Znaczenie śródmięśniowej tkanki łącznej w jakości mięsa

• Autorzy: Gorska M. , Wojtysiak D.

Warianty tytułu

EN

Importance of intramuscular connective tissue for meat quality

• Języki publikacji: PL

Abstrakty

EN

During ageing, meat undergoes many structural and biochemical changes which make it possible to obtain meat of specific taste and physico-chemical parameters. One of the most important quality parameters is meat tenderness and juiciness. This work presents the results of studies concerning the possible effect of intramuscular connective tissue (IMCT) on the final meat quality. The amount, quality and organization of this tissue depend on the type of muscle, as well as its location in the carcass and function in the body. Muscles with high amounts of IMCT are generally less tender due to a considerable collagen content. The breakdown of IMCT network increases collagen solubility and decreases the number of extracellular matrix components, which may lead to increased meat tenderness and reduced meat juiciness. However, the final meat quality is determined not only by the proportion of connective tissue in the muscle structure, the size and organization of collagen fibres, the intramuscular fat content and the total collagen level, but also by the soluble collagen content. The effect of IMCT on the final meat quality requires further research, mainly at the molecular level.

Słowa kluczowe

PL

mieso; jakosc; tkanka laczna srodmiesniowa; struktura; wlasciwosci; cechy sensoryczne; kruchosc miesa; soczystosc; tekstura

• Wydawca: -
• Czasopismo: Medycyna Weterynaryjna
• Rocznik: 2016
• Tom: 72
• Numer: 10
• Opis fizyczny: s.600-603,fot.,bibliogr.

Twórcy

autor

Gorska M.

• Zakład Anatomii Zwierząt, Instytut Nauk Weterynaryjnych, Wydział Hodowli i Biologii Zwierząt, Uniwersytet Rolniczy w Krakowie, Al.Mickiewicza 24/28, 30-059 Kraków

autor

Wojtysiak D.

• Zakład Anatomii Zwierząt, Instytut Nauk Weterynaryjnych, Wydział Hodowli i Biologii Zwierząt, Uniwersytet Rolniczy w Krakowie, Al.Mickiewicza 24/28, 30-059 Kraków

Bibliografia

• An J. Y., Zheng J. X., Li J. Y., Zeng D., Qu L. J., Xu G. Y., Yang N.: Effect of myofiber characteristics and thickness of perimysium and endomysium on meat tenderness of chickens. Poult. Sci. 2010, 89, 1750-1754.
• Astruc T.: Connective tissue: structure, function, and influence on meat quality. Encyclopedia of Meat Sci. 2014, 1, 321-328.
• Blicharski T. (red.): Aktualna wartość dietetyczna wieprzowiny, jej znaczenie w diecie i wpływ na zdrowie konsumentów. Polski Związek Hodowców i Producentów Trzody Chlewnej POLSUS, Warszawa 2013, s. 24-36.
• Dąbrowska E., Jankowska B., Kwiatkowska A., Cierach M.: Zawartość kolagenu w mięśniach tylnej ćwierćtuszy wołowej. Inż. Ap. Chem. 2011, 50, 18-19.
• Dubost A., Micol D., Picard B., Lethias C., Andueza D., Bauchart D., Listrat A.: Structural and biochemical characteristics of bovine intramuscular connective tissue and beef quality. Meat Sci. 2013, 95, 555-561.
• Fosang A. J., Hardingham T. E.: Matrix Proteoglycans, [w:] Comper W. D. (red.): Extracellular Matrix. T. 2., Harwood Academic Publishers, Amsterdam 1996, s. 200-229.
• Janicki B., Buzała M.: Wpływ kolagenu na jakość technologiczną mięsa. Zywn. Nauk. Technol. Ja. 2013, 2, 19-29.
• Krzyżanowska-Gołąb D., Lemańska-Perek A., Kątnik-Prastowska I.: Fibronektyna jako aktywny składnik macierzy pozakomórkowej. Postepy Hig. Med. Dosw. 2007, 61, 655-663.
• Lachowicz H. K., Závět A. K., Maryško M., Vinai F.: Magnetic phases in nanogranular Co-Cu structures. J. Magn. Magn. Mater. 2004, 272-276, 1521-1523.
• Lepetit J.: A theoretical approach of the relationships between collagen content, collagen crosslinks and meat tenderness. Meat Sci. 2007, 76, 147-159.
• Lewis G. J., Purslow P. P.: Connective tissue differences in the strength of cooked meat across the muscle fibre direction due to test specimen size. Meat Sci. 1990, 28, 183-194.
• Lewis G. J., Purslow P. P., Rice A. E.: The effect of conditioning on the strength of perimysial connective tissue dissected from cooked meat. Meat Sci. 1991, 30, 1-12.
• Listrat A., Hocquette J. F.: Analytical limits of total and insoluble collagen content measurements and of type I and III collagen analysis by electrophoresis in bovine muscles. Meat Sci. 2004, 68, 127-136.
• Nakamura Y. N., Iwamoto H., Ono Y., Shiba N., Nishimura S., Tabata S.: Relationship among collagen amount, distribution and architecture in the M. longissimus thoracis and M. pectoralis profundus from pigs. Meat Sci. 2003, 64, 43-50.
• Nakano T., Li X., Sunwoo H. H., Sim J. S.: Immunohistochemical localization of proteoglycans in bovine skeletal muscle and adipose connective tissues. Canadian J. Anim. Sci. 1997, 77, 169-172.
• Nishimura T.: Role of extracellular matrix in development of skeletal muscle and postmortem aging of meat. Meat Sci. 2015, 109, 48-55.
• Nishimura T.: The role of intramuscular connective tissue in meat texture. J. Anim. Sci. 2010, 81, 21-27.
• Nishimura T., Fang S., Wakamatsu J., Takahashi K.: Relationships between physical and structural properties of intramuscular connective tissue and toughness of raw pork. J. Anim. Sci. 2009, 80, 85-90.
• Nishimura T., Hattori A., Takahashi K.: Relationship between degradation of proteoglycans in basement membrane and intramuscular connective tissue of bovine semitendinosus muscle. Acta Anat. 1996a, 155, 257-265.
• Nishimura T., Ojima K., Liu A., Hattori A., Takahashi K.: Structural changes in the intramuscular connective tissue during development of bovine semitendinosus muscle. Tissue Cell 1996b, 28, 527-536.
• Passerieux E., Rossignol R., Chopard A., Carnino A., Marini J. F., Letellier T., Delage J. P.: Structural organization of the perimysium in bovine skeletal muscle: functional plates and associated intracellular subdomains. J. Struct. Biol. 2006, 154, 206-216.
• Petibois C., Gouspillou G., Wehbe K., Delage J. P., Dèlèris G.: Analysis of type I and IV collagens by FT-IR spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue. Anal. Bioanal. Chem. 2006, 386, 1961-1966.
• Purslow P. P.: Intramuscular connective tissue and its role in meat quality. Meat Sci. 2005, 70, 435-447.
• Purslow P. P.: New developments on the role of intramuscular connective tissue in meat toughness. Annu. Rev. Food Sci. T. 2014, 5, 133-153.
• Purslow P. P.: The structure and functional significance of variations in the connective tissue within muscle. Comp. Biochem. Physiol. A 2002, 133, 947-966.
• Scott J. E., Thomlinson A. M.: The structure of interfibrillar proteoglycan bridge (‘shape modules’) in extracellular matrix of fibrous connective tissues and their stability in various chemical environments. J. Anat. 1998, 192, 391-405.
• Suzuki K., Kishioka Y., Wakamatsu J., Nishimura T.: Decorin activates akt down stream of IGF-IR and promotes myoblast differentiation. J. Anim. Sci. 2013, 84, 669-674.
• Swatland H. J., Gullett E., Hore T., Buttenham S.: UV fiber-optic probe measurements of connective tissue in beef correlated with taste panel scores for chewiness. Food Res. Int. 1995, 28, 23-30.
• Turrina A., Martinez-González M. A.: The muscular force transmission system: Role of the intramuscular connective tissue. J. Bodyw. Mov. Ther. 2013, 17, 95-102.
• Velleman S. G.: Meat science and muscle biology: Extracellular matrix regulation of skeletal muscle formation. J. Anim. Sci. 2012, 90, 936-941.
• Voermans N. C., Bönnemann C. G., Huijing P. A.: Clinical and molecular overlap between myopathies and inherited connective tissue diseases. Neuromuscular. Disord. 2010, 18, 843-856.
• Weston A. R., Rogers R. W., Althen T. G.: Review: the role of collagen in meat tenderness. Prof. Anim. Sci. 2002, 18, 107-111.
• Wojtysiak D.: Effect of breed on microstructure and tenderness of porcine semimembranosus muscle. Ann. Anim. Sci. 2014, 14, 697-705.
• Yang B., Yang B. L., Savari R. C., Turley E. A.: Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein. EMBOJ. 1994, 13, 286-296.
• Zhu J., Li Y., Shen W., Qiao C., Ambrosio F., Lavasani M., Nozaki M., Branca M. F., Huard J.: Relationships between transforming growth factor-β1, myostatin, and decorin: implications for skeletal muscle fibrosis. J. Biol. Chem. 2007, 282, 25852-25863.

Identyfikatory

DOI

10.21521/mw.5577