Advertisement

Meat-Derived Protein Ingredients

  • Rodrigo Tarté

Introduction

Meat-derived protein ingredients are a group of high-protein ingredients derived primarily from meat animal by-products and sometimes from meat itself (Table 7.1). In order to adequately understand the status of these ingredients it helps understand how meat and its by-products are defined and regulated.
Table 7.1

Main types of nonmeat ingredients derived from edible animal by-products

Source

Ingredients

 

Blood

Blood plasma (liquid, frozen, dried) Whole blood (liquid and dried) Red cell protein (decolorized) Plasma transglutaminase

 

Bone

Gelatin (type B) Edible bone collagen (ossein) Bone collagen hydrolysates (stocks and broths) Edible bone phosphate Edible fat

 

Pig skin

Gelatin (type A) Stocks and broths

 

Beef hides

Gelatin (type B)

 

Poultry skin (chicken, turkey)

Concentrated collagen Stocks and broths Edible fat

 

Collagen-rich tissues

Concentrated collagen Collagen hydrolysates

 

Keywords

Myofibrillar Protein Gelatin Hydrolysate Blood Plasma Protein Meat Batter Plasma Protein Fraction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. Antoniewski, M. N., Barringer, S. A., Knipe, C. L., & Zerby, H. N. (2007) Effect of a gelatin coating on the shelf life of fresh meat. Journal of Food Science 72, E382—E387.Google Scholar
  2. Antonini, E., & Brunori, M. (1971). Hemoglobin and myoglobin in their reactions with ligands Amsterdam: North-Holland Publishing.Google Scholar
  3. Bailey, A. J., & Light, N. D. (1989). Connective tissue in meat and meat products. London: Elsevier Applied Science.Google Scholar
  4. Bailey, A.J., & Paul, R. G. (1998). Collagen: A not so simple protein. Journal of the Society of Leather Technologists and Chemists 82, 104–110.Google Scholar
  5. Bandman, E. (1987). Chemistry of animal tissues. Part 1 — Proteins. In J. F. Price & B. S. Schweigert (Eds.), The science of meat and meat products (3rd ed., pp. 61–101). Westport, CT: Food & Nutrition Press.Google Scholar
  6. Bechtel, P. J. (1986). Muscle development and contractile proteins. In P. J. Bechtel (Ed.), Muscle as food (pp. 1–35). Orlando, FL: Academic Press.Google Scholar
  7. Caldironi, H. A., & Ockerman, H. W. (1982). Incorporation of blood proteins into sausage. Journal of Food Science 47, 405倓408.Google Scholar
  8. Campbell, R. E., & Kenney, P. B. (1994). Edible by-products from the production and processing of muscle foods. In D. M. Kinsman, A. W. Kotula, & B. C. Breidenstein (Eds.), Muscle foods: Meat, poultry and seafood technology (pp. 79–10). New York: Chapman & Hall.Google Scholar
  9. Chen M. J., & Lin, C. W. (2002). Factors affecting the water-holding capacity of fibrinogen/ plasma protein gels optimized by response surface methodology. Journal of Food Science 67 2579–2582.Google Scholar
  10. CLITRAVI (Liaison Centre for the Meat Processing Industry in the E.U.). (2002). Guidance document on the application of Commission Directive 2001/101 of 26 November 2001 on the definition of meat amending Directive 2000/13 of 20 March 2000. Retrieved May 13, 2007, from http://www.fsai.ie/publications/guidance_notes/gn14_Clitravi.pdf
  11. Code of Federal Regulations. (2007a). Definitions. 9 C.F.R. § 301.2. Washington, DC: U.S. Government Printing Office.Google Scholar
  12. Code of Federal Regulations. (2007b). False or misleading labeling or practices generally; specific prohibitions and requirements for labels and containers. 9 C.F.R. § 317.8. Washington, DC: U.S. Government Printing Office.Google Scholar
  13. Code of Federal Regulations. (2007c). Determination of added water in cooked sausages. 9 C.F.R. § 318.22. Washington, DC: U.S. Government Printing Office.Google Scholar
  14. Code of Federal Regulations. (2007d). Mechanically separated (species). 9 C.F.R. § 319.5. Washington, DC: U.S. Government Printing Office.Google Scholar
  15. Code of Federal Regulations. (2007e). Cured pork products. 9 C.F.R. § 319.104. Washington, DC: U.S. Government Printing Office.Google Scholar
  16. Code of Federal Regulations. (2007f). Definitions. 9 C.F.R. § 381.1. Washington, DC: U.S. Government Printing Office.Google Scholar
  17. Code of Federal Regulations. (2007g). Mechanically separated (kind of poultry). 9 C.F.R. §381.173. Washington, DC: U.S. Government Printing OfficGoogle Scholar
  18. Code of Federal Regulations. (2007h). Use of food ingredients and sources of radiation. 9 C.F.R.§ 424.21. Washington, DC: U.S. Government Printing Office.Google Scholar
  19. Code of Federal Regulations. (2007i). Protein hydrolysates. 21 C.F.R. § 102.22. Washington, DC: U.S. Government Printing Office.Google Scholar
  20. Cole, C. G. B. (2000). Gelatin. In F. J. Francis (Ed.), Encyclopedia of Food Science and Technology (2nd ed., pp. 1183–1188). New York: John Wiley & Sons.Google Scholar
  21. Cole, C. G. B., & Roberts, J. J. (1996). Changes in the molecular composition of gelatine due to the manufacturing process and animal age, as shown by electrophoresis. Journal of the Society of Leather Technologists and Chemists 80, 136–141.Google Scholar
  22. Commission of the European Communities. (2006). Guidance note. Interpretation of Regulation 1774/2002/EC. Questions arising from FVO inspections to member states (2004–2005). Retrieved January 18, 2008, from the European Commission Health and Consumer Protection Directorate General Web Site: http://ec.europa.eu/food/food/biosafety/animalbyproducts/guidancefvomission_en.pdf
  23. Dàvila, E., Parés, D., Cuvelier, G., & Relkin, P. (2007). Heat-induced gelation of porcine blood plasma proteins as affected by pH. Meat Science 76, 216–225.Google Scholar
  24. de Jong, G. A. H., & Koppelman, S. J. (2002). Transglutaminase catalyzed reactions: Impact on food applications. Journal of Food Science 67, 2798–2806.Google Scholar
  25. de Jong, G. A. H., Wijngaards, G., Boumans, H., Koppelman, S. J., & Hessing, M. (2001). Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense. Journal of Agricultural and Food Chemistry 49, 3389–3393.Google Scholar
  26. Dill, C. W., & Landmann, W. A. (1988). Food grade proteins from edible blood. In A. M. Pearson & T. R. Dutson (Eds.), Advances in meat research: Vol. 5. Edible meat by-products (pp. 127–145). London: Elsevier Applied Science.Google Scholar
  27. Doerscher, D. R., Briggs, J. L., & Lonergan, S. M. (2003). Effects of pork collagen on thermal and viscoelastic properties of purified porcine myofibrillar protein gels. Meat Science 66 181–188.Google Scholar
  28. Eilert, S. J., Blackmer, D. S., Mandigo, R. W., & Calkins, C. R. (1993). Meat batters manufactured with modified beef connective tissue. Journal of Food Science 58, 691–696.Google Scholar
  29. Elias, E., Komanowsky, M., Sinnamon, H. I., & Aceto, N. C. (1970). Converts collagen to food additives. Food Engineering 42(11), 125.Google Scholar
  30. European Commission, Health and Consumer Protection Directorate-General. (2001, July 19). Stricter labelling requirements for sausages and preserved meat products [Press release]. Retrieved November 30, 2007, from http://ec.europa.eu/dgs/health_consumer/library/press/press168_en.html
  31. European Food Safety Authority. (2005). Opinion of the Scientific Panel on Food Additives, Flavourings, Processing Aids and Materials in Contact with Food on a request from the Commission related to use of an enzyme preparation based on thrombin:fibrinogen derived from cattle and/or pigs as a food additive for reconstituting food. Question number EFSA-2004-025. Adopted on 26 April 2005 [Electronic version]. EFSA Journal, 214, 1–8. Retrieved October 15, 2007, from http://www.efsa.europa.eu/EFSA/Scientific_Opinion/afc_op_ej214_fibrimex_en2,0.pdf
  32. European Parliament and Council. (2002). Regulation (EC) No 1774/2002 of the European Parliament and of the Council of 3 October 2002 laying down health rules concerning animal by-products not intended for human consumption. Retrieved November 30, 2007, from European Union Law Web Site: http://eur-lex.europa.eu/LexUriServ/LexUriServ.do?uri=OJ:L:2002:273:0001:0095:EN:PDF
  33. European Parliament and Council. (2004). Corrigendum to Regulation (EC) No 853/2004 of the European Parliament and of the Council of 29 April 2004 laying down specific hygiene rules for food of animal origin. Official Journal of the European Communities, L 226 (June 25, 2004), 22–82. Retrieved May 13, 2007, from http://europa.eu.int/eur-lex/lex/LexUriServ/site/en/oj2004/l_226/l_22620040625en00220082.pdf/2span> Google Scholar
  34. European Parliament and Council. (2006). Directive No. 95/2/EC of 20 February 1995 on food additives other than colours and sweeteners (consolidated version of August 15, 2006; pp. 1–57) [Electronic version]. Retrieved November 14, 2007, from European Union Law Web Site: http://eur-lex.europa.eu/LexUriServ/site/en/consleg/1995/L/01995L0002-20060815-en.pdf
  35. European Parliament and Council. (2007). Directive 2000/13/EC of 20 March 2000 on the approximation of the laws of the Member States relating to the labelling, presentation and advertising of foodstuffs (consolidated version of January 12, 2007, pp. 1–27) [Electronic version]. KRetrieved November 14, 2007, from European Union Law Web Site: http://eur-lex. europa.eu/LexUriServ/LexUriServ.do?uri=CONSLEG:2000L0013:20070112:EN:PDF
  36. European Union. (2007). Animal by-products not intended for human consumption [Fact sheet]. Retrieved November 30, 2007, from European Union Web Site: http://europa.eu/scadplus/leg/en/lvb/f81001.htm
  37. Eyre, D. R. (1987). Collagen stability through covalent crosslinking. In A. M. Pearson, T. R. Dutson, & A. J. Bailey (Eds.), Advances in meat research: Vol. 4. Collagen as a food (pp. 69–85). New York: Van Nostrand Reinhold.Google Scholar
  38. Flores, N. C., Boyle, E. A. E., & Kastner, C. L. (2007). Instrumental and consumer evaluation of pork restructured with activa TM or with fibrimex TM formulated with and without phosphate. Lebensmittel Wissenschaft und Technologie 40, 179–185.Google Scholar
  39. Foegeding, E. A., Allen, C. E., & Dayton, W. R. (1986). Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels. Journal of Food Science 51, 104–108, 112.Google Scholar
  40. Foegeding, E. A., Dayton, W. R., & Allen, C. E. (1986). Interaction of myosin—albumin and myosin—fibrinogen to form protein gels. Journal of Food Science 51, 109–112.Google Scholar
  41. Foegeding, E. A., Lanier, T. C., & Hultin, H. O. (1996). Characteristics of edible muscle tissues. In O. R. Fennema (Ed.), Food Chemistry (3rd ed., pp. 879–942). New York: Marcel Dekker.Google Scholar
  42. Folk, J. E. (1980). Transglutaminases. Annual Review of Biochemistry, 49, 517–531.Google Scholar
  43. Fonkwe, L. G., & Singh, R. K. (1996). Protein recovery from mechanically deboned turkey residue by enzymic hydrolysis. Process Biochemistry 31, 605–616.Google Scholar
  44. Gelatin Manufacturers Institute of America, Inc. (2006). 2. Physical/chemical testing. In GMIA standard methods for the testing of edible gelatin. Retrieved January 5, 2008, from http://www.gelatin-gmia.com/PDFs/2.1%20Gel%20Strength.pdf
  45. Gillett, T. A. (1987). Collagen in meat emulsions. In A. M. Pearson, T. R. Dutson, & A. J. Bailey (Eds.), Advances in meat research: Vol. 4. Collagen as a food (pp. 223–249). New York: Van Nostrand Reinhold.Google Scholar
  46. Gorbatov, V.M. (1988). Collection and utilization of blood and blood proteins for edible purposes in the USSR. In A. M. Pearson & T. R. Dutson (Eds.), Advances in meat research: Vol. 5. Edible meat by-products (pp. 167ȓ195). London: Elsevier Applied Science.Google Scholar
  47. Griffin, M., Casadio, R., & Bergamini, C. M. (2002). Transglutaminases: Nature's biological glues. Biochemical Journal, 368, 377–396.Google Scholar
  48. Halliday, D. A. (1973). Blood — A source of proteins. Process Biochemistry 8, 15–17.Google Scholar
  49. Hamada, J. S. (1992). Modification of food proteins by enzymatic methods. In B. J. F. Hudson (Ed.), Biochemistry of food proteins (pp. 249–270). London: Elsevier Applied Science.Google Scholar
  50. Harper, J. P., Suter, D. A., Dill, C. W., & Jones, E. R. (1978). Effects of heat treatment and protein concentration on the rheology of bovine plasma protein suspensions. Journal of Food Science 43, 1204–1209.Google Scholar
  51. Hermansson, A. M. (1978). The function of blood proteins and other proteins in meat products. Proceedings of the 24th European Meeting of Meat Research Workers (pp. H1:3—H1:11); Kulmbach, Germany.Google Scholar
  52. Hermansson, A.-M. (1982). Gel characteristics — Structure as related to texture and waterbinding of blood plasma gels. Journal of Food Science 47, 1965–1972.Google Scholar
  53. Hermansson, A.-M., & Lucisano, M. (1982). Gel characteristics — Waterbinding properties of blood plasma gels and methodological aspects on the waterbinding of gel systems. Journal of Food Science 47, 1955–1959.Google Scholar
  54. Howell, N. K. (1992). Protein—protein interactions. In B. J. F. Hudson (Ed.), Biochemistry of food proteins (pp. 35–74). London: Elsevier Applied Science.Google Scholar
  55. Howell, N. K., & Lawrie, R. A. (1984). Functional aspects of blood plasma proteins. 2. Gelling properties. Journal of Food Technology 19, 289–295.Google Scholar
  56. Jobling, A. (1994). Food proteins from red meat by-products. In B. J. F. Hudson (Ed.), New and developing sources of food proteins (pp. 31–50). London: Chapman & Hall.Google Scholar
  57. Judge, M. D., Aberle, E. D., Forrest, J. C., Hedrick, H. B., & Merkel, R. A. (1989). Principles of meat science (2nd ed.). Dubuque, IA: Kendall/Hunt.Google Scholar
  58. Kahn, D. R., & Cohen, I. (1981). Factor XIIIa-catalyzed coupling of structural proteins. Biochimica et Biophysica Acta (MBBA), 668, 490–494.Google Scholar
  59. Kauffman, R. G. (2001). Meat composition. In Y. H. Hui, W.-K. Nip, R. W. Rogers, & O. A. Young (Eds.), Meat science and applications (pp. 1–19). New York: Marcel Dekker.Google Scholar
  60. Kijowski, J. (2001). Muscle proteins. In Z.E. Sikorski (Ed.), Chemical & functional properties of food proteins (pp. 233–269). Lancaster, PA: Technomic.Google Scholar
  61. King, J., de Pablo, S., & Montes de Oca, F. (1989) Evaluation of gelation and solubility of bovine plasma protein isolates Journal of Food Science 54, 1381–1382.Google Scholar
  62. Knipe, C. L. (1988). Production and use of animal blood and blood proteins for human food. In A. M. Pearson & T. R. Dutson (Eds.), Advances in meat research: Vol. 5. Edible meat byproducts (pp. 147–165). London: Elsevier Applied Science.Google Scholar
  63. Krochta J. M., & De Mulder-Johnson, C. (1997). Edible and biodegradable polymer films: challenges and opportunities. Food Technology 51(2), 61–74.Google Scholar
  64. Kurth, L., & Rogers, P. J. (1984). Transglutaminase catalyzed cross-linking of myosin to soya protein, casein and gluten. Journal of Food Science 49, 573–576, 589.Google Scholar
  65. Lahl, W. J., & Braun, S. D. (1994). Enzymatic production of protein hydrolysates for food use. Food Technology 48(10), 68–71.Google Scholar
  66. Linden, G., & Lorient, D. (1999). In M. Rosengarten, Trans.; M. K. Lewis, Advisory (Eds.), New ingredients in food processing: Biochemistry and agriculture Cambridge, England: Woodhead Publishing. (Original work published 1994.)Google Scholar
  67. Liu, D.-C., & Ockerman, H. W. (2001). Meat co-products. In Y. H. Hui, W.-K. Nip, R. W. Rogers, & O. A. Young (Eds.), Meat science and applications (pp. 582–603). New York: Marcel Dekker.Google Scholar
  68. Lou, X., Wang, C., Xiong, Y. L., Wang, B., & Mims, S. D. (2000). Gelation characteristics of paddlefish (Polyodon spathula) surimi under different heating conditions. Journal of Food Science 65, 394–398.Google Scholar
  69. Mahmoud, M. I. (1994). Physicochemical and functional properties of protein hydrolysates in nutritional products. Food Technology 48(10), 89–95.Google Scholar
  70. McCormick, R. J., & Phillips, A. L. (1999). Muscle extracellular matrix: Role in growth, development, and meat tenderness. In Y. L. Xiong, C.-T. Ho, & F. Shahidi (Eds.), Quality attributes of muscle foods (pp. 219–227). New York: Kluwer Academic/Plenum Press.Google Scholar
  71. Motoki, M., & Seguro, K. (1998). Transglutaminase and its use in food processing. Trends in Food Science & Technology 9, 204–210.Google Scholar
  72. Muguruma, M., Tsuruoka, K., Katayama, K., Erwanto, Y., Kawahara, S., Yamauchi, K., Sathe, S. K., & Soeda, T. (2003). Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Science 63, 191–197.Google Scholar
  73. Muguruma, M., Tsuruoka, K., Fujino, H., Kawahara, S., Yamauchi, K., Matsumura, S., & Soeda, T. (1999). Gel strength enhancement of sausages by treating with microbial transglutaminase. In Proceedings of the International Congress of Meat Science and Technology (pp. 138–139), Yokohama, Japan.Google Scholar
  74. Nielsen, G. S., Petersen, B. R., & Møller, A. J. (1995). Impact of salt, phosphate and temperature on the effect of a transglutaminase (F XIIIa) on the texture of restructured meat. Meat Science 41, 293–299.Google Scholar
  75. Ockerman, H. W., & Hansen, C. L. (2000). Animal by-product processing and utilization Lancaster, PA: Technomic.Google Scholar
  76. Oord van den, A. H. A., & Wesdorp, J. J. (1979). Decolouration of slaughterhouse blood by treatment with hydrogen peroxide. Proceedings of the 25th European Meeting of Meat Research Workers (pp. 827–828), Budapest, Hungary.Google Scholar
  77. Osburn, W. N., Mandigo, R. W., & Eskridge, K. M. (1997). Pork skin connective tissue gel utilization in reduced-fat bologna. Journal of Food Science 62, 1176–1182.Google Scholar
  78. Paardekooper, E. J. C., & Wijngaards, G. (1986). Composite meat product and method for the manufacture thereof. European Patent No. 0 201 975 B1. Munich, Germany: European Patent Organisation.Google Scholar
  79. Pearson, A. M., & T. A. Gillett. (1999). Processed meats (3rd ed., pp. 355–371). Gaithersburg, MD: Aspen Publishers.Google Scholar
  80. Pedersen, B. (1994). Removing bitterness from protein hydrolysates. Food Technology 48(10), 96–98.Google Scholar
  81. Pegg, R. B., & Shahidi, F. (2000). Nitrite curing of meat: The N-nitrosamine problem and nitrite alternatives. Trumbull, CT: Food & Nutrition Press.Google Scholar
  82. Penteado, M. D. V. C., Lajolo, F. M., & Pereira Dos Santos, N. (1979). Functional and nutritional properties of isolated bovine blood proteins. Journal of the Science of Food and Agriculture 30, 809–815.Google Scholar
  83. Piette, G. (1999). Enzymes in meat technology. In R. Rastall (Ed.), LFRA ingredients handbook — Enzymes (pp. 13–39). Surrey, UK: Leatherhead Food RA.Google Scholar
  84. Pinto E Silva, M. E. M., Mazzilli, R. N., & Cusin, F. (1999). Composition of hydrolysates from meat. Journal of Food Composition and Analysis 12, 219–225.Google Scholar
  85. Piot, J. M., Guillochon, D., & Thomas, D. (1986). Preparation of decolorized peptides from slaughter-house blood. World Journal of Microbiology and Biotechnology 2359–364.Google Scholar
  86. Prabhu, G. (2002). Utilizing functional meat-based proteins in processed meat applications. In Proceedings of the 55th Reciprocal Meat Conference (pp. 29–34). Savoy, IL: American Meat Science Association.Google Scholar
  87. Prabhu, G. (2003). Poultry collagen: Ingredients that combine flavor and functionality. Meat & Poultry, 49(1), 68–70.Google Scholar
  88. Prabhu, G., & Doerscher, D. (2000). Collagen's new application. Meat & Poultry 46(4), 65–66, 68–9.Google Scholar
  89. Prabhu, G. A., Doerscher, D. R., & Hull, D. H. (2004). Utilization of pork collagen protein in emulsified and whole muscle meat products. Journal of Food Science 69, C388–C392.Google Scholar
  90. Prabhu, G., & Hull, D. (2001, June). Meat based protein ingredients. Paper presented at the Annual Meeting of the Institute of Food Technologists, New Orleans, LA.Google Scholar
  91. Proliant, Inc. (2008). Proliant meat ingredients. Meat Ingredients Division products — Specialty products. Retrieved January 3, 2008, from http://www.proliantinc.com/meatingredients/prod-ucts/Specialty.asp
  92. Purslow, P. P. (1999). The intramuscular connective tissue matrix and cell/matrix interactions in relation to meat toughness. In Proceedings of the International Congress of Meat Science and Technology (pp. 210–219), Yokohama, Japan.Google Scholar
  93. Ramos-Clamont, G., Fernández-Michel, S., Carrillo-Vargas, L., Martínez-Calderó;n, E., & Vázquez-Moreno, L. (2003). Functional properties of protein fractions isolated from porcine blood. Journal of Food Science 68, 1196–1200.Google Scholar
  94. Rosenthal, A. J. (1999). Relation between instrumental and sensory measures of food texture. In A. J. Rosenthal (Ed.), Food texture: Measurement and perception (pp. 1–17). Gaithersburg, MD: Aspen Publishers.Google Scholar
  95. Sadowska, M., Sikorski, Z. E., & Dobosz, M. (1980). Influence of collagen on the rheological properties of meat homogenates. Lebensmittel Wissenschaft und Technologie 13, 232–236.Google Scholar
  96. Sato, Y., Hayakawa, S., & Hayakawa, M. (1981). Preparation of blood globin through carboxyme-thyl cellulose chromatography. Journal of Food Technology 16, 81–91.Google Scholar
  97. Satterlee, L. D. (1975). Improving utilization of animal by-products for human foods — A review. Journal of Animal Science 41, 687–697.Google Scholar
  98. Satterlee, L. D., Zachariah, N. Y., & Levin, E. (1973). Utilization of beef and pork skin hydro-lyzates as a binder or extender in sausage emulsions. Journal of Food Science 38, 268–270.Google Scholar
  99. Schilling, M. W., Mink, L. E., Gochenour, P. S., Marriott, N. G., & Alvarado, C. Z. (2003). Utilization of pork collagen for functionality improvement of boneless cured ham manufactured from pale, soft, and exudative pork. Meat Science 65, 547–553.Google Scholar
  100. Shahidi, F., Naczk, M., Rubin, L. J., & Diosaday, L. L. (1984). Functional properties of blood globin. Journal of Food Science 49, 370–372.Google Scholar
  101. Sims, T. J., & Bailey, A. J. (1981). Connective tissue. In R. A. Lawrie (Ed.), Developments in meat science: Vol. 2 (pp. 29–59). London: Applied Science Publishers.Google Scholar
  102. Sonac B.V. (2007a). Fibrimex® frozen and Fibrimex® powder [Brochure]. Loenen, Netherlands: Author. Retrieved May 14, 2007, from http://www.sonac.biz
  103. Sonac B.V. (2007b). Harimix proteins: Color enhancement of meat [Brochure]. Loenen, Netherlands: Author. Retrieved January 3, 2008, from http://www.sonac.biz/upload/harimexpr_w.pdf
  104. Stachowicz, K. J., Eriksson, C. E., & Tjelle, S. (1977). Enzymic hydrolysis of ox-blood hemoglobin. In R. L. Ory & A. J. St. Angelo (Eds.), Enzymes in food and beverage processing (ACS Symposium Series 47, pp. 295–303). Washington, DC: American Chemical Society.Google Scholar
  105. Stainsby, G. (1987). Gelatin gels. In A. M. Pearson, T. R. Dutson, & A. J. Bailey (Eds.), Advances in meat research: Vol. 4. Collagen as a food (pp. 209–222). New York: Van Nostrand Reinhold.Google Scholar
  106. Stryer, L. (1988). Connective-tissue proteins. In Biochemistry (3rd ed., pp. 261–281). New York: W. H. Freeman.Google Scholar
  107. Suter, D. A., Sustek, E., Dill, C. W., Marshall, W. H., & Carpenter, Z. L. (1976). A method for measurement of the effect of blood protein concentrates on the binding forces in cooked ground beef patties. Journal of Food Science 41, 1428–1432.Google Scholar
  108. Synowiecki, J., Jagielka, R, & Shahidi, F. (1996). Preparation of hydrolysates from bovine red blood cells and their debittering following plastein reaction. Food Chemistry 57, 435–439.Google Scholar
  109. Terrell, R. N., Crenwelge, C. H., Dutson, T. R., & Smith, G. C. (1982). A technique to measure binding properties of non-meat proteins in muscle-juncture formation. Journal of Food Science 47, 711–713.Google Scholar
  110. Terrell, R. N., Weinblatt, P. J., Smith, G. C., Carpenter, Z. L., Dill, C. W., & Morgan, R.G. (1979). Plasma protein isolate effects on physical characteristics of all-meat and extended frankfurters. Journal of Food Science 44, 1041–1043, 1048.Google Scholar
  111. Tornberg, E., & Jönsson, T. (1981). The interfacial and emulsifying properties of blood plasma proteins. In Proceedings of the 27th European Meetings of Meat Research Workers (Vol. 2; pp. 369–373), Vienna, Austria.Google Scholar
  112. Tseng, T.-F., Liu, D.-C., & Chen, M.-T. (2000). Evaluation of transglutaminase on the quality of low-salt chicken meat-balls. Meat Science 55, 427–431.Google Scholar
  113. Tybor, P. T., Dill, C. W., & Landmann, W. A. (1973). Effect of decolorization and lactose incorporation on the emulsification capacity of spray-dried blood protein concentrate. Journal of Food Science 38, 4–6.Google Scholar
  114. Tybor, P. T., Dill, C. W., & Landmann, W. A. (1975). Functional properties of proteins isolated from bovine blood by a continuous pilot plant process. Journal of Food Science 40 155–159.Google Scholar
  115. United States Department of Agriculture, Food Safety and Inspection Service. (n.d.). Questions and answers relating to ingredients that may be designated as flavors, flavorings, natural flavors or natural flavorings in the ingredients statements on the labels of meat and poultry products (FSIS Directive 7140.1). Retrieved November 30, 2007, from http://www.fsis.usda.gov/OPPDE/rdad/FSISDirectives/7140-1.pdf
  116. United States Department of Agriculture, Food Safety and Inspection Service. (1995a). Labeling and Consumer Protection. Questions and answers relating to use and labeling of ingredients, including flavorings, proprietary ingredient mixes, ingredients in standardized and non-standardized foods, and protein hydrolysates. Retrieved January 13, 2008, from http://www.fsis.usda.gov/OPPDE/larc/Ingredients/PMC_QA.htm
  117. United States Department of Agriculture, Food Safety and Inspection Service. (1995b). Processing inspectors' calculations handbook (FSIS Directive 7620.3). Retrieved June 3, 2007, from http://www.fsis.usda.gov/OPPDE/rdad/FSISDirectives/7620-3.pdf
  118. United States Department of Agriculture, Food Safety and Inspection Service. (2004, January 1). Prohibition of the use of specified risk materials for human food and requirements for the disposition of non-ambulatory disabled cattle. 69 Fed. Reg. 1861–1874 (to be codified at 9 C.F.R. pts. 309, 310, 311, 318, & 319).Google Scholar
  119. United States Department of Agriculture, Food Safety and Inspection Service. (2005). Food standards and labeling policy book. Retrieved October 20, 2007, from http://www.fsis.usda.gov/OPPDE/larc/Policies/Labeling_Policy_Book_082005.pdf
  120. United States Department of Agriculture, Food Safety and Inspection Service. (2006a, June). Food safety information: Natural flavorings on meat and poultry labels [Fact sheet]. Retrieved November 30, 2007, from www.fsis.usda.gov/PDF/Natural_Flavorings_on_Meat_and_Poultry_Labels.pdf
  121. United States Department of Agriculture, Food Safety and Inspection Service (2006b, August). Food Safety Information: Meat and poultry labeling terms [Fact sheet]. Retrieved May 10, 2007, from http://www.fsis.usda.gov/PDF/Meat_and_Poultry_Labeling_Terms.pdf
  122. United States Department of Agriculture, Food Safety and Inspection Service. (2007). Safe and suitable ingredients used in the production of meat and poultry products (FSIS Directive 7120.1, Amendment 13). Retrieved November 12, 2007, from: http://www.fsis.usda.gov/OPPDE/rdad/FSISDirectives/7120.1Amend13.pdf
  123. Villegas R, O'Connor T. P., Kerry J. P., & Buckley D. J. (1999). Effect of gelatin dip on the oxida-tive and colour stability of cooked ham and bacon pieces during frozen storage. International Journal of Food Science and Technology 34, 385–389.Google Scholar
  124. Voutila, L., Mullen, A. M., Ruusunen, M., Troy, D., & Puolanne, E. (2007). Thermal stability of connective tissue from porcine muscles. Meat Science 76, 474–480.Google Scholar
  125. Wanasundara, P. K. J. P. D., Amarowicz, R., Pegg, R. B. & Shand, P. J. (2002) Preparation and characterization of hydrolyzed proteins from defibrinated bovine plasma. Journal of Food Science 67, 623–630.Google Scholar
  126. Wang, B., Wang, C., Mims, S. D., & Xiong, Y. L. (2000). Characterization of the proteases involved in hydrolyzing paddlefish (Polyodon spathula) myosin. Journal of Food Biochemistry 24, 503–515.Google Scholar
  127. Webster, J. D., Ledward, D. A., & Lawrie, R.A. (1982). Protein hydrolysates from meat industry by-products. Meat Science.7, 147–167.Google Scholar
  128. Wismer-Pedersen, J. (1979). Utilization of animal blood in meat products. Food Technology 33 76–80.Google Scholar
  129. Whiting, R. C. (1989). Contribution of collagen to the properties of comminuted and restructured meat products. In Proceedings of the 42nd Reciprocal Meat Conference (pp. 149–156). Savoy, IL: American Meat Science Association.Google Scholar
  130. Xiong, Y. L. (2004). Muscle proteins. In R. Y. Yada (Ed.), Proteins in food processing. Cambridge, England: Woodhead Publishing.Google Scholar
  131. Zhu, Y., Rinzema, A., Tramper, J., & Bol, J. (1995). Microbial transglutaminase — a review of its production and application in food processing. Applied Microbiology and Biotechnology 44 277–282.Google Scholar

Copyright information

© Springer Science + Business Media, LLC 2009

Authors and Affiliations

  • Rodrigo Tarté
    • 1
  1. 1.Meat Science ResearchResearch, Development & Quality Kraft Foods Inc.MadisonUSA

Personalised recommendations