificity, linearity, accuracy, precision, quantitation limit and recovery.

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.10
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• pp.1344-1349
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• 2004

Titin-cap (TCAP), one of the abundant transcripts in skeletal muscles, was nvestigated in this study in cattle because of its role in regulating the proliferation and differentiation of myoblasts by interacting with the myostatin gene. From the 5, and 3, RACE experiments, full-length TCAP coding sequence was identified, comprising 166 amino acids. The amino acid comparison showed high sequence similarities with previously identified human (95.8%) and mouse (95.2%) TCAP genes. The TCAP expression, addressed by northern blot, is limited in muscle tissues as indicated by Valle et al. (1997). The radiation hybrid analysis localized the gene on BTA19, where the comparative human and porcine counterparts are on HSA17 and SSC12. A few muscle-related genetic disorders were mapped on HSA17 and some growth-related QTLs were identified on SSC12. The bovine TCAP gene found in this study opens up new possibilities for the investigation of muscle-related genetic diseases as well as meat yield traits in cattle.