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Bovine Muscles (bovine + muscle)
Selected AbstractsProtein Denaturation and Structural Damage During High-Pressure-Shift Freezing of Porcine and Bovine MuscleJOURNAL OF FOOD SCIENCE, Issue 6 2000F. Fernández-Martín ABSTRACT: Pork and beef muscles were subjected to 200 MPa and ,20 °C with or without water freezing. Both tissues responded to the treatment with similar behavior. Protein denaturation was greater when freezing occurred. Pressure-induced cold denaturation was complete for actin and very considerable for myosin and other muscle proteins. Connective proteins remained practically unaltered by pressurization and/or freezing. Structural changes in the muscle at sarcomere levels caused by pressurization were more severe when freezing occurred. Color, drip loss, and textural properties on the pressurized samples also revealed an additional deleterious influence of freezing. Pressurization alone and pressure-shift freezing resulted unsuitable for muscle preservation. [source] Adiposity, fatty acid composition, and delta-9 desaturase activity during growth in beef cattleANIMAL SCIENCE JOURNAL, Issue 5 2006Stephen B. SMITH ABSTRACT Oleic acid (18:1n-9) is the most abundant fatty acid in bovine adipose tissue. Because most of the lipid in bovine muscle is contributed by intramuscular adipocytes, oleic acid also is the predominant fatty acid in beef. In many species, the concentration of oleic acid in adipose tissue is dictated by the average concentration of oleic acid in the diet, but in ruminant species such as beef cattle, oleic acid is hydrogenated largely to stearic acid by ruminal microorganisms. In these species, the concentration of oleic acid in adipose tissue is dependent upon the activity of ,9 desaturase, encoded by the stearoyl coenzyme A desaturase (SCD) gene. Expression of the SCD gene is essential for bovine preadipocyte differentiation, and desaturase gene expression and catalytic activity increase dramatically as adipose tissue mass increases after weaning. Feeding a hay-based diet to American Wagyu steers to a typical Japanese bodyweight endpoint (650 kg) markedly stimulated desaturase enzyme activity as well as the accumulation of both oleic acid and intramuscular lipid, but the increase in oleic acid and intramuscular lipid was much less in hay-fed Angus steers. Increasing the concentration of oleic acid improves the palatability and healthiness of beef, and Korean Hanwoo and Japanese Black (and American Wagyu) seem especially well adapted to accumulate oleic acid in their adipose tissue. [source] Residues from anabolic preparations after good veterinary practice,,APMIS, Issue 4 2001D. M. Henricks The purpose of this study was to determine the endogenous concentrations of estrogens, particularly estradiol-17, (E2,), in edible tissues of beef cattle (females and intact and neutered males) and the concentrations of E2,, and trenbolone beta and alpha (,Tb, ,Tb) after an E2, and/or trenbolone acetate (TA) ear implant. Radioimmunoassays were validated for quantitation of E2, (active isomer), E2,, estrone (E1), ,Tb and ,Tb for bovine muscle, liver, kidney and fat tissues. The criteria of accuracy, precision, specificity and sensitivity were applied according to the standards of the U.S. Food & Drug Administration. In steer tissues, endogenous E2, was <15 ppt, as was heifer muscle; but heifer liver and kidney were 3-fold greater. An E2, implant in steers had no effect on muscle E2, concentration, but increased E2, in liver and fat 4- and 3-fold, respectively, but by 24 h post-implant removal, E2, had fallen by half. Tissue E1 concentrations in cyclic females were similar to E2,, but rose many fold greater than did E2, during gestation; E2, rose 3-fold during gestation. After E2,/TA implant, steer tissues had E2, concentrations equal to (for muscle and fat) and one-half (for liver) the E2, measured in E2, implant only steers; ,Tb was in a low range (250,380 ppt) in muscle, liver and fat and ,Tb was even lower, except in liver (800,1500 ppt). An implant of TA only (no E2,) resulted in ,Tb and ,Tb concentrations 2,3-fold greater in liver, kidney and fat, but no greater in muscle than ,Tb in tissues of E2,/TA implant steers. In conclusion, anabolic implants in steers resulted in tissue E2, concentrations less than the FDA allowable increment and ,Tb in the lowest quartile (0.25) of a part per billion 30 days after implant. [source] Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosisPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 3 2006Xiaohong Jia Abstract To study early post-mortem changes in muscle tissues from bull calves, cytosole proteins from two muscles: M. longissimus dorsi (LD) and M. semitendinosis (ST) at 0 and 24,h after slaughter were analysed by 2-DE. Principal component analysis (PCA) and rotation testing were used to analyse the protein patterns in the two muscles in order to select protein spots that were significantly different at the two time-points. Selected proteins were identified by MALDI-TOF/TOF. Five proteins, namely cofilin, lactoylglutathione lyase, substrate protein of mitochondrial ATP-dependent proteinase SP-22, HSP 27 and HSP20, were changed in both LD and ST muscles during post-mortem storage. Fifteen additional protein changes were observed in either LD or ST muscles, and some of these changes have not previously been observed to change during post-mortem storage of bovine muscles. Further studies will reveal the relevance of these biomarkers for meat quality. [source] Effects of muscle type on beef taste-traits assessed by an electric sensing systemANIMAL SCIENCE JOURNAL, Issue 5 2010Koichi CHIKUNI ABSTRACT To assess the role of muscle fiber type in beef taste-traits, we analyzed cooked meats from bovine masseter, diaphragm, psoas major, longissimus thoracis, and semitendinosus muscles with an electric taste sensing system (INSENT SA402B). The system is composed of five taste sensors of polymer membranes fixing different lipids. The sensors, CT0, CA0, AAE, C00 and AE1 are designed to respond to the individual tastes of salty, sour, umami, bitter and astringent, respectively. The system found significant differences in the converted outputs of CA0 (cvCA0), C00 (cvC00) and AE1 (cvAE1) among the bovine muscles. The slow-type muscles (masseter and diaphragm) showed lower cvCA0, higher cvC00, and higher cvAE1 than did the fast-type muscles (psoas major, longissimus thoracis, and semitendinosus). Lactic acid content was different among muscle types and was highly related to the cvCA0 output and pH. carbonyl compounds and free fatty acids were higher in the slow-type muscles. Free fatty acids were major components causing the difference in the C00 output among the muscle types. Iron content was also different among the muscle types and related to the cvC00 and cvAE1 outputs. These results suggested that the muscle fiber type affects the beef taste characteristics. [source] Relationships between tropomyosin and myosin heavy chain isoforms in bovine skeletal muscleANIMAL SCIENCE JOURNAL, Issue 2 2009Mika OE ABSTRACT The composition of tropomyosin (TPM) and myosin heavy chain (MyHC) isoforms was analyzed in 10 physiologically different bovine muscles (masseter, diaphragm, tongue, semispinalis, pectoralis profundus, biceps femoris, psoas major, semimembranosus, longissimus thoracis and semitendinosus) to clarify the relationships between TPM and MyHC isoforms in different muscle fiber types. The content of TPM1 and TPM3 was different in muscles according to their function in muscle contraction, although the content of TPM2 was constantly about 50% of the total TPM in all muscles. The content of TPM1 was higher in semimembranosus, longissimus thoracis and semitendinosus, while that of TPM3 was higher in masseter and diaphragm. The high positive correlation between MyHC-slow content and TPM3 content (r = 0.92) suggested a coexpression of TPM3 and MyHC-slow isoforms in a muscle fiber. MyHC-slow and TPM3 were expressed at the same level in masseter and diaphragm, whereas there was more TPM3 than MyHC-slow in tongue and semispinalis, so it appears that the excess TPM3 in tongue and semispinalis is expressed with other MyHC isoforms. MyHC-2a was the only fast type isoform expressed in tongue and semispinalis. Therefore, the excess TPM3 was composed of myofibrils with MyHC-2a. The results suggested that a fiber expressing MyHC-2a would be regulated delicately by changing the TPM isoform types. [source] | ||||||||||