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Connective Tissue: Structure, Function, and Influence on Meat Quality Thierry Astruc Connective tissue: structure, function, and influence on meat quality Thierry Astruc To cite this version: Thierry Astruc. Connective tissue: structure, function, and influence on meat quality. Encyclopedia of Meat Sciences, 1 (2ème ed.), Elsevier Ltd, 2014. hal-02801237 HAL Id: hal-02801237 https://hal.inrae.fr/hal-02801237 Submitted on 5 Jun 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Provided for non-commercial research and educational use only. Not for reproduction, distribution or commercial use. This article was originally published in Encyclopedia of Meat Sciences 2e published by Elsevier, and the copy attached is provided by Elsevier for the author’s benefit and for the benefit of the author’s institution, for non- commercial research and educational use including without limitation use in instruction at your institution, sending it to specific colleagues who you know, and providing a copy to your institution’s administrator. All other uses, reproduction and distribution, including without limitation commercial reprints, selling or licensing copies or access, or posting on open internet sites, your personal or institution’s website or repository, are prohibited. For exceptions, permission may be sought for such use through Elsevier’s permissions site at: http://www.elsevier.com/locate/permissionusematerial Astruc T. Connective Tissue: Structure, Function, and Influence on Meat Quality. In: Carrick Devine & Michael Dikeman, editors-in-chief. Encyclopedia of Meat Sciences 2e, Vol. 1, Oxford: Elsevier; 2014. pp. 321-328. © 2014 Elsevier Ltd. All rights reserved. Author's personal copy CONNECTIVE TISSUE: STRUCTURE, FUNCTION, AND INFLUENCE ON MEAT QUALITY T Astruc, INRA de Clermont-Ferrand-Theix, Saint Genès Champanelle, France r 2014 Elsevier Ltd. All rights reserved. This article is a revision of the previous edition article by RG Taylor, volume 1, pp 306–314, © 2004 Elsevier Ltd. Glossary cross-links, which increase the tensile strength of collagen. Collagen It is the main component of connective tissue. The number of cross-links generally increases with the age of There are many types of collagen, of which the main ones in the animals. muscle are type I and type III, which are the focus of this Collagen solubility While heating, molecular chains of article. In muscle, collagen forms the endomysium, collagen separate and solubilizes to gelatin. The perimysium, and the epimysium. solubilization of collagen decrease when the number of Collagen content With approximately 25–35% of the cross-links increase. whole body protein content, collagen is the most abundant Proteoglycans These are heavily glycosolated proteins that protein in mammals. It generally constitutes 1–2% of are a filler substance between cells that regulate movement muscle tissue but may represent up to 6% of the weight in of molecules through the matrix and affect activity and high tendinous muscles. stability of proteins and signaling molecules. Collagen cross-linking The individual protein subunits of collagen are assembled together by covalent intermolecular Introduction Intramuscular connective tissue is principally comprised of collagen and elastin proteins within a proteoglycan matrix. Connective tissue is produced by fibroblasts and is the most Muscle elastin content is approximately 0.1–0.2% of dry matter, abundant protein in mammals, making up approximately 30% except in semitendinosus and latissimus dorsi muscles, where it of the total protein content. When mineralized, it is found in reaches approximately 2%. The vast majority of this connective skeletal tissues including bone, teeth, and cartilage. The non- tissue is composed of collagen in amounts ranging from 1.5% mineralized soft connective tissue is found in skin, tendon, to approximately 10% of dry weight. Collagen I and III are the ligament, adipose tissue, blood and lymphatic tissue, and the predominant types in muscle, but collagens IV, V, VI, XII, XIV, connective fiber framework in muscles. It contains a mixture of XV, and XIX are also present in minor quantities (Figure 1). polysaccharides and fibrous proteins. The most abundant pro- Collagen is composed of three polypeptide alpha chains tein in connective tissue is collagen, but it also contains various with a simple repeating primary structure Gly–X–Y, where X is other proteins (such as elastin, fibronectin, and laminin) and often proline and Y is often hydroxyproline. The three chains are proteoglycans in varying proportions, depending on the organ. assembled together to form a triple helix of tropocollagen. The Connective tissue represents a small proportion of skeletal tropocollagen molecules are assembled together to form fibrils muscle and is mainly found in extracellular matrix of muscle that are then assembled to form collagen fibers (Figure 2). fibers. However, the meat is the result of transformation of the The fibrous collagen is cross-linked by a mechanism based muscle after slaughter of the livestock animal. Connective tissue on aldehyde formation from lysine or hydroxylysine side content and composition significantly affects the quality of chains. Fibrils and fibers are stabilized by intermolecular meat and meat products, particularly texture and water-holding lysine-derived cross-links formed between lysine aldehyde capacity. For this reason, numerous scientific studies have been or hydroxylysine aldehyde and hydroxylysine to form an led to characterize its structure, organization, and composition aldimine or oxo-imine bond. These bonds are replaced during in order to understand its role in determining meat quality. aging by stable multivalent mature cross-links, which are thought to link microfibrils and increase matrix stability. Thus, higher collagen cross-linking translates into higher mechanical Distribution, Composition, and Structure of Muscle strength. Connective Tissue From a structural standpoint, intramuscular connective tissue is divided into three main structures (see Figure 3). Muscle connective tissue content varies from 1.5 to 15% of Epimysium is a layer of dense irregular connective tissue dry matter depending on muscle and muscle function. that surrounds whole skeletal muscle. It protects muscles from Encyclopedia of Meat Sciences, Volume 1 doi:10.1016/B978-0-12-384731-7.00186-0 321 Author's personal copy 322 Connective Tissue: Structure, Function, and Influence on Meat Quality Collagen I, III, V, IX, and XI (fibrillar) Decorin Fibrillin Collagen VI Elastin 2 (nonfibrillar) Fibulin Laminin-2 2 1 Nidogen Tenascin-C Collagen XV and XVIII Tenascin-X (multiplexins) Collagen IV Perlecan (nonfibrillar) Biblycan -DG Collagen IV Fibronectin (nonfibrillar) 7 1 β δ α γ -DG Sarcospan Sarcoglycans Caveolin 3 Integrin Collagen XIII and XVII (transmembrane) Figure 1 Representation of the muscle fiber extracellular matrix. Reproduced from Voermans, N.C., Bönnemann, C.G., Huijing, P.A., et al., 2010. Clinical and molecular overlap between myopathies and inherited connective tissue diseases. Neuromuscular Disorder 18, 843–856. Myo Pm Myo (a) 1 µm (b) 0.2 µm Figure 2 Collagen fibers (bovine semitendinosus muscle). (a) Collagen fibers seen in perimysium. (b) Longitudinal section of collagen fibers. Myo, myofibrils; Pm, perimysium. friction against other muscles and bones. The epimysium is Perimysium is a layer that separates bundles of muscle generally separated from the body of the muscle and need fibers within the muscle. It represents approximately 90% not be considered as a factor in meat texture, except in some of total muscle connective tissue, where it is organized as meat products such as dry and cooked ham where muscles a network of interconnected segments that vary extensively are intact. according to muscle type, species, age, and region in the Author's personal copy Connective Tissue: Structure, Function, and Influence on Meat Quality 323 Connective Tissue Properties Related to Meat Texture The content, nature, and heat solubility of collagen are key factor of meat tenderness. Technological processes help to reduce the impact of con- Fi nective tissue on the texture of meat products. Mincing, for Pm Pm Em example, can decrease the sensation of toughness in meat, Fi whereas cooking, by solubilizing collagen, significantly re- Ad duces the mechanical strength of the connective tissue. Acidic Ad marinating can also partially degrade the connective tissue, which may tenderize meat. However, some meats, like roasts Ad Fi and grilled meat, are consumed after maturation and short- Pm term cooking, in which case cooking temperature at core of the meat piece remains too low to solubilize the collagen. As 100 μm collagen content is relatively unaffected by the action of pro- teases during maturation, it ultimately defines the basal Figure 3 Transversal section of porcine longissimus thoracis muscle. hardness of raw or undercooked meat. Thus, the less tender Ad, Adipocyte; Em, endomysium; Fi, muscle fiber; Pm, perimysium. muscles, like pectoralis profundus, generally have high colla- gen concentrations and a high number of cross-links,
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