Louis Lefaucheur

A second look into fibre typing--relation to meat quality.

Despite intensive research, a large variation in meat quality is still observed in most meat producing species. It is widely accepted that myofibre type composition is an important source of variation in meat quality. However, the identification of specific and universal relationships between myofibre characteristics, growth performance and meat quality traits remains a challenge. After the presentation of recent knowledge underlying fibre typing, this review describes the involvements of Ca2+-dependent mechanisms, and the energy state of the myofibres in the control of contractile and metabolic properties, with a special attention to the AMP-activated protein kinase pathway and mitochondrial compartment. In order to identify muscle components which could mask specific relationships between fibre type composition and meat quality, an analysis of the interactions between myofibres and other muscle cellular components is presented. After a brief description of myogenesis, the significance of the total number of fibres, myofibre cross-sectional area and fibre type composition for growth performance and meat quality is presented. Then, some genetic and environmental factors are proposed as possible tools to control meat quality trough the modulation of fibre type characteristics. Finally, a conclusion makes the point on bottlenecks still preventing the identification of specific relationships between fibre characteristics, growth performance and meat quality, and suggests future perspectives such as direct selection on fibre traits and study of correlated responses, the development of in vitro approaches using cell cultures, manipulation of myogenesis during the fetal period, and the production and use of genetically modified animals.

New Insights into Muscle Fiber Types in the Pig

The accurate classification of skeletal muscle fiber types according to myosin heavy chain (MyHC) polymorphism remains a difficult task in the pig. Combined myofibrillar ATPase and metabolic enzyme histochemistry, in situ hybridization, and immunocytochemistry were performed on serial transverse sections of pig longissimus (L) and rhomboideus (R) muscles at 100 kg body weight to give a new insight into muscle fiber typing in the pig. Several monoclonal antibodies (MAbs) either specific for a single MyHC (I, IIa, or IIb) or of multiple MyHCs (IIa + IIx or I + IIx + IIb) were used. No monospecific IIx antibody was available for the pig. All three adult Type II isoforms were expressed in the white L muscle, whereas no IIb was observed in the red R muscle, which was confirmed using RNase protection analysis. In most fibers, the distribution of the transcripts closely matched that of the corresponding proteins. When observed, co-expression of MyHCs mostly occured for IIx and IIb in L muscle, and was more common at the protein (11.5%) than at the mRNA (2.2%) level. A minor proportion of myofibers showed a mismatch between MyHC mRNA and protein. According to the type grouping distribution of myofibers encountered in pig muscle, MyHC isoform expression followed the rank order of I→Iia→Iix→IIb from the center to the periphery of the islets, concomitantly with a decrease in oxidative metabolism and an increase in fiber size. The developmental origin and functional significance of the type grouping distribution are discussed.

Effects of age and/or weight at slaughter on longissimus dorsi muscle: Biochemical traits and sensory quality in pigs

The effect of increasing either age alone through feed restriction, or both age and weight at slaughter, on the quality of the longissimus dorsi muscle (LM) was investigated. Starting at 83 days of age and 32 kg, 80 pigs were allotted within litter to four experimental groups. All pigs were free of RYR1 mutated gene. Pigs were fed either ad libitum (A100, A130) or restricted 30% (R100, R130) and slaughtered at either 100 kg (A 100, R100) or 130 kg (A130, R130) body weight. Restricting feed intake in order to increase age at the same weight resulted in slower growth, better feed efficiency and increased leanness, whereas increasing age and weight simultaneously elicited slower growth, reduced feed efficiency and fatter carcasses. Intramuscular fat (IMF) and muscle collagen concentration were reduced by restricted feeding. Increase in both age and weight of pigs resulted in lower water, and higher protein and IMF concentrations. Although pigs were free of RYR1 gene, the PSE condition (defined as pH1 ≤ 5.9) developed in 25 carcasses, with a higher incidence in restricted pigs. PSE animals were excluded from the subsequent analysis of meat quality data. Feed restriction resulted in higher drip loss and lower a(∗) and c(∗) (saturation index) values. Longer myofibril fragments in muscle of restricted pigs on day 1 post mortem are indicative of slower maturation, while longer fragments on day 4 in heavier pigs, suggest that the extent of post mortem tenderisation could be negatively affected by the elevation of slaughter weight. Feed restriction had no significant effect on meat sensory quality, whereas increase in both age and weight resulted in lower tenderness, chewiness and mouth coating scores. Our results indicate that increasing age at a given body weight, via feed restriction, reduced IMF and collagen concentrations, and the rate of post mortem proteolysis, however, this had no significant impact on pork quality assessed after 4 days of ageing. On the other hand, increasing both age and weight at slaughter could alter pork texture, in spite of elevated IMF concentration.

Skeletal muscle proteomics in livestock production

Proteomics allows studying large numbers of proteins, including their post-translational modifications. Proteomics has been, and still are, used in numerous studies on skeletal muscle. In this article, we focus on its use in the study of livestock muscle development and meat quality. Changes in protein profiles during myogenesis are described in cattle, pigs and fowl using comparative analyses across different ontogenetic stages. This approach allows a better understanding of the key stages of myogenesis and helps identifying processes that are similar or divergent between species. Genetic variability of muscle properties analysed by the study of hypertrophied cattle and sheep are discussed. Biological markers of meat quality, particularly tenderness in cattle, pigs and fowl are presented, including protein modifications during meat ageing in cattle, protein markers of PSE meat in turkeys and of post-mortem muscle metabolism in pigs. Finally, we discuss the interest of proteomics as a tool to understand better biochemical mechanisms underlying the effects of stress during the pre-slaughter period on meat quality traits. In conclusion, the study of proteomics in skeletal muscles allows generating large amounts of scientific knowledge that helps to improve our understanding of myogenesis and muscle growth and to control better meat quality.

Effect of slaughter weight and/or age on histological characteristics of pig longissimus dorsi muscle as related to meat quality

The effect of increasing both weight and age or age alone through feed restriction on muscle longissimus dorsi histological characteristics were studied in relation to fresh and cooked meat quality. Starting at 83 days (32 kg) 80 crossbred Duroc × (Large White×Landrace) barrows were allotted within litter to 4 experimental groups (A100, R100, A130, R130). Pigs were fed either ad libitum (A) or were restricted 30% (R) and slaughtered either at 100 kg or 130 kg. Muscle fibres were classified as βR, αR or αW according to Ashmore and Doerr (1971)(Ashmore, C.R., & Doerr, L. (1971). Comparative aspects of muscle fibre types in different species. Experimental Neurology, 31, 408-418.). Percentages (PC), cross-sectional areas (CSA) and relative areas (RA) of each fibre type were evaluated. Phenotypic correlations between histological traits showed that RA of a particular fibre type depends essentially on its numerical abundance. Increasing weight together with age led to enlargement of βR and αW muscle fibres, without changing muscle histochemical profile. When age was increased at the same weight (restriction), higher RA of βR fibres was observed. Low, but significant correlation between loin eye area and CSA was observed, but not within experimental group. The phenotypic correlations between histological and meat quality traits were generally low. This material showed some significant correlations suggesting that increasing PC or CSA of overall αW fibres can be beneficial for water holding capacity of fresh meat and juiciness of cooked meat. ©

How Muscle Structure and Composition Influence Meat and Flesh Quality.

Skeletal muscle consists of several tissues, such as muscle fibers and connective and adipose tissues. This review aims to describe the features of these various muscle components and their relationships with the technological, nutritional, and sensory properties of meat/flesh from different livestock and fish species. Thus, the contractile and metabolic types, size and number of muscle fibers, the content, composition and distribution of the connective tissue, and the content and lipid composition of intramuscular fat play a role in the determination of meat/flesh appearance, color, tenderness, juiciness, flavor, and technological value. Interestingly, the biochemical and structural characteristics of muscle fibers, intramuscular connective tissue, and intramuscular fat appear to play independent role, which suggests that the properties of these various muscle components can be independently modulated by genetics or environmental factors to achieve production efficiency and improve meat/flesh quality.

Myosin isoform transitions in four rabbit muscles during postnatal growth.

SummaryFour rabbit muscles (i.e. semimembranosus proprius, psoas major, biceps femoris and longissimus lumborum), differing in their fibre type composition in the adult, were investigated during postnatal development. Muscle samples were taken at 1, 7, 14, 21, 28, 35, 49 and 77 days of age. Complementary techniques were used to characterize myosin heavy chain (MHC) isoform transitions, i.e. SDS-PAGE, immunocytochemistry and conventional histochemistry. Good accordance was found between electrophoretic and immunocytochemical techniques. Our results show that rabbit muscles were phenotypically immature at birth. At 1 day of age, perinatal isoform represented 70–90% of the total isoform content of the muscles. Two generations of myofibres could be observed on the basis of their morphology and reaction to specific antibodies. In all muscles, primary fibres expressed slow MHC. In contrast, secondary generation of fibres never expressed slow MHC in future fast muscles, while half of them expressed slow MHC in the future slow-twitch muscle, the semimembranosus proprius. During the postnatal period, all muscles displayed a transition from embryonic to perinatal MHC isoforms, followed by a transition from perinatal to adult MHC isoforms. These transitions occured mainly during the first postnatal month. The embryonic isoform was no longer expressed after 14 days, except in longissimus where it disappeared after 28 days. On the contrary, large differences were found in the timing of disappearance of the perinatal isoform between the four muscles. The perinatal isoform disappeared between 28 and 35 days in semimembranosus proprius and 35 and 49 days in psoas and biceps femoris. Interestingly, the perinatal isoform was still present in 6% of the fibres in longissimus at 77 days, the commercial slaughter age, denoting a great delay in the maturation. Fate of each generation of fibres differed between muscles.

Consequences of divergent selection for residual feed intake in pigs on muscle energy metabolism and meat quality

Selection to decrease Residual Feed Intake (RFI) is a relevant way to improve feed efficiency in growing pigs. However, RFI criterion is correlated with body composition and muscle characteristics. Present study evaluated adaptive responses to divergent selection on RFI on muscle metabolism and homeostasis through AMP-activated protein kinase pathway. Consequences on technological and sensory meat quality were also analyzed in two lines of Large White pigs after six generations of divergent selection on RFI. RFI(-) pigs (n=60) exhibited similar growth rate but lower feed intake and conversion ratio, and were leaner than RFI(+) pigs (n=57). Despite higher glycogen content, metabolic enzyme capacities involved in glycolytic, fatty acid oxidation pathway and energy balance were reduced in the Longissimus muscle of the RFI(-) pigs. Reduced muscle homeostasis in the RFI(-) line influenced post-mortem metabolism and impaired technological quality traits of loin and ham but had only slight effects on meat eating quality.

A sulfur amino acid deficiency changes the amino acid composition of body protein in piglets

Experiments carried out to determine the amino acid requirement in growing animals are often based on the premise that the amino acid composition of body protein is constant. However, there are indications that this assumption may not be correct. The objective of this study was to test the effect of feeding piglets a diet deficient or not in total sulfur amino acids (TSAA; Met + Cys) on nitrogen retention and amino acid composition of proteins in different body compartments. Six blocks of three pigs each were used in a combined comparative slaughter and nitrogen balance study. One piglet in each block was slaughtered at 42 days of age, whereas the other piglets received a diet deficient or not in TSAA for 19 days and were slaughtered thereafter. Two diets were formulated to provide either 0.20% Met and 0.45% TSAA (on a standardized ileal digestible basis) or 0.46% Met and 0.70% TSAA. Diets were offered approximately 25% below ad libitum intake. At slaughter, the whole animal was divided into carcass, blood, intestines, liver, and the combined head, tail, feet and other organs (HFTO), which were analyzed for nitrogen and amino acid contents. Samples of the longissimus muscle (LM) were analyzed for myosin heavy chain (MyHC) and actin contents. Nitrogen retention was 20% lower in piglets receiving the TSAA-deficient diet (P < 0.01). In these piglets, the nitrogen content in tissue gain was lower in the empty body, carcass, LM and blood (P < 0.05) or tended to be lower in HFTO (P < 0.10), but was not different in the intestines and liver. The Met content in retained protein was lower in the empty body, LM and blood (P < 0.05), and tended to be lower in the carcass (P < 0.10). The Cys content was lower in LM, but higher in blood of piglets receiving the TSAA-deficient diet (P < 0.05). Skeletal muscle appeared to be affected most by the TSAA deficiency. In LM, the Met content in retained protein was reduced by 12% and total Met retention by more than 60%. The MyHC and actin contents in LM were not affected by the TSAA content of the diet. These results show that a deficient TSAA supply affects the amino acid composition of different body proteins. This questions the use of a constant ideal amino acid profile to express dietary amino acid requirements, but also illustrates the plasticity of the animal to cope with nutritional challenges.

Comparative study of two classifications of muscle fibres: Consequences for the photometric determination of glycogen according to fibre type in red and white muscle of the pig

The present experiment was designed to compare two classifications of myofibres in samples of muscles longissimus lumborum (LL) and semispinalis capitis (SC) taken at slaughter from 56 Large White pigs. Comparisons were made for the percentage and histological characteristics of the different types of myofibres and for the photometric determination of glycogen using periodic acid schiff (PAS) staining. Computerized image analysis was used (i) to classify the fibres on the basis of myosin ATPase activity [Brooke and Kaiser (1970) Arch. Neurol.23, 3669; types I, IIA and HB], or by combination of myosin ATPase and succino-dehydrogenase (SDH) activities [Ashmore and Doerr (1971) Exp. Neurol.31, 408: types βR, αR, and αW] and (ii) to compute the PAS staining luminance in individual fibres. Glycogen and related metabolites were determined in muscle homogenates using enzymatic techniques. The LL showed significantly higher glycogen and lactate contents than the SC and a significantly lower average PAS staining luminance (indicative of higher glycogen content). The LL was composed predominantly of fast-twitch (89%) and white (77.3%) fibres. The SC contained mainly red (61.1%) and fast-twitch (59.3%) fibres. In both muscles, the comparison of the two classifications indicates that all type I fibres showed high SDH activity and were therefore typed as βR in Ashmore and Doerrs classification. However, in the LL, approximately 7% of the type IIB fibres showed a marked SDH activity and were thus typed as αR in Ashmore and Doerrs classification. Furthermore, significant differences were found between these two types for the cross sectional area of the fibres. In the SC, no significant differences were found for the pairwise comparisons of corresponding types between the two classifications. According to the photometric determination, fast-twitch glycolytic fibres of the LL showed significantly higher glycogen content than red (fast- and slow-twitch) fibres, whereas in the SC, slow-twitch fibres had significantly lower glycogen levels than fast-twitch (red and white fibres). Corresponding types between the two classifications showed similar glycogen levels.