Proportion of types I and III collagen in longissimus collagen from bulls and steers (original) (raw)
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Comparison of collagen profile and tenderness of muscles from heifers and single-calf cows
South African Journal of Animal Science, 2015
The aim of the study was to compare slaughter value, collagen profile, shear force and sensory quality of muscles originating from carcasses of heifers and single-calf cows of Polish Holstein-Friesian x Limousine crossbreds. Eight heifers (540 days old) and eight single-calf cows (836 days old), which were produced in a semi-intensive system, were included in the study. Single-calf cows were heavier than the heifers, which had higher dressing percentages and average daily gains. Calving and age at slaughter did not influence cooking loss of semimembranosus (SEM) and infraspinatus (INF) muscles or the shear force of SEM. The ventral part of the INF muscle from single-calf cows exhibited higher shear force values. In both muscles, higher water-soluble and lower acid-soluble collagen contents were noted in heifers compared with single-calf cows. There were no differences in sensory quality of SEM obtained from the carcasses of singlecalf cows and heifers, whereas cross-section appearance, tenderness, juiciness and overall acceptability of INF were scored higher for single-calf cows than for heifers. Thus, it can be concluded that heifers and single-calf cows produce meat with similar eating quality.
Meat Science, 2004
Three to 16 animals were necessary to detect a difference of 50-20% in total collagen contents in Longissimus thoracis muscle, between two experimental groups of cattle, using the facilities available in our laboratory. The inter-assay variability was higher for insoluble collagen content than for total collagen content. Consequently differences between two groups are determined less accurately for insoluble collagen content than for total collagen content. This may be partly compensated by repeated measurements (minimum 4) to detect a difference of 40% or even higher. The low reproducibility of type I and type III collagen contents determined by electrophoretic analysis is due to uncontrollable technical parameters. Normalisation of the results is thus necessary for accurate quantification. The recommended procedure is to use total protein content detected and quantified on the gels as a covariable in the statistical model. This procedure induces a 15% reduction in intra-subject variability, and hence in sample size required to detect significant differences.
animal, 2013
The aim of this paper was to identify pre-slaughter factors that modify total and insoluble collagen contents in bovine muscle to construct a model of collagen dynamics. The meta-analyses were performed with primary data of total (n= 1165) and insoluble (n= 1145) collagen contents from INRA experiments obtained from different muscles in young bulls, cows and steers. According to both the bibliography and meta-analyses, total collagen content and solubility were greatly affected by the muscle (type). Moreover, the pattern of the evolution of collagen characteristics was similar amongLongissimus,SemitendinosusandTriceps brachiimuscles in young bulls. In cows, collagen contents in theTriceps brachiimuscle had delayed dynamics compared with the other muscles. Collagen characteristics differed among breeds because of variation in the maturity of the breed. Similarly, according to the meta-analyses, total and insoluble collagen content evolutions with the degree of maturity (DOM; proporti...
Meat Science, 2003
Raw samples of 14 muscles: Mm. biceps femoris (BF), quadriceps femoris (CF), diaphragm (DI), flexor digitorum (FD), gluteus medius (GM), infraspinatus (IE), longissimus lumborum (LL), longissimus thoracis (LT), psoas major (PM), pectoralis profundus (PP), semimembranosus (SM), semitendinosus (ST), sternomandibularis (STER) and triceps brachii (TB) from four Swiss Brown (485 AE15 days old) young bull carcasses and weighing approximately 300 kg were evaluated for some chemical and physical properties. PM (2.11 kg) and DI (2.24 kg) were the muscles which had the lowest Warner-Bratzler shear force values, while PP (6.66 kg) had the greatest shear force (P< 0.05). FD and IE muscles had the highest concentration of total collagen content while PM and DI had the lowest (P< 0.05) contents, TB and IE muscles presented the highest insoluble collagen concentration while PM and LT had the lowest (P< 0.05) contents. High positive correlation between total collagen content and Warner-Bratzler shear force of raw samples was found (r=0.723; P< 0.01) and between insoluble collagen content and Warner-Bratzler shear force was (r=0.661; P< 0.01). Significant differences (P< 0.05) were observed among muscles for differential scanning calorimetry, sarcomere length, pH and colour parameters.
In continental Europe, intramuscular fat (IMF) content in beef is low but plays a key role in determining flavor. IMF expands inside the extracellular matrix (ECM) of intramuscular connective tissue. This ECM contains among others, collagens XII and XIV, two minor collagens probably involved in muscle metabolism. So, our purpose was to determine if there was an association between the contents in collagens XII and XIV and muscle metabolism. Rectus abdominis (RA, oxidative) and Semitendinosus (ST, oxido-glycolytic) muscles were sampled from steers of two genotypes with high (Angus [Ang], n¼ 10) or low (Limousine [Lim], n ¼ 10) intramuscular fat level. Collagens XII and XIV relative abundance was evaluated by Western blot analysis. The characteristic parameters of metabolism were previously measured. Ang muscles contained more collagen XIV than Lim muscles (p o0.001). RA muscle contained more collagen XII than ST muscle (po 0.01). Across the two breeds and muscles, collagen XII was positively correlated with A-and H-fatty acid binding protein (FABP) contents (þ0.43 and þ 0.53, respectively, po0.05) and activities of three oxidative enzymes (cytochrome-c oxidase: þ0.41, isocitrate dehydrogenase [ICDH]: þ0.40, citrate synthase [CS]: þ 0.32) (p o0.05) and collagen XIV was positively correlated with tria-cylglycerol content (þ 0.35, po 0.35), A-and H-FABP protein contents (þ0.35 and þ 0.38, respectively, po 0.05) and ICDH (þ0.34, po 0.05) and negatively with activities of two enzymes of glycolytic metabolism (phosphofructokinase: À 0.31 and lactate dehydrogenase: À 0.42, po 0.05). After removing the genotype and muscle effects, only collagen XII remained correlated with A-and H-FABP and CS activity (þ0.30, þ0.34 and þ0.46, respectively, po 0.0505). H-FABP is expressed in various tissues but predominantly in cardiac and oxidative skeletal muscles, whereas A-FABP is exclusively expressed within adipocytes. From these results, we can conclude that collagen XII and XIV are both associated with bovine muscle fiber and intramuscular lipid metabolism, but probably by different mechanisms. As a matter of fact, collagens XII is associated with intramuscular fat differentiation (from its correlation with A-FABP content) and oxidative metabolism (from its correlation with H-FABP content and CS activities) regardless of breed and muscle, whereas type XIV collagen is associated with the same parameters plus enzymes of glycolytic metabolism that discriminate breeds.
The Histochemical journal, 2000
The ontogenesis of total collagen and of different collagen types was studied in four muscle types from genetically different cattle. Hydroxyproline content was 1.2-fold higher in muscles from cross-bred foetuses with normal muscle growth compared to those of the other genetic types (pure bred with different growth rates, double-muscled breed). A similar tendency was observed for type III collagen content. In all muscles of each animal studied, type XII and XIV collagens were colocated in perimysium. Immunolabelling obtained for type XII collagen was higher during foetal life than after birth, while for type XIV collagen, the opposite result was obtained. Whatever the muscle studied, but especially in semitendinosus muscle, during the foetal and the post-natal period until 15 months of age, immunolabelling with antibody anti-type XIV collagen tended to be more intense in muscles of animals from fathers selected for a low muscle growth capacity compared to those from fathers selected...
Korean Journal for Food Science of Animal Resources
The objective of this study was to determine the influence of quality grade (QG) on meat tenderness characteristics of ten major muscles from Hanwoo steers. A total of 25 Hanwoo carcasses (5 carcasses × 5 QGs) were selected. Intramuscular fat content, collagen content, sarcomere length, and Warner-Bratzler shear force (WBSF) of Longissimus thoracis (LT), Longissimus lumborum (LL), Psoas major (PM), Semisponals (SS), Triceps brachii (TB), Semimembranosus (SM), Gluteus medius (GM), Rectus Abdominis (RA), Superficialis flexor (SF), and Internal and external intercostal (IC) were determined. IC had the highest fat content, followed by LT, RA, LL, PM, GM, SS, SF, TB, and SM. High-fat muscles such as LT, LL, IC, RA, and PM had significantly (p<0.05) different fat contents among QGs. Collagen contents were significantly (p<0.05) different among QGs. With decreasing QG, increasing collagen content was found in muscles. There were significant (p<0.05) differences in sarcomere length among QGs of several muscles. However, no significant (p>0.05) difference in sarcomere length was found among QGs for LL, PM, or RA muscle. PM had the lowest WBSF, followed by LL, LT, RA, IC, GM, SM, SF, SS, and TB. WBSF of QG 1 + + was lower than that of QG 1 for SS, TB, and SM. All muscles of QG 1 showed lower WBSF than QG 3 except TB or IC. Results of this study suggested that differences in WBSF among these 10 muscles by QG were due to differences in collagen content and sarcomere length.
Meat Science, 2011
Variations in texture were determined for 10 day aged raw and cooked Longissimus thoracis (LT) muscle from 436 bulls of 15 European cattle breeds slaughtered at an age of 13-16 months. Variations in texture were related to differences in pH 24 h post-mortem, sarcomere length, collagen characteristics and lipid content. The shear force of cooked meat samples varied from 43.8 to 67.4 N/cm 2 . Simmental, Highland and Marchigiana cattle had the highest shear force values and Avileña-Negra Ibérica, Charolais, Casina and Pirenaica cattle had the lowest values. Cooked meat toughness showed a weak negative correlation to lipid content (P b 0.001) but no correlation to collagen characteristics. Raw meat texture measured by compression correlated positively (P b 0.001) with total and insoluble collagen. In conclusion, collagen characteristics showed correlation to raw meat texture but not to cooked meat toughness of LT muscle in European young bulls.
Folia Biologica, 2013
WOJTYSIAK D. 2013. Effect of age on structural properties of intramuscular connective tissue, muscle fibre, collagen content and meat tenderness in pig longissimus lumborum muscle. Folia Biologica (Kraków) $: 221-226. Changes in the structure and properties of the intramuscular connective tissue, muscle fibre size, collagen content and meat tenderness of m. longissimus lumborum during growth was studied in 45 Polish Large White (PLW) pigs slaughtered at 90, 150 and 210 days of age. The results show that the endomysial sheath in m. longissimus lumborum consists of collagen fibrils of wavy appearance which run in all directions and form a loose network. The arrangement of collagen fibrils in the endomysium and perimysium becomes denser and more regular with increasing age of pigs. In addition, the increase in endomysium and perimysium thickness was paralleled by a significant increase in muscle fibre diameter, as well as an increase in shear force value with chronological aging. In contrast, the percentage of collagen area in muscle structure and the amount of total collagen and amount of soluble collagen decreased gradually with age of pigs. In conclusion, the structural changes in the arrangement of collagen fibres in the architecture of intramusclular connective tissue, as well as the decrease in soluble collagen content in m. longissimus lumborum during growth of pigs are important factors influencing shear force value, and thus raw meat tenderness.
Tenderness of major muscles from three breed-types of cattle at different times-on-feed
Meat Science, 1985
Seventy-five steers (9 to 12 months of age) of Angus (n = 25), Brahman (n =25) and Brahman × Angus (n = 25) breed-types of known history were fed a high-energy diet and five steers from each breed-type were slaughtered after O, 56, 112, 168 and224 days on test. At seven days post mortem, the left side of each carcass was fabricated and eight major primals or subprimals were obtained. Steaks were removed from the shoulder clod, strip loin, tenderloin, top sirloin, knuckle, top round, bottom round and eye of round for Warner-Bratzler shear (WBS) determinations and from the strip loin and bottom round for sensory panel evaluations. Steaks from Angus and Brahman x Angus steers were generally more tender than steaks from Brahman steers. Tenderness of steaks from steers of the three breed-types responded to time-on-feed differently: (a) steaks from Brahman steers improved (P < 0.05) in tenderness with increasing time-on-feed for all muscles except the M. psoas major (tenderloin); (b) with the exception of the M. longissimus muscle (strip loin), the tenderness of steaks from Angus steers did not change (P > 0"05) as time-on-feed increased and (c) Jor the Brahman x Angus steers, five of the ten muscles studied improved (P < 0-05) in