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15 (2008) | nr 1 (56) | 5--22
Tytuł artykułu

Jakość wołowiny

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Warianty tytułu
Beef Quality
Języki publikacji
Głównym przeznaczeniem użytkowym wołowiny jest mięso kulinarne. W ocenie konsumenckiej jakość wołowiny w punkcie sprzedaży określają: barwa, ilość widocznego tłuszczu, konsystencja i zapach. O właściwościach kulinarnych wołowiny przeznaczonej do obróbki cieplnej decydują kruchość i smakowitość. Omówiono czynniki wpływające na wartość odżywczą wołowiny, jej barwę, kruchość i smakowitość. Na wymienione cechy jakościowe mają wpływ zarówno naturalne różnice między mięśniami, wynikające z ich funkcji fizjologicznej i budowy, jak również działania podejmowane przez producentów (hodowców, dostawców zwierząt) i technologów. (abstrakt oryginalny)
Beef meat is mainly used as a culinary meat. At a meat outlet, consumers judge the quality of beef by its colour, visible fat content, consistency, and odour. The culinary features of beef meat to be thermally treated are determined by its tenderness and palatability. The factors influencing nutritional value of beef, its colour, tenderness, and palatability are discussed. The factors as pointed out here are impacted by both the natural differences between the muscles, resulting from their physiological function and structure, and the actions taken by producers (breeders, suppliers of animals) and technologists. (original abstract)
Opis fizyczny
  • Akademia Rolnicza w Krakowie
  • [1] Abbot M.T., Pearson A.M., Price J.F., Hooper G.R.: Ultrastructural changes duringautolysis of red and white porcine muscle. J. Food Sci., 1977, 42, 1185-1188.
  • [2] Aberle E.D., Forrest J.C., Gerrard D.E., Mills E.W., Hedrick H.B., Judge M.D., Merkel R.A.: Principles of Meat Science. Kendall/Hunt Publishing Company, 2001.
  • [3] Bailey A.J., Light N.D.: Connective tissue in meat and meat products. Elsevier Applied Science, London 1989.
  • [4] Baker M.A., Lawen A.: Plasma membrane NADH-oxidoreductase system. A critical review of the structural and functional data. Antioxidants & Redox Signaling, 2000, 2, 197-212.
  • [5] Bekhit A.E.D., Faustman C.: Metmyoglobin reducting activity. Meat Sci., 2005, 71, 407-439.
  • [6] Bekhit A.E.D., Geesink G.H., Morton J.D., Bickerstaffe R.: Metmyoglobin reducting activity and color stability of ovine Longissimus muscle. Meat Sci., 2001, 57, 427- 435.
  • [7] Bendall J.R.: The elastin content of various muscles of beef animals. J. Sci. Food Agr., 1967, 18, 553-558.
  • [8] Bodwell C.E., McClain P.E.: Chemistry of Animal Tissues. Proteins. In: Price J.F., Schweigert B.S. (Eds.): The Science of Meat and Meat Products. W.H. Freeman and Company, USA, 1971, pp. 78- 132.
  • [9] Borg T.K., Caulfield J.B.: Morphology of connective tissue in skeletal muscle. Tissue Cell., 1980, 12, 197-207.
  • [10] Bouton P.E., Harris P.V.: The effect of some post-slaughter treatments on the mechanical properties of bovine and ovine muscle. J. Food Sci., 1972, 37, 539-543.
  • [11] Bratzler L.J.: Palatability factors and evaluation. In: Price J.F., Schweigert B.S. (Eds.): The Science of Meat and Meat Products. W.H. Freeman and Company, USA, 1971, pp. 328-347.
  • [12] Brooks J.: The oxidation of haemoglobin to methaemoglobin by oxygen. II. The relation between the rate of oxidation and the partial pressure of oxygen. Proc. Royal Society, London, Series.B, 1935, 118, 560-577.
  • [13] Brooks J.C., Savell J.: Perimysium thickness as an indicator of beef tenderness. Meat Sci., 2004, 67, 329-334.
  • [14] Carpanter Z.L., Kauffman R.G., Bray R.W., Briskey E.J., Weckel K.G.: Factors influencing quality in pork. A. Histological observations. J. Food Sci., 1963, 28, 467-471.
  • [15] Casas E., White S.N., Wheeler T.L., Shackelford S.D., Koohmaraie M., Riley D.G., Chase C.C., Johnson D.D., Smith T.P.L.: Effects of calpastatin and μ-calpain markers in beef cattle on tenderness traits. J. Animal Sci., 2006, 84, 520-525.
  • [16] Ciobanu D.C., Bastiaansen J., Malek M., Helm J., Wollard J., Plastow G.S.: Evidence for new alleles in calpastatin gene are associated with meat quality traits in pigs. J. Animal Sci., 2004, 82, 2829-2839.
  • [17] Dransfield E.: Optimisation of tenderization, ageing and tenderness. Meat Sci., 1994, 36, 105-121.
  • [18] Dutson T.R., Lawrie R.A.: Release of lysosomal enzymes during post-mortem conditioning and their relationship to tenderness. J. Food Technol., 1974, 9, 43-50.
  • [19] Dutson T.R., Pearson A.M., Merkel R.A.: Ultrastructural post-mortem changes in normal and low quality porcine muscle fibers. J. Food Sci., 1974, 39, 32-37.
  • [20] Echevarne C., Renerre M., Labas R.: Metmyoglobin reductase activity in bovine muscles. Meat Sci., 1990, 27, 161-172.
  • [21] Faustman C., Cassens R.G.: The biochemical basis for meat discolouration in fresh meat: a review. J. Muscle Foods, 1990, 1, 217-243.
  • [22] Faustman C., Cassens R.G.: The effect of cattle breed and muscle type on discoloration and various biochemical parameters in fresh beef. J. Animal Sci., 1991, 69, 184-193.
  • [23] Feldhusen F., Warnatz A., Erdmann R., Wenzel S.: Influence of storage time on parameters of color stability of beef. Meat Sci., 1995, 40, 235-243.
  • [24] Gasser U., Grosch W.: Identification of volatile flavour compounds with high aroma values from cooked beef. Z.Lebensm.Unters.Forsch., 1988, 186, 489-494.
  • [25] Geesink G.H., Koohmaraie M.: Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage. J. Animal Sci., 1999, 77, 1490-1501.
  • [26] Goll D.E., Thompson V.F., Li H.Q., Wei W., Cong J.Y.: The calpain system. Physiol. Rev., 2003, 83, 731-801.
  • [27] Gorraiz C., Beriain M.J., Chasco J., Insausti K.: Effect of ageing time on volatile compounds, odor and flavour of cooked beef from Pireneica and Friesian bulls and heifers. J. Food Sci., 2002, 67, 916-922.
  • [28] Grosch W.: Evaluation of the key odorant of foods by dilution experiments, aroma models and omission. Chem. Senses., 2001, 26, 533-545.
  • [29] Hammond J.: Growth and the development of mutton qualiteis in the sheep. Biological monographs and manuals. London, Oliver and Boyd, 1932, vol. X.
  • [30] Hood D.E.: Factors affecting the rate of metmyoglobin accumulation in pre-packed beef. Meat Sci., 1980, 4, 247-265.
  • [31] Hornstein I.: Chemistry of Meat Flavor. In: Price J.F., Schweigert B.S. (Eds.): The Science of Meat and Meat Products. W.H. Freeman and Company, USA, 1971, pp. 348-366.
  • [32] Hunt M.C., Hendrick B.: Chemical, physical and sensory characteristics of bovine muscle from four quality groups. J. Food Sci., 1977, 42, 716-720.
  • [33] Kendall T.L., Koohmaraie M., Arbona J.R., Williams S.E., Young L.L.: Effect of pH and ionic strength on bovine m-calpain and calpastatin activity. J. Animal Sci., 1993, 71, 96-104.
  • [34] Kołczak T.: Wpływ czynników poubojowych na kruchość wołowiny. Gosp. Mięs., 2000, 5, 28-31.
  • [35] Kołczak T., Palka K., Pospiech E.: Changes in collagen solubility of raw and roasted bovine psoas major and minor and semitendinosus muscles during cold storage. Pol. J. Food Nutr. Sci., 2003, 12/53, 57-61.
  • [36] Kołczak T., Palka K., Zarzycki A.: Wpływ kolagenu śródmięśniowego na kruchość i inne cechy sensoryczne mięśni bydła. Acta Agr. et Silv., ser. zootech., 1992, 30, 76-85.
  • [37] Kołczak T., Pospiech E., Palka K., Łącki J.: Changes of myofibrillar and centrifugal drip proteins and shear force of psoas major and minor and semitendinosus muscles from calves, heifers and cows during post-mortem ageing. Meat Sci., 2003, 64, 69-75.
  • [38] Kołczak T., Pospiech E., Palka K., Łącki J.: Changes in structure of psoas major and minor and semitendinosus muscles of calves, heifers and cows during post-mortem ageing. Meat Sci., 2003, 64, 77-83.
  • [39] Koohmaraie M.: Effect of pH, temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle mμ-calpain. J. Animal Sci., 1992, 70, 3071-3080.
  • [40] Koohmaraie M., Schollmeyer J.E., Dutson T.R.: Effect of low-calcium requiring calcium activated factor on myofibrils under varying pH and temperature conditions. J. Food Sci., 1986, 51, 28-32.
  • [41] Kristensen L., Purslow P.P.: The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins. Meat Sci., 2001, 58, 17-23.
  • [42] Larick D.K., Turner B.E.: Flavour characteristics of forage and grain-fed beef as influenced by phospholipid and fatty acid compositional differences. J. Food Sci., 1990, 55, 312-318.
  • [43] Lawrie R.A.: Meat Science. Pergamon Press, Oxford, 1985.
  • [44] Ledward D.A.: Post-slaughter influences on the formation of metmyoglobin in beef muscles. Meat Sci., 1985, 15, 149-171.
  • [45] 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.
  • [46] Light N.D., Champion A.E., Voyle C., Bailey A.J.: The role of epimysial, perimysial and endomysial collagen in determining texture of six bovine muscles. Meat Sci., 1985, 30, 1-12.
  • [47] Lonergan S.M., Huff-Lonergan E., Wiegand B.R., Kriese-Anderson L.A.: Post mortem proteolysis and tenderization of top loin steaks from brangus cattle. J. Muscle Foods, 2001, 12, 121-136.
  • [48] Lu J., Tan J., Shatadal P., Gerrard Gerard.E.: Evaluation of pork color by using computer vision. Meat Sci., 2000, 56, 57-60.
  • [49] Maddock K.R., Huff-Lonergan E., Rowe L.J., Lonergan S.M.: Effect of pH and ionic strength on μ- and m-calpain inhibition by calpastatin. J. Animal Sci., 2005, 83, 1370-1376.
  • [50] Madhavi D.L., Carpenter C.E.: Aging and processing affect color, metmyoglobin reductase and oxygen consumption of beef muscles. J. Food Sci., 1993, 58, 939-942.
  • [51] Mancini R.A., Hunt M.C.: Current research in meat color. Meat Sci., 2005, 71, 100-121.
  • [52] Marsh B.B.: The basis of tenderness in muscle foods. The basis of quality in muscle foods. J. Food Sci., 1977, 42, 295-297.
  • [53] McCornick R.J.: The flexibility of the collagen compartment of muscle. Meat Sci., 1994, 36, 79-91.
  • [54] McKenna D.R., Mies P.D., Baird B.E., Pfeiffer K.D., Ellebracht J.W., Savell J.W.: Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles. Meat Sci., 2005, 70, 665-682.
  • [55] Melody J.L., Lonergan S.M., Rowe L.J., Huiatt T.W., Mayes M.S., Huff-Lonergan E.: Early post mortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. J. Animal Sci., 2004, 82, 1195-1205.
  • [56] Miller M.F., Carr M.A., Ramsey C.B., Crockett K.L., Hoover L.C.: Consumer thresholds for establishing the value of beef tenderness. J. Amimal Sci., 2001, 79, 3062-3068.
  • [57] Nishimura T., Hattori A., Takahashi K.: Ultrastructure of the intramuscular connective tissue in bovine skeletal muscle. Acta Anatomica, 1994, 151, 250-227.
  • [58] Nishimura T., Hattori A., Takahashi K.: Structural weaking of intramuscular connective tissue during conditioning of beef. Meat Sci., 1995, 39, 127-133.
  • [59] Nishimura T., Hattori A., Takahashi K.: Relationship between degradatation of proteoglycans in basement membrane and intramuscular connective tissue of bovine semitendinosus muscle. Acta Anatomica, 1996, 155, 257-265.
  • [60] O'Grady M.N., Monahan F.J., Mooney M.T.: Oxymyoglobin in bovine muscle systems as affected by oxidizing lipids, vitamin E and metmyoglobin reductase activity. J. Muscle Foods, 2001, 12, 19- 35.
  • [61] O'Keeffe M., Hood D.E.: Biochemical factors influencing metmyoglobin formation in beef from muscles of differing colour stability. Meat Sci., 1982, 7, 209-228.
  • [62] O'Sullivan A., Byrne D.V., Martens H., Gidskehaug G.H., Andersen H.J., Martens M.: Evaluation of pork colour. Prediction of visual sensory quality of meat from instrumental and computer vision methods of colour analysis. Meat Sci., 2003, 65, 909-918.
  • [63] Ouali A., Demeyer D., Raichon C.: An introduction to the workship. Biochemie, 1992, 74, 213-215.
  • [64] Parr T., Sensky P., Kemp C., Bardsley R., Buttery P.: The molecular control and genetics of meat quality tenderization across species. Animal Sci., 2006, 1 (suppl.), 202-203.
  • [65] Purslow P.P.: Intramuscular connective tissue and its role in meat quality. Meat Sci., 2005, 70, 435- 447.
  • [66] Purslow P.P., Ertbjerg P., Baron C.P., Christensen M., Lawson M.A.: Patterns of variation in enzyme activity and cytoskeletal proteolysis in muscle. Proc. 47th Int. Congr. Meat Sci. Technol., Kraków, 2001, pp. 38-43.
  • [67] Raes K., Haak L., Balcaen A., Claeys E., Demeyer D., De Smet S.: The effect of feeding lenseed at similar linoleic acid levels on the fatty acid composition of double-muscled Belgian Blue young bulls. Meat Sci., 2004, 66, 307-315.
  • [68] Reddy I.M., Carpenter C.E.: Determination of metmyoglobin reductase activity in bovine skeletal muscles. J. Food Sci., 1991, 56, 1161-1164.
  • [69] Renerre M., Labas R.: Biochemical factors influencing metmyoglobin formation in beef muscles. Meat Sci., 1987, 19, 151-165.
  • [70] Roncales P., Geesink G.H., van Laack R.L.J.M., Jaile I., Beltran J.A., Barnier V.M.H., Smulders F.J.M.: Meat tenderization: enzymatic mechanisms. In: Ouali A., Demeyer D.I., Smulders F.J.M. (Eds.). Expression of tissue proteinases and regulation of protein degradation as related to meat quality. ECCEAMST series, 1995, pp. 311-330.
  • [71] Schmidt J.M., Zhang L., Lee H.S., Stromer M.H., Robson R.M.: Interaction of titin with actin: sensitive modulation of filament crosslinking activity. Arch. Biochem. Biophys., 1999, 366, 139-150.
  • [72] Scollan N.D., Wood J.D.: Enhancing the nutritional value of beef and its relationships with meat quality. Animal Sci., 2006, 1, suppl., 83-85.
  • [73] Scollan N.D., Choi N.J., Kurt E., Fisher A.V., Enser M., Wood J.D.: Manipulating the fatty acid composition of muscle and adipose tissue in beef cattle. Br. J. Nutr., 2001, 85, 115-124.
  • [74] Scollan N.D., Hocquette J.F., Nuernberg K., Dannenberger D., Richardson I., Moloney A.P.: Innovations in beef production systems that enhance the nutritional value of beef and its relationship with meat quality. Meat Sci., 2006, 74, 17-33.
  • [75] Sensky P.L., Parr T., Bardsley R.G., Buttery P.J.: The relationship between plasma epinephrine concentration and the activity of the calpain enzyme system in porcine longissimus muscle. J. Animal Sci., 1996, 74, 380-387.
  • [76] Sentandreu M.A., Coulis G., Ouali A.: Role of muscle andopeptidases and their inhibitors in meat tenderness. Trends in Food Science and Technology, 2002, 13, 400-421.
  • [77] Shirabe K., Yubisui T., Borgese N., Tang C.-Y., Hultquist D., Takeshita M.: Enzymatic instability of NADH-cytochrome b5 reductase as a case of hereditary methemoglonemia type I (Red Cell Type). J. Biol. Chem., 1992, 267, 20416-20421.
  • [78] Takahashi K.: Structural weakening of skeletal muscle tissue during post-mortem ageing of meat. The non-enzymatic mechanism of meat tenderization. Meat Sci., 1996, 43 S, 67-80.
  • [79] Taylor R.G., Geesing G.H., Thompson V.F., Koohmaraie M., Goll D.E.: Is Z-disk degradation responsible for post-mortem tenderization? J.Animal Sci., 1995, 73, 1351-1358.
  • [80] Whipple G., Koohmaraie M., Dikeman M.E., Crouse J.D., Hunt M.C., Klemm R.D.: Evaluation of attributes that affect longissimus muscle tenderness in bos taurus and bos indicus cattle. J. Animal Sci., 1990, 68, 2716-2724.
  • [81] Williams S.N., Frye T.M., Frigg M., Schefer D.M., Scheller K.K., Liu Q.: Vitamin E. Meat Focus International, 1992, 3 (2), 22-23.
  • [82] Zając M.: Porównanie jakości wybranych mięśni bydlęcych. Praca doktorska, AR Kraków, 2007.
  • [83] Zu L.G., Brewer M.S.: Metmyoglobin reducting capacity of fresh normal, PSE and DFD pork during retail disply. J. Food Sci., 1998, 63, 390-393.
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