BazEkon - Biblioteka Główna Uniwersytetu Ekonomicznego w Krakowie

BazEkon home page

Meny główne

Lesiów Tomasz
Prognozowanie jakości wyrobów z mięsa kurcząt na podstawie reologicznych właściwości homogenatów
Predicting Quality of Final Products From Poultry Meat on the Basis of Muscle Homogenate Rheological Properties.
Prace Naukowe Akademii Ekonomicznej we Wrocławiu. Seria : Monografie i Opracowania (nr 139), 2001, nr 889, 134 s., rys., bibliogr. s.93-104, Aneks
Słowa kluczowe
Mięso drobiowe, Przemysł mięsny, Jakość mięsa, Badanie jakości mięsa, Technologia produkcji żywności, Przegląd literatury
Poultry meat, Meat industry, Meat quality, Meat quality tests, Food production technology, Literature review
Podjęto próbę ustalenia wpływu pH i siły jonowej na właściwości żelujące homogenatów mięśni piersiowych i udowych kurcząt przy pośrednim stężeniu białka (4,5%) oraz wpływu typu mięśnia i zróżnicowanej ilości solanki peklującej o zmiennym składzie na jakość modelowych wędlin drobiowych.

In systems with low protein concentration, gel properties of poultry light and dark muscle myofibrillar proteins are influenced by muscle fibre type composition, pH and protein concentration. In systems with high protein concentration (myofibrils, comminuted and chopped meat) the rheological characteristics of thermally induced gels are the pH most dependent. There is lack of information about rheological properties of chicken muscle homogenates in the intermediate protein concentration range and final products processed from whole muscles. Therefore, the aim of this study was to measure influence of pH from 5,8 to 6,6 and ionic strength from 0,05 to 0,67 on apparent viscosity and gelation properties of chicken breast and thigh muscle homogenates at 4,5% protein concentration; examine two heating methods on cooking losses and shear force of light and dark muscles and coarsely ground model products manufactured with 2% NaCl or cured; and use of two different in composition curing brines on color and texture of model poultry products, i.e., filet (breast muscles) and ham (mixture of breast and leg muscles at ratio 1:1). Moreover, the gelation properties of muscle homogenates gels measured by penetration method and dynamic thermomechanical analysis (TMA) were compared with parameters of mechanical properties of final products measured by instrumental texture profile analysis (TPA), test F40 (40% sample compression) and shear force. The type of muscle, pH and ionic strength of extraction solutions had pronounced influence on rheological properties of meat homogenates. Breast muscle homogenates exhibited optimal rheological properties (apparent viscosity and gelation) at pH 6,3 and thigh at pH 6,0-6,3. These properties were influenced by increase of amount of bound water by muscle homogenates and decrease of amount of extractable proteins occurring simultaneously with increase in pH. The rheological properties of breast muscle homogenates were lower than thigh ones at pH 5,8 and 6,0, and were better at pH 6,3. The muscle type, its pH and form (whole or comminuted) and heating procedure applied, influenced cooking losses and shear force of model products. Also, muscle type and/or pH, as well as type and amount of curing brine influenced color and mechanical properties of commercially manufactured final model products. The textural properties of model filet (pH 6,35) produced with brine A were insignificantly higher than model ham (pH 6,50). Therefore, no relationship was found between both muscle homogenate gelation properties at different pH and textural properties of final model products processed with brine A. Model fillet (pH 6,25) produced with brine B had better textural properties than model ham (pH 6,39), what was in accordone with better gelation properties of breast muscle homogenates at pH 6,3 than thigh at pH 6,3-6,6, however, the protein content in model ham was not comparable with model filet (lower by 1,5%). To guarantee high quality of final products it is important: to eliminate of PSE and DFD muscles, to use functional additives and to control brine pH at level which will promote extractability and secure proteins water binding during curing and tumbling, as well as desired matrix formation during heat treatment. Poultry processors in Poland are faced with problem of defective meat (PSE, DFD). In 1999 the economical losses associated with the processing of PSE meat by polish poultry industry were equall of 0,76% for chicken breast muscles and 3,31% for turkey breast muscles in relation to the poultry livestock value. Therefore, reduction of preslaughter stress, fast postslaughter chilling technologies and sorting-out PSE and DFD meat from normal (use of pH or lightness L* characteristic), may result in advatages in processing of higher quality products and substantial reduction of economic losses. The results and technological observations gathered in this studies will provide processors with more options to utilize PSE meat in products of similar quality as those made from normal meat. (original abstract)
Dostępne w
Biblioteka Główna Uniwersytetu Ekonomicznego w Krakowie
Biblioteka Główna Uniwersytetu Ekonomicznego w Poznaniu
Biblioteka Główna Uniwersytetu Ekonomicznego we Wrocławiu
  1. Aberle E.D., Addis P.B., Shoffner R.N., 1979. Fiber types in skeletal muscles of broiler- and layer-type chickens. Poultry Science, 58, 1210-1212.
  2. Acton J.C., Hanna M.A., Satterlee L.D., 1981. Heat-induced gelation and protein-protein interaction of actomyosin. J. Food Biochem., 5, 101-113.
  3. Acton J.C., Ziegler G.R., Burge Jr.D.L., 1983. Functionality of muscle constituents in the processing of comminuted meat products. CRC Crit. Rev. Food Sei. Nutr., 18, 99-121.
  4. Acton J.C., Dick R.L., 1986. Thermal transitions of natural actomyosin from poultry breast and thigh tissues. Poultry Science, 65, 2051-2055.
  5. Allen C.D., Russell S.M., Fletcher D.L., 1997. The relationship of broiler breast meat color and pH to shelf-life and odor development. Poultry Science, 76,1042-1046.
  6. Allen C.D., Fletcher D.L., Northcutt J.K., Russell S.M., 1998. The relationship of broiler breast color to meat quality and shelf-life. Poultry Science, 77, 361-366.
  7. Alvarado C.Z., Sams A.R., 2000. Injection marination strategies for remediation of PSE broiler breast meat. Poultry Science, 79 (Suppl.l), Abstract 231, 53.
  8. Amato P.M., Hamann D.D., Ball Jr. H.R., Foegeding E.A., 1989. Influence of poultry species, muscle groups, and NaCl level on strength, deformability, and water retention in heat-set muscle gels. J. Food Sei., 54, 1136-1140, 1157.
  9. Anon., 1997. Mięso wieprzowe o cechach PSE. Mięso i Wędliny, Nr 4, 26-32.
  10. AOAC. Official Methods of Analysis. 15th Ed. Assoc. of Official Analytical Chemists, 1999, Washington, DC.
  11. Asghar A., Morita J.I., Samejima K., Yasui T., 1984. Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress. Agric. Biol. Chem., 48, 2217-2224.
  12. Babji A.S., Froning G.W., Ngoka D.A., 1982. The effect of preslaughter environmental temperature in the presence of electrolyte treatment on turkey meat quality. Poultry Science, 61,2385-2389.
  13. Barbut S., 1993. Colour measurements for evaluating the pale soft exudative (PSE) occurrence in turkey meat. Food Res. Int., 26, 39-43.
  14. Barbut S., 1996. Estimates and detection of the PSE problem in young turkey breast meat. Can. J. Anim. Sei., 76, 455-457.
  15. Barbut S., 1997. Occurrence of pale soft exudative in mature turkey hens. Br. Poultry Sei., 38, 74-77.
  16. Barbut S., 1997a. Problem of pale soft exudative meat in broiler chickens. Br. Poultry Sei., 38, 355-358.
  17. Barbut S., 1998. Estimating the magnitude of the pale soft exudative problem in poultry. J. Muscle Foods, 9, 35-49.
  18. Barbut S., Mittal G.S., 1990. Effect of heating rate on meat batter stability, texture and gelation. J. Food Sei., 55, 334-337.
  19. Barbut S., Mittal G. S., 1993. Effects of pH on physical properties of white and dark turkey meat. Poultry Science, 72, 1557-1565.
  20. Bauermeister L.J., Lewis S.J., McKee S.R., 2000. Using microbial transglutaminase to improve meat binding characteristics of PSE poultry meat. Poultry Science, 79 (Suppl.l), Abstract 32, 53.
  21. Boles J.A., Parrish F.C., Huiatt T.W., Robson R.M., 1992. Effect of porcine stress syndrome on the solubility and degradation of myofibrillar/cytoskeletal proteins. J. Animal Sei., 70, 454-464.
  22. Boulianne M., King A.J., 1995. Biochemical and color characteristics of skinless boneless pale chicken breast. Poultry Science,74, 1693-1698.
  23. Boulianne M., King A.J., 1998. Meat color and biochemical characteristics of unacceptable dark-colored broiler chicken carcasses. J. Food Sei., 63, 759-762.
  24. Bourne M.C., 1978. Texture profile analysis. Food Technol., 32, 62-66, 72.
  25. Boyer C., Joandel S., Rousssilhes V., Culioli J., Ouali A., 1996. Heat-induced gelation of myofibrillar proteins and myosin from fast- and slow-twitch rabbit muscles. J. Food Sei., 61, 1138-1142, 1164.
  26. Boyer C., Joandel S., Culioli J., Ouali A., 1996a. Ionic strength effects on heat-induced gelation of myofibrils and myosin from fast- and slow-twitch rabbit muscles. J. Food Sei., 61, 1143-1148.
  27. Boyer C., Joandel S., Ouali A., Culioli J., 1996b. Determination of surface hydrophobicity of fast and slow myosins from rabbit skeletal muscles: Implication in heat-induced gelation. J. Sei. Food Agric., 72, 367-375.
  28. Camou J.P., Sebranek J.G., Olson D.G., 1989. Effect of heating rate and protein concentration on gel strength and water loss of muscle protein gels. J. Food Sei., 54, 850-854.
  29. Chen M.-T., Lin S-S., Lin L-C., 1991. Effect of stresses before slaughter on changes to the physiological, biochemical and physical characteristics of duck muscle. Br. Poultry Sei., 32, 997-1004.
  30. Culioli J., Boyer C., Vignon X., Ouali A., 1993. Heat-induced gelation properties of myosin: Influence of purification and muscle type. Sei. Aliments., 13, 249-260.
  31. Cybulska E. B., 2000. Woda jako składnik żywności. W: Chemia Żywności. Red. Z. E. Sikorski. WNT, Warszawa.
  32. Daum-Thunberg D.L., Foegeding E.A., Ball JR. H.R., 1992. Rheological and water-holding properties of comminuted turkey breast and thigh: Effects of initial pH. J. Food Sei., 57, 333-337.
  33. Dawson P.L., Sheldon B.W., Ball Jr. H.R., 1990. Effect of washing and adding spray-dried egg white to mechanically deboned chicken meat on the quality of cooked gels. Poultry Science, 69, 307-312.
  34. deFremery D., Pool M. F., 1960. Biochemistry od chicken muscle as related to rigor-mortis and tenderization. Food Res., 25, 73-87.
  35. De Lamballerie M., Chraiti F., Culioli J., Ouali A., 1993. Gelification de protéines myofibrillaires bovines. Sei. Aliments, 13, 237-247.
  36. Duda Z., 1998. Dodatki funkcjonalne w przetwórstwie mięsa. Część I. Gospodarka Mięsna, 50, 32-37.
  37. Duda Z., 1998a. Dodatki funkcjonalne w przetwórstwie mięsa. Część II. Gospodarka Mięsna, 50, 40-47.
  38. Duda Z., 1998b. Wybrane zagadnienia stosowania azotynu w przetwórstwie mięsa. Żywność. Technologia. Jakość, 5 (3), 5-42.
  39. Dudziak J.A., Foegeding E.A., 1988. Isolation of actomyosin and myosin from post-rigor turkey breast and thigh. J. Food Sei., 53, 1287-1289, 1339.
  40. Dudziak J.A., Foegeding E.A., Knopp J.A., 1988. Gelation and thermal transitions in post-rigor turkey myosin/actomyosin suspensions. J. Food Sei., 53, 1278-1281, 1332.
  41. Dybowski G., Kobuszyńska M., Nosecka B., Świetlik K., 2000. Rynek drobiu i jaj. IBRiGŻ, 18, 1-32.
  42. Egelandsdal B., Fretheim K., Samejima K., 1986. Dynamie rheological measurements on heat-induced myosin gels: Effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate. J. Sei. Food Agric., 37, 915-926.
  43. Ferry J.D., 1948. Protein gels. Adv. Protein Chetn., 4, 1-78.
  44. Fletcher D.L., 1991. Ante mortem factors related to meat quality. Proc. 37th ICoMST, Kulmbach, Germany, 11-19.
  45. Fletcher D.L., 1992. The influence of ante-mortem and post-mortem factors on broiler meat quality. Proc. 19th World's Poultry Congress, Amsterdam, The Netherlands, 3, 37-41.
  46. Fletcher D.L., 1995. Relationship of breast meat color variation to muscle pH and texture. Poultry Science, 74 (Suppl. 1), Abstract 120.
  47. Fletcher D.L., 1999. Broiler breast meat color variation, pH and texture. Poultry Science, 78, 1323-1327.
  48. Foegeding E.A., 1987. Functional properties of turkey salt-soluble proteins. J. Food Sei., 52, 1495-1499.
  49. Foegeding E.A., 1988. Thermally induced changes in muscle proteins. Food Technol., 42, 58, 60-62, 64.
  50. Foegeding E.A, Ramsey S.R., 1987. Rheological and water-holding properties of gelled meat batters containing iota carrageenan, kappa carrageenan or xanthan gum. J. Food Sei., 52, 549-553.
  51. Foegeding E.A, Liu M.N., 1995. Functional differences of myofibrillar proteins from fast and slow twitch muscles. J. Muscle Foods, 6, 109-123.
  52. Foegeding E.A., Allen C.E., Dayton W.R., 1986. Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels. J. Food Sei., 51, 104-108, 112.
  53. Fretheim K., Samejima K., Egelandsdal B., 1986. Myosins from red and white bovine muscles: Part I-Gel strength (elasticity) and water-holding capacity of heat-induced gels. Food Chem., 22, 107-121.
  54. Froning G.W., Norman G., 1966. Binding and water retention properties of light and dark chicken meat. Poultry Science, 45, 797-800.
  55. Froning G.W., Babji A.S., Mather F.B., 1978. The effect of preslaughter temperature, stress, struggle and anaesthetization on colour and textural characteristics of turkey muscle. Poultry Science, 57, 630-633.
  56. Froning G.W., Uijttenboogaart T.G., 1988. Effect of post-mortem electrical stimulation on color, texture, pH, and cooking losses of hot and cold deboned chicken broiler breast meat. Poultry Science, 67, 1536-1544.
  57. Gao J.C., Pigott G.M., Reine B., 1999. Gel forming additive effects on properties of thermally induced minced fish gels. J. Food Sei., 64, 414-417.
  58. Giese J., 1995. Measuring physical properties of foods. Food Technol., 49, 54-63.
  59. Górska-Warsewicz H., 2000. Konsument na rynku mięsa i przetworów drobiowych. Przemysł Spożywczy, 54, 8-9.
  60. Grabowski T, 1993. Surowiec do produkcji mięsa drobiowego. W: Technologia mięsa drobiowego. Red. T. Grabowski. WNT, Warszawa.
  61. Hay J.D., Currie R.W., Wolfe F.H, Sanders E.J., 1973. Effect of postmortem aging on chicken muscle fibrils. J. Food Sei., 38, 981-986.
  62. Hay J.D., Currie R.W., Wolfe F.H., 1973a. Polyacrylamide disc gel electrophoresis of fresh and aged chicken muscle proteins in sodium dodecylsulfate. J. Food Sei., 38, 987-990.
  63. Hermansson A.M., Harbitz O., Langton M., 1986. Formation of two types of gels from bovine myosin. J. Sei. Food Agric., 37, 69-84.
  64. Honikel K.O., 1987. Critical evaluation of methods detecting water-holding capacity in meat. In: Accelerated processing of meat. Ed. A. Romita, C. Valin, A.A. Taylor. Elsevier Applied Science, London and New York, 225-239.
  65. Hoogenkamp H.W., 1998. Innowacje w dziedzinie wyrobów z mięsa drobiowego. Część I. Mięso i Wędliny, Nr 4, 36-39.
  66. Hudspeth J.P., May K.N., 1967. A study of the emulsifying capacity of salt soluble proteins of poultry meat. 1. Light and dark meat tissues of turkeys, hens, and broilers, and dark meat tissues of ducks. Food Technol., 21, 1141-1142.
  67. Inklaar P.A., Fortuin J., 1969. Determining the emulsifying and emulsion stabilizing capacity of proteins meat additives. Food Technol., 23, 103-105.
  68. Ishioroshi M., Samejima K., Yasui T., 1979. Heat-induced gelation of myosin: Factors of pH and salt concentrations. J. Food Sei., 44, 1280-1284.
  69. Ishioroshi M., Samejima K., Yasui T., 1983. Heat-induced gelation of myosin filaments at a low salt concentration. Agric. Biol. Chem., 47, 2809-2816.
  70. Jankiewicz L., Słowiński M., 1999. Technologia produkcji wędlin. Część 2. Wędzonki parzone. PWF, Warszawa.
  71. Kannan G., Heath J.L., Wabeck C.J., Souza M.C.P., Howe J.C., Mench J.A., 1997. Effects of crating and transport on stress and meat quality characteristics in broilers. Poultry Science, 76, 523-529.
  72. Khan A.W., 1962. Extraction and fractionation of proteins in fresh chicken muscle. J. Food Sei., 27, 430-433. (Chan, A.W., 1971. Effects of temperature during post-mortem glycolysis and dephosphorylation of high energy phosphates on poultry meat tenderness. J. Food Sei., 36, 120-121.
  73. Kiessling K.H., 1977. Muscle structure and function in the goose, quail, pheasant, guinea hen, and chicken. Comp. Biochem. Physiol., 57B, 287-292.
  74. Kijowski J., 1996. Zagadnienia surowcowe, technologiczne i marketingowe w przetwórstwie mięsa drobiowego. Gospodarka Mięsna, 48, 30-37, 40.
  75. Kijowski J., 1999. Systemy produkcji drobiu i produktów drobiarskich o gwarantowanej jakości. Mięso i Wędliny, Nr 2, 50-56.
  76. Kijowski J., 2000. Wartość żywieniowa mięsa drobiowego. Przemysł Spożywczy, 54, 10-12.
  77. Kijowski J., Niewiarowicz A., 1978. Emulsifying properties of proteins and meat from broiler breast muscle as affected by their initial pH values. J. Food Technol., 13, 451-459.
  78. Kijowski J.M., Mast M.G., 1988. Thermal properties of proteins in chicken broiler tissue. J. Food Sei., 53, 363-366.
  79. Kijowski J.M., Mast M.G., 1988a. Effect of sodium chloride and phosphate on the thermal properties of chicken meat proteins. J. Food Sei., 53, 367-370, 387.
  80. Kolczak J., 2000. O lepszą jakość wędlin. Gospodarka Mięsna, 52, 40, 42, 44.
  81. Kopeć W., 1998. Charakterystyka biofizykochemiczna i właściwości żelujące precypitatów aktomiozyny mięśni kurcząt. Zeszyty Naukowe AR we Wrocławiu, Nr 341, 1-103.
  82. Kotarbiński T, 1982. Traktat o dobrej robocie. Zakład Narodowy im. Ossolińskich, Wrocław-Warszawa-Kraków-Gdańsk-Łódź.
  83. Kozioł J., 1985. Mięso i produkty mięsne. W: Towaroznawstwo. Produkty spożywcze. Red. A. Lempka. PWE, Warszawa.
  84. Lachowicz K, Gajowiecki L., Sobczyk M., Oryl B., 1999. Wpływ dodatku karagenu na teksturę kiełbasy parówkowej o zróżnicowanej zawartości wody i tłuszczu. Żywność, l (18), 25-37.
  85. Lan Y.H., Novakofski J., McCusker R.H., Brewer M.S., Carr T.R., McKeith F.K., 1995. Thermal gelation properties of protein fractions from pork and chicken breast muscles. J. Food Sei., 60, 742-747, 752.
  86. Lan Y.H., Novakofski J., McCusker R.H., Brewer M.S., Carr T.R., McKeith F.K., 1995a. Thermal gelation of pork, beef, fish, chicken and turkey muscles as affected by heating rate and pH. J. Food Sei., 60, 936-940, 945.
  87. Lan Y.H., Novakofski J., McCusker R.H., Brewer M.S., Carr T.R., McKeith F.K., 1995b. Thermal gelation of myofibrils from pork, beef, fish, chicken and turkey. J. Food Sei., 60, 941-945.
  88. Lavelle C.L., Foegeding E.A., 1993. Gelation of turkey breast and thigh myofibrils: Effects of pH, salt and temperature. J. Food Sei., 58, 727-730, 760.
  89. Lawrie R.A., 1998. The conversion of muscle to meat. In: Lawrie's Meat Science. 6th ed. Woodhead Publishing Ltd., Cambridge, England, 97-118.
  90. Lee Y.B., Hargus G.L., Hageberg E.G., Forsythe R.H., 1976. Effect of antemortem environmental temperatures on postmortem glycolysis and tenderness in excised broiler breast muscle. J. Food Sei.,41, 1466-1469.
  91. Lefevre F., Fauconneau B., Ouali A., Culioli J., 1998. Thermal gelation of brown trout myofibrils: Effect of muscle type, heating rate and protein concentration. J. Food Sei., 63, 299-304.
  92. Leman J., 1999. Funkcjonalne właściwości białek serwatkowych. Przemysł Spożywczy, 53, 5, 45-49.
  93. Lesiów T., 1993. Comparison of changes occurring in functional properties of nutria meat cured by dry method and beef cured without or with the participation of enzymatic preparation. Nahrung, 37, 476-483.
  94. Lesiów T., 1996. Rola kalpain w skruszaniu mięsa. Prace Naukowe AE, Technologia l, Wrocław, 728, 185-197.
  95. LesiówT., 2000. Apparent viscosity of chicken muscle homogenates. Influence of pH and muscle type. Nahrung, 44, 328-332.
  96. LesiówT., 2000a. Gelation of chicken breast and thigh muscle homogenates: Effect of pH and time of aging. Nahrung, 44, 426-430.
  97. Lesiów T., Skrabka-Błotnicka T., 1984. Studies on gel forming capacities of muscular proteins of nutria. Acta Alimentaria Polonica, X, 3-4, 311-321.
  98. Lesiów T., Pietrasik Z., 2000. Wpływ solanki i innych dodatków na smak wędlin drobiowych. Magazyn Przemysłu Spożywczego, 6, 15-18.
  99. Lesiów T., Xiong Y.L., 2000. Gelation properties of poultry myofibrillar proteins and comminuted poultry meat: Effect of protein concentration, pH and muscle type. A review (w druku: Fleischwirtschaft).
  100. Lesiów T., Xiong Y. L., 2000a. Mechanism of rheological changes in poultry myofibrillar proteins during gelation: A review (w druku: Poultry and Avian Biology Reviews).
  101. Liu M.N., Foegeding E.A., 1996. Denaturation and aggregation of chicken myosin isoforms. J. Agric. Food Chem., 44, 1435-1440.
  102. Liu M.N., Foegeding E.A., 1996a. Thermally induced gelation of chicken myosin isoforms. J. Agric. Food Chem., 44, 1441-1446.
  103. Liu G., Xiong Y.L., 1996b. Contribution of lipid and protein oxidation to rheological differences between chicken white and red muscle myofibrillar proteins. J. Agric. Food Chem., 44, 779-784.
  104. Liu G., Xiong Y.L., 1997. Gelation of chicken muscle myofibrillar proteins treated with protease inhibitors and phosphates. J. Agric. Food Chem., 45, 3437-3442.
  105. Lyon C.E., Towsend W.E., Wilson Jr. R.L., 1976. Objective color values of non-frozen and frozen broiler breasts and thighs. Poultry Science, 55, 1307-1312.
  106. Lyon C.E., Hamm D., Thomson J.E., 1984. The effects of holding time and added salt on pH and functional properties of chicken meat. Poultry Science, 63, 1952-1957.
  107. Lyon B.G., Lyon C.E., 1993. Effects of water-cooking in heat-sealed bags versus conveyor-belt grilling on yield, moisture, and texture of broiler breast meat. Poultry Science, 72, 2157-2165.
  108. Ma R.T-L, Addis P.B., Allen E., 1971, Response to electrical stimulation and post-mortem changes in turkey pectoralis major muscle. J. Food Sei., 36, 125-129.
  109. Ma R.T-L, Addis P.B., 1973. The association of struggle during exsanguination to glycolysis, protein solubility and shear in turkey pectoralis muscle. J. Food Sei., 38, 995-997.
  110. Macfarlane J.J., Schmidt G.R., Turner R.H., 1977. Binding of meat pieces: A comparison of myosin, actomyosin and sarcoplasmic proteins as binding agents. J. Food Sei., 42, 1603-1605.
  111. Maesso E.R., Baker R.C., Vadehra D.V., 1970. The effect of vacuum, pressure, pH and different meat types on the binding ability of poultry meat. Poultry Science, 49, 697-700.
  112. Mallia J.G., Barbut S., Vaillancourt J.-P., Martin S.W., McEwen S.A., 2000. A dark, firm dry-like condition in turkeys condemned for cyanosis. Poultry Science, 79, 281-285.
  113. Mallia J.G., Barbut S., Vaillancourt J.-P., Martin S.W., McEwen S.A., 2000a. Roaster breast meat condemned for cyanosis: A dark firm dry-like condition? Poultry Science, 79, 908-912.
  114. Mallia J.G., Hunter B., Vaillancourt J.-R, Irwin R., Muckle C.A., Martin S.W., McEwen S.A., 2000b. Bacteriological and histological profile of turkeys condemned for cyanosis. Poultry Science, 79, 1194-1199.
  115. Maruyama K., Kanemaki N., 1991. Myosin isoform expression in skeletal muscles of turkeys at various ages. Poultry Science, 70, 1748-1757.
  116. Maurer A.J., Baker R.C., Vadehra D.V., 1969. The influence of type of poultry and carcass part on the extractability and emulsifying capacity of salt-soluble proteins. Poultry Science, 48, 994-997.
  117. McCormick R.J., 1999. Extracellular modifications to muscle collagen: Implications for meat quality. Poultry Science, 78, 785-791.
  118. McCready S.T., Cunningham F.E., 1971. Salt-soluble proteins of poultry meat. 1. Composition and emulsifying capacity. Poultry Science, 50, 243-249.
  119. McCurdy R., Barbut S., Quinton M., 1996. Seasonal effect on pale soft exudative occurrence in young turkey breast meat. Food Res. Int. 29, 363-366.
  120. McKee S.R., Sams A.R., 1997. The effect of seasonal heat stress on rigor development and the incidence of pale, exudative turkey meat. Poultry Science, 76, 1616-1620.
  121. McKee S.R., Hirschler E.M., Sams A.R., 1997. Physical and biochemical effects.of broiler breast tenderization by aging after pre-rigor deboning. J. Food Sei., 62, 959-962.
  122. McKee S.R., Sams A.R., 1998. Rigor mortis development at elevated temperatures induces pale exudative turkey meat characteristics. Poultry Science, 77, 169-174.
  123. Michalski M.M., 1998. Karageny w przemyśle mięsnym. Gospodarka Mięsna, 50, 62, 66, 67.
  124. Molina M.L, Kropp K.E., Gulick J., Robbins J., 1987. The sequence of an embryonic myosin heavy chain gene and isolation of its corresponding cDNA. J. Biol. Chem., 14, 6478-6488.
  125. Monin G., 1998. Recent methods for predicting quality of whole meat. Meat Sei., 49 (Suppl. 1), S231-S243.
  126. Morita J.I., Choe Il-Shin., Yamamoto K., Samejima K., Yasui T., 1987. Heat-induced gelation of myosin from leg and breast muscles of chicken. Agric. Biol. Chem., 51, 2895.
  127. Murphy R.Y., Marks B.P., Marcy J.A., 1998. Apparent specific heat of chicken breast patties and their constituent proteins by different scanning calorimetry. J. Food Sei., 63, 88-91.
  128. Nakai S., Li-Chan E., Hayakawa S., 1986. Contribution of protein hydrophobicity to its functionality. Nahrung, 30, 327-336.
  129. Nakayama T., Sato Y., 1971. Relationships between binding quality of meat and myofibrillar proteins. 2. The contribution of native tropomyosin and actin to the binding quality of meat. Agric. Biol. Chem., 35, 208-218.
  130. Ndi E.E., Brekke C.J., 1992. Thermal aggregation properties of duck salt-soluble proteins at selected pH values. J. Food Sei., 57, 1316-1320.
  131. Ndi E.E., Brekke C.J., Barbosa-Canovas G.V., 1994. Thermal gelation of duck breast and leg muscle proteins. J. Muscle Foods, 5, 27-36.
  132. Newton K.G., Gill C.O., 1980/1981. The microbiology of DFD fresh meats: A review. Meat Sei., 5, 223-232.
  133. Ngoka D.A., Froning G.W., 1982. Effect of free struggle and preslaughter excitement on color of turkey breast muscles. Poultry Sei., 61, 2291-2293.
  134. Ngoka D.A., Froning G.W., Lowry S.R., Babji A.S., 1982. Effect of sex, age, preslaughter factors, and holding conditions on the quality characteristics and chemical composition of turkey breast muscles. Poultry Sei., 61, 1996-2003.
  135. Niewiarowicz A., 1973. Meat anomalies in broilers. Poultry Int., 17, 50-51.
  136. Niewiarowicz A., Trojan M., Kijowski J., Pikul J., 1973-1977. Biochemical, nutritive and technological characteristics of the chicken meat with the symptoms of muscle dystrophy. Project No. E-21-MQ-9. Grant No. FG-Po-282, 1-1-4.
  137. Northcutt J.K., Lavelle C.L., Foegeding E.A., 1993. Gelation of turkey breast and thigh myofibrils: Changes during isolation of myofibrils. J. Food Sei., 58, 983-986.
  138. Northcutt J.K., Foegeding E.A., Edens F.W., 1994. Water-holding properties of thermally preconditioned chicken breast and leg meat. Poultry Science, 73, 308-316.
  139. Nuckles R.O., Smith D.M., Merkel R.A., 1991. Properties of heat-induced gels from beef skeletal, heart, lung and spleen protein fractions. J. Food Sei., 56, 1165-1170.
  140. Obinata T., Masaki T., Takano H., 1979. Immunochemical comparison of myosin light chains from chicken fast white, slow red, and cardiac muscle. J. Biochem., 86, 131-137.
  141. Offer G., 1991. Modelling of the formation of pale, soft and exudative meat: Effects of chilling regime and rate and extent of glycolysis. Meat Sei., 30, 157-184.
  142. Offer G., Trinick J., 1983. On the mechanism of water holding in meat: The swelling and shrinking of myofibrils. Meat Sei., 8, 245-281.
  143. Oktaba W., 1980. Elementy statystyki matematycznej i metodyka doświadczalnictwa. PWE, Warszawa.
  144. Olszewski A., 1999. Pomiar pH jako miernik jakości mięsa i jego przetworów. Gospodarka Mięsna, 51,30-35.
  145. O'Neil E., Morrissey P.A., Mulvihill D.M., 1993. Heat-induced gelation of actomyosin. Meat Sei., 33, 61-74.
  146. O'Neil E., Mulvihill D.M., Morrissey P.A., 1994. Molecular forces involved in the formation and stabilization of heat-induced actomyosin gels. Meat Sei., 36, 407-421.
  147. Owens C.M., Sams A.R., 2000. The influence of transportation on turkey meat quality. Poultry Science, 79, 1204-1207.
  148. Owens C.M., Hirschler E.M., McKee S.R., Sams A.R., 1998. The incidence and characterization of pale, soft, exudative turkey in commercial plant. Poultry Science, 77 (Suppl. 1), Abstract 308,81.
  149. Owens C.M., McKee S.R., Matthews N.S., Sams A.R., 2000. The development of pale, exudative meat in two genetic lines of turkeys subjected to heat stress and its prediction by halothane screening. Poultry Science, 79, 430-435.
  150. Owens C.M., Hirschler E.M., McKee S.R., Martinez-Dawson R., Sams A.R., 2000a. The characterization and incidence of pale, soft, exudative turkey meat in a commercial plant. Poultry Science, 79, 553-558.
  151. Panasik M., Świderska J., 1996. Mięso drobiowe - zapiski technologa. Gospodarka Mięsna, 48, 20-21.
  152. Parsons N., Knight P., 1990. Origin of variable extraction of myosin from myofibrils treated with salt and pyrophosphate. J. Sei. Food Agric., 51, 71-90.
  153. Paxhia J.M., Parrish Jr. F.C., 1988. Effect of postmortem storage on titin and nebulin in pork and poultry light and dark muscles. J. Food Sei., 53, 1599-1601, 1670.
  154. Percival A.L., Williams A.J., Kenyon J.L., Grinsell M.M., Airey I.A., Sutko J.L., 1994. Chicken skeletal muscle ryanodine receptor izoforms: Ion channel properties. Biophysical J., 67, 1834-1850.
  155. Pietrzak M., Greaser M.L., Sosnicki A.A., 1994. Effect of rapid onset of rigor mortis on protein functionality in turkey breast muscle. Poultry Science, 73 (Suppl.1), Abstract 194, 65.
  156. Pietrzak M., Greaser M.L., Sosnicki A.A., 1997. Effect of rapid rigor mortis processes on protein functionality in pectoralis major muscle of domestic turkeys. J. Animal Sei., 75, 2106-2116.
  157. Pikul J., Leszczyński D.E., Bechtel P.J., Kummerow F.A., 1984. Effects of frozen storage and cooking on lipid oxidation in chicken meat. J. Food Sei., 49, 838-843.
  158. Pikul J., Niewiarowicz A., Góra A., Szczyrba R., 1988. Barwa mięsa kurcząt brojlerów podczas chłodniczego i zamrażalniczego przechowywania. Gospodarka Mięsna, 40, 23-26.
  159. Pikul J., 1996. Lipidy mięsa drobiu. Gospodarka Mięsna, 48, 28-34.
  160. Pośpiech E., Greaser M.L., Sosnicki A.A., 1995. Titin changes in turkey breast muscles varying in quality. J. Animal Sei., 73 (Suppl. 1), Abstract 205, 161.
  161. Pośpiech E., 1997. Analiza możliwości przetwarzania mięsa o obniżonej jakości. Gospodarka Mięsna, 49, 34-37.
  162. Pośpiech E., Grześ B., 1997. Wybrane białka cytoszkieletowe i ich rola w kształtowaniu właściwości funkcjonalnych tkanki mięśniowej. Żywność. Technologia. Jakość, 3 (12), 5-19.
  163. Pośpiech E., 2000. Diagnozowanie odchyleń jakościowych mięsa. Gospodarka Mięsna, 52, 68-71.
  164. Qiao M., Fletcher D.L., Smith O.P., Northcutt J.K., 2000. The influence of broiler breast meat color variation on chemical composition. Poultry Science, 79 (Suppl. 1), Abstract 230, 53.
  165. Rachwał A., 2000. Stres ptaków przyczyną znacznych strat ekonomicznych w produkcji drobiarskiej. Polskie Drobiarstwo, 10, 30-32.
  166. Rathgeber B.M., Boles J.A., Shand P.J., 1998. Rapid postmortem glycolysis and delayed chilling have detrimental effects on turkey muscle proteins. Poultry Science, 77 (Suppl. 1), Abstract 309, 81.
  167. Renerre M., 1990. Review: Factors involved in the discoloration of beef meat. Int. J. Food Sei. Tech., 25, 613-630.
  168. Richardson R.I., Jones J.M., 1987. The effects of salt concentration and pH upon water-binding, water-holding and protein extractability of turkey meat. Int. J. Food Sei. Tech., 22, 683-692.
  169. Richardson R.I., 1999. Poultry meat for further processing. Proc. XII Europ. Symp. on the Quality of Poultry Meat, 25-29 September, Zaragoza, 351-360.
  170. Rowe R.W.D., 1973. The ultrastructure of disks from white, intermediate, and red fibers of mammalian striated muscles. J. Cell Biology., 57, 261-277.
  171. Rushbrook J.I., Wadewitz A.C., Elzinga M., Yao T.-T, Somes Jr. R.G., 1988. Variability in the amino terminus of myosin light chain 1. Biochemistry, 27, 8953-8958.
  172. Rushbrook J.I., Weiss C.,Yao T.-T, 1990. Complexity of sarcomeric myosin species at the protein level. In: The Dynamic State of Muscle Fiber, Petta D., Ed., Walter de Gruyter, Berlin, 303.
  173. Sackett B.A.M., Froning G.W., Deshazer J.A., Struwe F.J., 1986. Effect of gaseous preslaughter environment on chicken broiler meat quality. Poultry Science, 65, 511-519.
  174. Samejima K., Ishioroshi M., Yasui T., 1981 Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J. Food Sei., 46, 1412-1418.
  175. Samejima K., Ishioroshi M., Yasui T., 1982. Heat-induced gelling properties of actomyosin: Effect of tropomyosin and troponin. Agric. Biol. Chem., 46, 535-540.
  176. Samejima K., Egelandsdal B., Fretheim K., 1985. Heat gelation properties and protein extractability of beef myofibrils. J. Food Sei., 50, 1540-1543, 1555.
  177. Samejima K., Oka Y, Yamamoto K., Asghar A., Yasui T., 1988. Effects of SH groups, E - NH2 groups, ATP, and myosin subfragments on heat-induced gelling of cardiac myosin and comparison with skeletal myosin and actomyosin gelling capacity. Agric. Biol. Chem., 52, 63-70.
  178. Sams A.R., Janky D.M., 1990. Research note: Simultaneous histochemical determination of three fiber types in single sections of broiler skeletal muscles. Poultry Science, 69, 1433-1436.
  179. Sams A.R., Janky D.M., 1991. Characterization of rigor mortis development in four broiler muscles. Poultry Science, 70, 1003-1009.
  180. Sams A., 1999. Looking for solutions pale meat, poor yield. Broiler Industry, November, 26-30.
  181. Sano T., Noguchi S.F., Matsumoto J.J., Tsuchiya T., 1990. Effect of ionic strength on dynamic viscoelastic behavior of myosin during thermal gelation. J. Food Sei., 55, 51-58, 70.
  182. Sante V., Bielicki G., Renerre M., Lacourt A., 1991. Post mortem evolution in the pectoralis muscle from two turkey breeds: A relationship between pH and colour. Proc. 37' ICoMST, Kulmbach, Germany, 3:36, 465-467.
  183. Sante V., Sosnicki A.A., Greaser M.L., Pietrzak M., Pośpiech E., Ouali A., 1995. Impact of turkey breeding and production on breast meat quality. Poultry Meat Quality. Proc. XII European Symposium on the Quality of Poultry Meat, Zaragoza, Spain, 151-156.
  184. Sato Y., Nakayama T., 1970. Discussion of the binding quality of minced meats based on their rheological properties before and after heating. J. Texture Studies, 1, 309-326.
  185. Schmidt G.R., Mawson R.F., Siegel D.O., 1981. Functionality of a protein matrix in comminuted meat products. Food Technol., 35, 235-237, 252.
  186. Sharp A. Offer G., 1992. The mechanism of formation of gels from myosin molecules. J. Sei. Food Agric., 58, 63-73.
  187. Shiga K., Kami T., Fuji M., 1988. Relation between gelation behavior of ground chicken muscle and soybean proteins and their differential scanning calorimetric studies. J. Food Sei., 53, 1076-1080.
  188. Siegel D.O., Theno D.M., Schmidt G.R., 1978. Meat Massaging: The effects of salt, phosphate and massaging on the presence of specific skeletal muscle proteins in the exudate of a sectioned and formed ham, J. Food Sei., 43, 327-330.
  189. Sikorski Z.E., 2000. Białka - budowa i właściwości. W: Chemia Żywności. Red. Z. E. Sikorski, WNT, Warszawa.
  190. Skrabka-Błotnicka T, 1986. Właściwości emulgujące i żelujące białek i mięśni drobiowych ze szczególnym uwzględnieniem drobiu wodnego. Badania porównawcze. Prace Naukowe AE, Nr 358, Seria: Monografie i opracowania nr 38, 1-74.
  191. Słowiński M., 2000. Jakość mięsa. Mięso i Wędliny, Nr 1, 51-52.
  192. Słowiński M., Mroczek J., 1997. Wybrane problemy jakości w przetwórstwie mięsa drobiowego. Przemysł Spożywczy, 51, 12-16.
  193. Słowiński M., Stolarski M., 1998. Przewodnictwo elektryczne i pH jako kryterium wstępnej oceny jakości technologicznej mięsa indyczego. Mięso i Wędliny, Nr 6, 40-44.
  194. Smith O.P., Fletcher D.L., 1988. Chicken breast muscle fiber type and diameter as influenced by age and intramuscular location. Poultry Science, 67, 908-913.
  195. Smith O.P., Fletcher D.L, Buhr R.J., Beyer R.S., 1993. Peckin duckling and broiler chicken Pectoralis muscle structure and composition. Poultry Science, 72, 202-208.
  196. Smyth A.B., Smith D.M., Vega-Warner V., O'Neil E., 1996. Thermal denaturation and aggregation of chicken breast muscle myosin and subfragments. J. Agric. Food Chem., 44, 1005-1010.
  197. Smyth A.B., O'Neil E., 1997. Heat-induced gelation properties of surimi from mechanically separated chicken. J. Food Sei., 62, 326-330.
  198. Smyth A.B., McCord A., O'Neil E., 1998. Heat-induced gelation properties of chicken breast muscle salt soluble proteins when mixed with ß-lactoglobulin or an a-lactalbumin enriched protein fraction. Meat Sei., 48, 135-147.
  199. Solomon M.B., Eastridge J.S., 1987. Occurrence of giant fibers in muscles from wild pigs native to the United States. Meat Sei., 20, 75-81.
  200. Solomon M.B., Van Laack R.L.J.M., Eastridge J.S., 1998. Biophysical basis of pale, soft, exudative (PSE) pork and poultry muscle: A review. J. Muscle Foods, 9, 1-11.
  201. Sosnicki A.A., Greaser M.L., Pietrzak M., Pośpiech E., 1995. Protein alterations in PSE turkey breast and porcine muscle. Meat Focus Int., May, 193-197.
  202. Sosnicki A.A., Greaser M.L., Pietrzak M., Pośpiech E., Sante V, 1998. PSE-like syndrome in breast muscle of domestic turkeys; A review. J. Muscle Foods, 9, 13-23.
  203. Sosnicki A.A., Wilson B.W., 1991. Pathology of turkey skeletal muscle: implications for the poultry industry. Food Structure, 10, 317-326.
  204. Staszczak M., Zdunek E., 1999. Proteoliza wewnątrzkomórkowa. Postępy Biochemii, 45, 32-41.
  205. Stone A.P., Stanley D.W., 1994. Muscle myosin gelation at low ionic strength. Food Res. Int., 27, 155.
  206. Swatland H.J., 1990. A note on the growth of connective tissue binding turkey muscle fiber together. Can. Inst. Food Sei. Techno!.J., 23, 239-241.
  207. Synowiecki J., Sikorska-Wiśniewska G., 1997. Funkcjonalne właściwości i żywieniowe zastosowanie hydrolizatów białkowych. Żywność. Technologia. Jakość, 3, 20-27.
  208. Szpendowski J., 1997. Hydrofobowość białek mleka a ich właściwości funkcjonalne. Przemysł Spożywczy, 51, 16-18, 31.
  209. Tanford C., 1980. The hydrophobic effect: Formation of micelles and biological membranes. 2nd ed. John Wiley and Sons, Inc., New York.
  210. Theno D.M., Siegel D.O., Schmidt G.R., 1978. Meat Massaging: Effect of salt and phosphate on the microstructural composition of the muscle exudate. J. Food Sei., 43, 483-487.
  211. Townsend W.E., Witnauer L.P., Riloff J.A., Swift C.E., 1968. Comminuted meat emulsions: differential thermal analysis of fat transitions. Food Technol., 22, 319-338.
  212. Trojan M., Niewiarowicz A., 1973. Badania wodnistości mięsa kurcząt. Roczniki Technologii i Chemii Żywności, Poznań, 23, 199-207.
  213. Vadehra D.V., McDonald B., Baker R.C., 1970: Biochemistry of avian meat hydration. 2. Factors affecting the hydration of broiler meat. Poultry Science, 49, Abstract, 1446.
  214. Van den Berg L., Lentz C.P., Khan A.W., 1964. Post-mortem changes in tenderness and waterholding and ion binding properties of poultry leg and breast meat. Food Technol. 18:573-575.
  215. Van Laack R.L.J.M., Lane J.L., 2000. Denaturation of myofibrillar proteins from chicken as affected by pH, temperature, and adenosine triphosphate concentration. Poultry Science, 79, 105-109.
  216. Van Laack R.L.J.M., Liu C.-H., Smith M.O., Loveday H.D., 2000. Characteristics of pale, soft, exudative broiler breast meat. Poultry Science, 79, 1057-1061.
  217. Walker J.M., Fletcher D.L., 1993. Effect of antemortem epinephrine injections on broiler breast meat color, pH and heme concentration. Poultry Science, 72 (Suppl. 1), Abstract 414, 138.
  218. Wang S.F., Smith D.M., Steffe J.F., 1990. Effect of pH on the dynamic rheological properties of chicken breast salt-soluble proteins during heat-induced gelation. Poultry Science, 69, 2220-2227.
  219. Wang S.F., Smith D.M., 1994. Poultry muscle proteins and heat-induced gelation. Poultry Sei. Rev., 5, 145-167.
  220. Wang S.F., Smith D.M., 1994a. Heat-induced denaturation and rheological properties of chicken breast myosin and F-actin in the presence and absence of pyrophosphate. J. Agric. Food Chem., 42, 2665-2670.
  221. Wang S.F., Smith D.M., 1995. Gelation of chicken breast muscle actomyosin as influenced by weight ratio of actin to myosin. J. Agric. Food Chem., 43, 331-336.
  222. Warriss P.D., Kestin S.C., Brown S.N., Bevis E.A., 1988. Depletion of glycogen reserves in fasting broiler chickens. Br. Poultry Sei., 29, 149-154.
  223. Warriss P.D., Kestin S.C., Brown S.N., Knowles T.G., Wilkins L.J., Edwards J.E., Austin S.D., Nicol C., 1993. The depletion of glycogen stores and indices of dehydration in transported broilers. Br. Vet. J., 149, 391-398.
  224. Warriss P.D., Wilkins L., Knowles T.G., 1999. The influence of ante-mortem handling on poultry meat quality. Poultry Meat Science. Poultry Science Symposium, Ed. Richardson, R.L, Mead G.C., 25, 217-230.
  225. Warriss P.D., Knowles T.G., Brown S.N., Edwards J.E., Kettlewell P.J., Mitchell M.A., Baxter C.A., 1999a. Effects of lairage time on body temperature and glycogen reserves of broiler chickens held in transport modules. Veterinary Record, 145, 218-222.
  226. Warriss P.D., 2000. Meat Sciente. An introductory text. CABI Publishing, Oxon.
  227. Weizsäcker E.U., Lovins A.B., Lovins L.H., 1999. Mnożnik cztery. Podwojony dobrobyt - dwukrotnie mniejsze zużycie zasobów naturalnych. Raport dla Klubu Rzymskiego. PTWKR, Toruń.
  228. Wierbicki E., Tiede M.G., Burrell R.C., 1962. Die Bestimmung der Fleischquellung als Methode zur Untersuchung der Wasserbindungskapazität von Muskelproteinen mit geringen salthaltevermögen. Fleischwirtschaft, 10, 948-951.
  229. Wilkins L.J., Brown S.N., Phillips A.J., Warriss P.D., 2000. Variation in the colour of broiler breast fillets in the UK. Br. Poultry Science, 41, 308-312.
  230. Wilson III G.G., van Laack R.L.J.M., 1999. Sarcoplasmic proteins influence water-holding capacity of pork myofibrils. J. Sei. Food Agric., 79, 1939-1942.
  231. Wiskus K.J., Addis PB., Ma R. T.-I., 1976. Distribution of ßR, αR and αW fibers in turkey muscles. Poultry Sei., 55, 562-572.
  232. Woelfel R.L, Owens C.M., Hirschler E.M., Sams A.R., 1998. The incidence and characterization of pale, soft and exudative chicken meat in commercial plant. Poultry Science, 77 (Suppl. 1), Abstract 235, 62.
  233. Woelfel R.L, Sams A.R., 1999. Marination performance of pale broiler breast meat. Poultry Science, 78 (Suppl. 1), Abstract 101, 24.
  234. Wu J.Q., Hamann D.D. and Foegeding E.A., 1991. Myosin gelation kinetic study based on rheological measurements. J. Agric. Food Chem., 39, 229-236.
  235. Xargayo M., Freixanet L., Lagares J., Fernandez E., De Jaeger-Ponnet P., 1998. Wirkung der Vormassage bei der Herstellung gegarter Fleischerzeugnisse aus ganzen Muskeln. Fleischwirtschaft, 78, 953-959.
  236. Xiong Y.L., 1992. Thermally induced interactions and gelation of combined myofibrillar protein from white and red broiler muscles. J. Food Sei., 57, 581-585.
  237. Xiong Y.L., 1993. A comparison of the rheological characteristics of different fractions of chicken myofibrillar proteins. J. Food Biochem., 16, 217-227.
  238. Xiong Y.L., 1994. Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing. CRC Crit. Rev. Food. Sei. Nutr., 34, 293-320.
  239. Xiong Y.L., 1997. Structure-function relationships of muscle proteins. Food proteins and their applications. Ed. S. Damodaran and A. Paraf, 341-392.
  240. Xiong Y.L., Blanchard S.P., 1992, Concentration-dependent thermal aggregation of muscle salt-soluble protein. Lebensm. Wiss. Technol., 25, 544-547.
  241. Xiong Y.L., Blanchard S.P., 1993. Viscoelastic properties of myofibrillar protein-polysaccharide composite gels. J. Food Sei., 58, 164-167.
  242. Xiong Y.L., Blanchard S.P., 1994. Dynamic gelling properties of myofibrillar protein from skeletal muscles of different chicken parts. J. Agric. Food Chem., 42, 670-674.
  243. Xiong Y.L., Blanchard S.P., 1994a. Rheological properties of salt-soluble protein from white and red skeletal muscles. J. Agric. Food Chem., 42, 1624-1628.
  244. Xiong Y.L., Blanchard S.P., 1994b. Myofibrillar protein gelation: Viscoelastic changes related to heating procedures. J. Food Sei., 59, 734-738.
  245. Xiong Y.L., Brekke C.J., 1989. Changes in protein solubility and gelation properties of chicken myofibrils during storage. J. Food Science, 54, 1141-1146.
  246. Xiong Y.L., Brekke C.J., 1990. Thermal transitions of salt-soluble proteins from pre- and postrigor chicken muscles. J. Food Sei., 55, 1540-1543, 1570.
  247. Xiong Y.L., Brekke C.J., 1990a. Physicochemical and gelation properties of pre- and postrigor chicken salt-soluble proteins. J. Food Sei., 55, 1544-1548.
  248. Xiong Y.L., Brekke C.J., 1991. Protein extractability and thermally induced gelation properties of myofibrils isolated from pre- and postrigor chicken muscles. J. Food Sei., 56, 210-215.
  249. Xiong Y.L., Decker E.A., 1995. Alterations of muscle protein functionality by oxidative and antioxidative processes. J. Muscle Foods, 6, 139-160.
  250. Xiong Y.L., Brekke C.J., Leung H. K., 1987. Thermal denaturation of muscle proteins from different species and muscle types as studied by differential scanning calorimetry. Can. Inst. Food Sei. Technol. J., 20, 357-362.
  251. Xiong Y.L., Cantor A.H., Pescatore A.J., Blanchard S.P., Straw M.L., 1993. Variations in muscle chemical composition, pH and protein extractability among eight different broiler crosses. Poultry Science, 72, 583-588.
  252. Xiong Y.L., Noel D.C., Moody W.G., 1999. Textural and sensory properties of low-fat beef sausages with added water and polysaccharides as affected by pH and salt. J. Food Sei., 64, 550-554.
  253. Yamamoto K., 1990. Electron microscopy of thermal aggregation of myosin. J. Biochem., 108, 896-898.
  254. Yang T.S., Froning G.W., 1992. Selected washing processes affect thermal gelation properties and microstructure of mechanically deboned chicken meat. J. Food Sei., 57, 325-329.
  255. Yang T.S., Froning G.W., 1992a. Effects of pH and mixing time on protein solubility during the washing of mechanically deboned chicken meat. J. Muscle Foods, 3, 15-23.
  256. Yasui T., Samejima K., 1990. Recent advances in meat science in Japan: Functionality of muscle proteins in gelation mechanism of structured meat products. Japan Agricultural Reseach Quaterly, 24, 131-140.
  257. Young O.A., Davey C.L., 1981. Electrophoretic analysis of proteins from single bovine muscle fibers. Biochem. J., 195, 317-327.
  258. Young O.A., Torley P.J., Reid, D.H., 1992. Thermal scanning rheology of myofibrillar proteins from muscles of defined fibre type. Meat Sei., 32, 45-63.
  259. Zezwolenie Głównego Inspektora Sanitarnego ZPU-4434-Ms.-33/IG/1999.
  260. Ziegler G.R., Acton J.C., 1984. Mechanisms of gel formation by proteins of muscle tissue. Food Technol., 38, 77-80, 82.
  261. Ziegler G.R., Foegeding E. A., 1990. The gelation of proteins. Adv. Food Nutr. Res., 34, 203-298.
  262. Zieliński R., Zieliński W., 1990. Tablice statystyczne. PWN, 274.
Cytowane przez
Udostępnij na Facebooku Udostępnij na Twitterze Udostępnij na Google+ Udostępnij na Pinterest Udostępnij na LinkedIn Wyślij znajomemu