Functional Food Protein Ingredients from Fish

  • Tyre C. Lanier


It is increasingly common to encounter commercially processed foods whose constituent carbohydrates, lipids, and proteins are derived from several differing natural sources. Often these food-ingredient materials have been refined as semipure fractions before being used as food ingredients. They may even represent the product of complex chemical and/or physical alterations to a naturally derived material, which, like cellulose for example, may not normally be a source of human food. Such refined and/or altered substances constitute the bulk of the present-day food-ingredient market, a vast assortment valued solely for, and specified by, their individual “functional properties.” This term is applicable only to materials destined to be food ingredients, referring to their individual ability to contribute to the taste, texture, and appearance of a formulated food.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Anonymous. 1988. “A Trial to Establish Technical and Commercial Viability of Cod Frame Mince Recovery. Canadian Industry Report of Fisheries and Aquatic Science, No. 197.Google Scholar
  2. Anonymous. 1990. “Surimi Based Foods Using Alaco Surimi Plus (Whey Protein Concentrate).” Technical application A604, Milk Products (N.Z.) Limited, UK.Google Scholar
  3. Anonymous , 1991a. Albuvir (whey protein isolate). Technical brochure, Union Laitiere Normande, France.Google Scholar
  4. Anonymous. 199lb. Fish Gelatin. Technical brochure. Croda Colloids Ltd., England.Google Scholar
  5. Arai , S., and Fujimaxi, M. 1978. “The Plastein Reaction. Theoretical Basis.” Ann. Nutr. Aliment. 32:701–707.Google Scholar
  6. Ayers , J. S., and Peterson, M. J. 1985. “Whey Protein Recovery Using a Range of Novel Ion-Exchangers.” New Zealand J. Dairy Sci. Technol. 20:129–142.Google Scholar
  7. Baldwin , R. E., and Sinthavalai, S. 1974. “Fish Protein Concentrate Foam.” J. Food Sci. 39:880–882.CrossRefGoogle Scholar
  8. Boye , S. W., and Lanier, T. C. 1988. “Effects of Heat-Stable Alkaline Protease Activity of Atlantic Menhaden on Surimi Gels.” J. Food Sci. 53:1340–1342, 1398.CrossRefGoogle Scholar
  9. Brekke , C. J., and Eisele, T. A. 1981. “The Role of Modified Proteins in the Processing of Muscle Foods.” Food Technol. 35(5):231–234.Google Scholar
  10. Brooks , Gladden M. 1989. Personal communication, Mississippi State University.Google Scholar
  11. Cheftel , J. C., Cuq, J-L., and Lorient, D. 1985. “Amino Acids, Peptides, and Proteins.” P. 339. In Food Chemistry, edited by O. W. Fennema, New York: Marcel Dekker.Google Scholar
  12. Chen , S. X., and Swaisgood, H. E. 1991. “Characteristics of a Structural Domain Prepared from ß-Lactoglobulin by Limited Proteolysis with Immobilized Trypsin. J. Dairy Sci. 74 (Suppl.1):102.Google Scholar
  13. Cooper , G. M. 1992. Personal communication. Morton Salt Co., Woodstock, IL.Google Scholar
  14. Creamer , L. K., Jimenez-Flores, R., and Richardson, T. 1988. “Genetic Modification of Food Proteins.” TIBTECH 6:163–169.CrossRefGoogle Scholar
  15. Crowe , J. H., Carpenter, J. F., Crowe, L. M., and Anchordoguy, T. J. 1990. “Are Freezing and Dehydration Similar Stress Vectors? A Comparison of Modes of Interaction of Stabilizing Solutes with Biomolecules.” Cryobiology 27:219.CrossRefGoogle Scholar
  16. Daum-Thunberg, D. L., Foegeding, E. A., and Ball, H. R., JR. 1992. “Rheological and Water-Holding Properties of Comminuted Turkey Breast and Thigh: Effects of Initial pH.” J. Food Sci. 57:333–338.CrossRefGoogle Scholar
  17. Fletcher , G. L., Shears, M. A., King, M. J., Davies, P. L., and Chew, C. L. 1988. “Evidence for Antifreeze Protein Gene Transfer in Atlantic Salmon (Salmo salar).” Can. J. Fish Aquat. Sci. 45:352.CrossRefGoogle Scholar
  18. French , J. S., and Pedersen, L. D. 1990. “Properties and Stability of Surimi Combined with Process-Water Protein Concentrates.” Pp. 95–102. In Chilling and Freezing of New Fish Products, Intl. Inst. Refrig., Paris.Google Scholar
  19. Goldhor , S. H., and Regenstein, J. M. 1988. “U.S. Fishery Byproducts: A Selective Update and Review. Pp. 213–221. In Proc. 12th Ann. Trop. Subtrop. Fish. Technol. Soc. Amer., Orlando, FL: Florida Sea Grant Prog. SGR92, Gainesville, FL.Google Scholar
  20. Gorga , C., and Rosivalli, L. J. 1988. Quality Assurance of Seafood. New York: Van Nostrand Reinhold.Google Scholar
  21. Greenberg , C. S., Birchbichler, P. J., and Rice, R. H. 1991. “Transglutaminases: Multifunctional Cross-Linking Enzymes That Stabilize Tissues.” FASEB J. 5:3071–3077.Google Scholar
  22. Gwinn , S. E. 1992. “Development of Surimi Technology in the United States.” Pp. 23–40. In Surimi Technology. edited by T. C. Lanier and C. M. Lee. New York: Marcel Dekker.Google Scholar
  23. Haard , N. F. 1992. “A Review of Proteolytic Enzymes from Marine Organisms and Their Application in the Food Industry.” J. Aquatic Food Prod. Technol. 1:17–35.CrossRefGoogle Scholar
  24. Hallerman , E. M., Kapuscinski, A. R., Hachett, P. B., Farras, A. J., and Guise, K. S. 1990. “Gene Transfer in Fish.” In Pp. 35–49.Advances in Fisheries Technology and Biotechnology for Increased Profitability, Lancaster, PA: Technomic Publishing Co.Google Scholar
  25. Hamann , D. D. 1987. “Instrumental Texture Measurements for Processed Meat Products.” Proc. Ann. Recipr. Meat Conf. Nat. Live Stock Meat Bd. 40:19–23.Google Scholar
  26. Hamann , D. D., Amato, P. M., Wu, M. C., and Foegeding, E. A. 1990. “Inhibition of Modori (Gel Weakening) in Surimi by Plasma Hydrolysate and Egg White.” J. Food Sci. 55:665–669, 794.Google Scholar
  27. Hasegawa , H., Watanabe, H., and Takai, R. 1982. “Methods of Recovery of Fish Muscle Water-Soluble Protein by Electrocoagulation.” Nippon Suisan Gakkaishi. 48:65–68.CrossRefGoogle Scholar
  28. Hashimoto , A., and Arai, K. 1984. “Temperature Dependence of Mg-ATPase Activity and its Ca-Sensitivity of Fish Myofibrils.” Nippon Suisan Gakkaishi. 50:853–863.CrossRefGoogle Scholar
  29. Hashimoto , A., Kobayashi, A., and Arai, K. 1982. Thermostability of fish myofibrillar Ca-ATPase and adaption to environmental temperature. Nippon Suisan Gakkaishi 48(5):671–684.CrossRefGoogle Scholar
  30. Hastings , R. J. 1989. Comparison of the Properties of Gels Derived from Cod Surimi and from Unwashed and Once-Washed Cod Mince.“ Internat. J. Food Sci. Technol. 24:93–102.CrossRefGoogle Scholar
  31. Hayashi , R. 1989. “Application of High Pressure to Food Processing and Preservation: Philosophy and Development. Pp. 815–826.In Engineering and Food, edited by W. E. L. Spiess and H. Schubert. Vol. 2. London: Elsevier Applied Science.Google Scholar
  32. Holden , C. 1971. “Fish Flour: Protein Concentrate Has Yet to Fulfill Expectations.” Science 173:410.CrossRefGoogle Scholar
  33. Holmes , K. (ed). 1987. “Surimi: It’s American Now.” Anchorage, AK: Alaska Fisheries Development Foundation.Google Scholar
  34. Holmquist , J. F. 1982. “Interrelations Between Salt-Extractable Protein, Actomyosin, Calcium ATPase Activity,and Kamaboko Quality Prepared from Frozen Red Hake Fillets, Mince,and Surimi. M. S. thesis, University of Massachusetts.Google Scholar
  35. Horisberger , M. 1979. “Lessons from the Past for Better Future Utilization of Fish Resources.” Pp. 41–49. Nestle Research News. Lausanne, Nestle Products Technical Assist. Co. Ltd.Google Scholar
  36. Hultin , H. O.1985. “Characteristics of Muscle Tissue.” P. 753. In Food Chemistry,edited by O. R. Fennema, New York: Marcel Dekker.Google Scholar
  37. Hultin , H. O. 1987. “Factors Responsible for Lipid Oxidation in Fish Muscle.” Pp. 185–224. In Proc. Conf. Fatty Fish Utilization: Upgrading from Feed to Food. University of North Carolina, Raleigh, NC, SeaGrant Publ. 88–04.Google Scholar
  38. Hwang , G.-C., Ochiai, Y., Watabe, S., and Hashimoto, K. 1991. “Changes of Carp Myosin Subfragment-1 Induced by Temperature Acclimation.” J. Corn. Physiol. B. 161:141–146.Google Scholar
  39. In , T. 1990. “Seafood Flavourants Produced by Enzymatic Hydrolysis.” Pp. 425–436. In Advances in Fisheries Technology and Biotechnology for Increased Profitability. Lancaster, PA: Technomic Publishing.Google Scholar
  40. Jang , H. D., and Swaisgood, H. E. 1990. “Analysis of Ligand Binding and ßLactoglobulin Denaturation by Chromatography on Immobilized Trans-Retinal.” J. Dairy Sci. 73:2067–2074.CrossRefGoogle Scholar
  41. Jiang , S.-T., Lan, C. C., and Tsao, C.-Y. 1986. “New Approach to Improve the Quality of Minced Fish Products from Freeze-Thawed Cod and Mackerel.” J. Food Sci. 51:310–312, 351.Google Scholar
  42. Johnston , I. A., and Goldspink, G. 1975. “Thermodynamic Activation Parameters of fish Myofibrillar ATPase Enzyme and Evolutionary Adaptations to Temperature.” Nature 257:620.CrossRefGoogle Scholar
  43. Johnston , I. A., Fleming, J. D., and Crockford, T. 1990. “Thermal Acclimation and Muscle Contractile Properties in Cyprinid Fish.” Amer. J. Physiol: Regulatory,Integr. Comp. Physiol. 28: R231–R236.Google Scholar
  44. Kamath , G. G., Lanier, T. C., Foegeding, E. A., and Hamann, D. D. 1992. “Non-disulfide Covalent Cross-Linking of Myosin Heavy Chain in `Setting’ of Alaska Pollock and Atlantic Croaker Surimi.” J. Food Biochem. 16:151–172.CrossRefGoogle Scholar
  45. Keay , J. N. (ed.). 1976. Proceedings of the Conference on the Production and Utilization of Mechanically Recovered Fish Flesh. 108 Pages. Aberdeen, Scotland: Ministry of Agriculture, Fisheries and Food.Google Scholar
  46. Kelleher , S. D., Silva, L. A., Hultin, H. O., and Wilhelm, K. A. 1992. “Inhibition of Lipid Oxidation During Processing of Washed Minced Atlantic Mackerel.” J. Food Sci. 57:1103–1108, 1119.CrossRefGoogle Scholar
  47. Kimura , I., Sugimoto, M., Toyoda, K., Seki, N., Arai, K., and Fujita, T. 1991. “A Study on the Cross-Linking Reaction of Myosin in Kamaboko `suwari’ Gels.” Nippon Suisan Gakkaishi. 57:1389–1396.CrossRefGoogle Scholar
  48. Kinoshita , M., Toyohara, H., and Shimizu, Y. 1990. “Proteolytic Degradation of Fish Gel (Modori Phenomenon) During Heating Process.” In Chilling and Freezing of New Fish Products. Paris: Intl. Inst. Refrig.Google Scholar
  49. Kishi , H., Nozawa, H., and Seki, N. 1991. “Reactivity of Muscle Transglutaminase on Carp Myofibrils and Myosin B.” Nippon Suisan Gakkaishi. 57:1203–1210.CrossRefGoogle Scholar
  50. Knight , M. K. 1990. “New Meat Ingredients.” Pp. 129–134. In Food Ingredients Exhibition Britain—Seminar Proceedings. London: Eppoconsult Publishers.Google Scholar
  51. Kolbe , E. R., Hsu, C. K., Lanier, T. C., Macdonald, G. A., Morrissey, M. T., and Simpson, R. 1992. “Product Alternatives for Pacific Whiting.” Proceedings of a Pacific Whiting Workshop on Harvesting, Processing,Marketing and Quality Assurance Programs. Astoria: Oregon State University.Google Scholar
  52. Korhonen , R. W., and Lanier, T. C. 1991. “Recovery of Surimi Leachwater Proteins.” Proc. Third Seafood Technol. and Regulatory Developments Conference: Seafood Waste Issues in the 1990’s. Washington, D.C.: New Orleans National Fisheries Institute.Google Scholar
  53. Korhonen , R. W., and Lanier, T. C. 1992. Unpublished data. North Carolina State University, Raleigh, NC.Google Scholar
  54. Kurth , L., and Rogers, P. J. 1984. “Transglutaminase Catalyzed Cross-Linking of Myosin to Soya Protein, Casein and Gluten.” J. Food Sci. 49:573.CrossRefGoogle Scholar
  55. Lanier , T. C. 1985a. “Menhaden: Soybean of the Sea. University of North Carolina, Raleigh, NC, Publ. No. UNC-SG-85–02.Google Scholar
  56. Lanier , T. C. 1985b. “Fish Protein in Processed Meats.” Proc. Ann. Recipr. Meat Conf.,Nat. Live Stock Meat Bd. 38:129–134.Google Scholar
  57. Lanier , T. C. 1986. “Functional Properties of Surimi.” Food Technol. 40(3):107–114, 124.Google Scholar
  58. Lanier , T. C. 1991. “Interactions of Muscle and Nonmuscle Proteins Affecting Heat-Set Gel Rheology.” In Pp. 268–284. Interactions of Food Proteins,edited by N. Parris and R. Barford Washington, DC: American Chemical Society. Symposium Series 454.CrossRefGoogle Scholar
  59. Lanier , T. C. 1992a. “Measurement of Surimi Composition and Functional Properties. Pp. 123–163. In Surimi Technology. edited by T. Lanier and C. Lee. New York: Marcel Dekker.Google Scholar
  60. Lanier , T. C. 1992b. Unpublished data. North Carolina State University, Raleigh.Google Scholar
  61. Lanier , T. C., Hart, K., and Martin, R. E. 1991. In A Manual of Standard Methods for Measuring and Specifying the Properties of Surimi. UNC Sea Grant Publication SG-91–01. Washington, DC: National Fisheries Institute.Google Scholar
  62. Lanier , T. C., Manning, P. K., Zetterling, T., and Macdonald, G. A. 1992. “Process Innovations in Surimi Manufacture.” Pp. 167–180. In Surimi Technology,edited by T. C. Lanier and C. M. Lee. New York: Marcel Dekker.Google Scholar
  63. Lee , H. G. 1991. Mechanism of Gel-Strengthening Effect of Sodium Ascorbate in Surimi Gel. M. S. thesis, University of Rhode Island, Kingston, RI.Google Scholar
  64. Lin , T. S., and Lanier, T. C. 1980. “Properties of an Alkaline Protease from the Skeletal Muscle of Atlantic Croaker.” J. Food Biochem. 4:17–28.CrossRefGoogle Scholar
  65. Macdonald , G. A., and Lanier, T. C. 1991. “Carbohydrates as Cryoprotectants for Meats and Surimi.” Food Technol. 45(3):150–159.Google Scholar
  66. Macdonald , G. A., Lelievre, J., and Wilson, N. D. C. 1990a. “Strength of Gels Prepared from Washed and Unwashed Minces of Hoki (Macruronus novaezelandiae) Stored in Ice.” J. Food Sci. 55:976–978, 982.CrossRefGoogle Scholar
  67. Macdonald , G. A., Wilson, N. D. C., and Lanier, T. C. 1990b. “Stabilised Mince: An Alternative to the Traditional Surimi Process.” Pp. 69–76. In Chilling and Freezing of New Fish Products, Intl. Inst. Refrig., Paris.Google Scholar
  68. Macfarlane , J. J., and Mckenzie, I. J. 1976. “Pressure-Induced Solubilization of Myofibrillar Proteins.” J. Food Sci. 41:1442–1446.CrossRefGoogle Scholar
  69. Mackie , I. M. 1983. “New Approaches in the Use of Fish Proteins.” Pp. 215–262. In Developments in Food Proteins-,edited by B.J.F. Hudson. New York: Applied Science Publishers.Google Scholar
  70. Martin , R. E. (ed.). 1972. In Proceedings of the First Technical Seminar on Mechanical Recovery and Utilization of Fish Flesh. Washington, DC: National Fisheries Institute and U. S. Department of Commerce, National Marine Fisheries Service.Google Scholar
  71. Martin , R. E. (ed.). 1974. In Proceedings of the Second Technical Seminar on Mechanical Recovery and Utilization of Fish Flesh. Washington, DC: National Fisheries Institute and U. S. Department of Commerce, National Marine Fisheries Service.Google Scholar
  72. Martin , R. E. (ed.). 1980. In Proceedings of the Third National Technical Seminar on Mechanical Recovery and Utilization of Fish Flesh. Washington, D.C.: National Fisheries Institute and U. S. Department of Commerce, National Marine Fisheries Service.Google Scholar
  73. Macron , J. 1979. “The Analytical, Nutritional and Toxicological Implications of Protein Food Processing.” Pp. 51–58. Nestle Research News,Lausanne: Nestle Products Technical Assist. Co. Ltd.Google Scholar
  74. Montejano , J. G., Hamann, D. C., and T. C. Lanier, 1984. “Thermally Induced Gelation of Selected Comminuted Muscle Systems—Rheological Changes During Processing, Final Strengths and Microstructure.” J. Food Sci. 49:1496–1505.CrossRefGoogle Scholar
  75. Niki , H., Matsuda, Y., and Suzuki, T. 1992. “Dried Forms of Surimi.” Pp. 209–243. In Surimi Technology, edited by T. Lanier and C. Lee. New York: Marcel Dekker.Google Scholar
  76. Nishimoto , S. I., Hashimoto, A., Seki, N., Kimura, I., Toyoda, K., and Fujita, T. 1987. “Influencing Factors on Changes in Myosin Heavy Chain and Jelly Strength of Salted Meat Paste from Alaska Pollock During Setting.” Nippon Suisan Gakkaishi. 53:2011–2020.CrossRefGoogle Scholar
  77. Nishimura , K., Ohtsuru, M., and Nigota, K. 1990. “Mechanism of Improvement Effect of Ascorbic Acid on the Thermal Gelation of Fish Meat.” Nippon Suisan Gakkaishi. 56:959.CrossRefGoogle Scholar
  78. Nishioka , F., and Shimizu, Y. 1983. “Recovery of Proteins from Washings of Minced Fish by pH Shifting Method.” Nippon Suisan Gakkaishi. 49:795–800.CrossRefGoogle Scholar
  79. Nishionka , F., Tokunaga, T., Fujiwara, T., and Yoshioka, S. 1990. “Development of New Leaching Technology and a System to Manufacture High Quality Frozen Surimi.” Pp. 123–32. In Chilling and Freezing of New Fish Products, Intl. Inst. Refrig., Paris.Google Scholar
  80. Niwa , E. 1992. “Chemistry of Surimi Gelation.” Pp. 389–428. In Surimi Technology, edited by T. Lanier and C. Lee. New York: Marcel Dekker.Google Scholar
  81. Norland , R. E. 1990. “Fish Gelatin.” Pp. 325–333. In Advances in Fisheries Technology and Biotechnology for Increased Profitability. Edited by M. N. Voigt and J. R. Botta. Lancaster, PA: Technomic Publishing Co.Google Scholar
  82. Okada , M. 1961. “The Effect of Oxidants on Jelly Strength of `Kamaboko.’ ” Nippon Suisan Gakkaishi. 27:203–208.CrossRefGoogle Scholar
  83. Okada , M. 1964. “Effect of Washing on the Jelly Forming Ability of Fish Meat.” Nippon Suisan Gakkaishi. 30:255–261.CrossRefGoogle Scholar
  84. Okazaki , E., Kanna, K., and Suzuki, T. 1986. “Effect of Sarcoplasmic Protein on Rheological Properties of Fish Meat Gel Formed by Retort Heating.” Nippon Suisan Gakkaishi. 52:1821–1827.CrossRefGoogle Scholar
  85. Okland , O. 1986. “High Quality Raw Material: A Condition for Success.” Fiskets Gang (Norway). 9(17):267–268.Google Scholar
  86. Okurowski , V. 1987. Effects of Phosphate Addition on the Heat Gelation Properties of Surimi. M. S. thesis, North Carolina State University, Raleigh, NC.Google Scholar
  87. Pariser , E. R., Wallerstein, M. B., Corkery, C. J., and Brown, N. L. 1978. In Fish Protein Concentrate: Panacea for Protein Malnutrition?“ Cambridge, MA: MIT Press.Google Scholar
  88. Park , J. W., Lanier, T. C., and Green, D. P. 1988. “Cryoprotective Effects of Sugar, Polyols, and/or Phosphates on Alaska Pollock Surimi.” J. Food Sci. 53:1–3.CrossRefGoogle Scholar
  89. Pomeranz , Y. 1992. “Modified Muscle Proteins.” Pp. 217–221. In Functional Properties of Food Components, San Francisco, CA: Academic Press.Google Scholar
  90. Saeki , H., Wakameda, A., Ichihara, Y., and Sasamoto, Y. 1989. “Effect of CaC12 on the Elution of Cross-Linking Factor in Alaska Pollock.” Nippon Suisan Gakkaishi. 55:1867.Google Scholar
  91. Sano , T., Noguchi, S. F., Tsuchiya, T., and Matsumoto, J. J. 1986. “Contribution of Paramyosin to Marine Meat Gel Characteristics.” J. Food Sci. 51:946.CrossRefGoogle Scholar
  92. Sano , T., Noguchi, S. F., Tsuchiya, T., and Matsumoto, J. J. 1989. “Paramyosin-Myosin-Actin Ineractions in Gel Formation of Invertebrate Muscle. J. Food Sci. 54:796–799, 842.CrossRefGoogle Scholar
  93. Seal , R. 1977. “Soya Products: A Food Processor’s Guide.” Chem. Ind. (London) 11:441–446.Google Scholar
  94. Shenouda , S. Y. 1980. “Theories of Protein Denaturation During Frozen Storage of Fish Flesh.” Edited by C. O. Chichester, E. M. Mrak and G. F. Stewart. Adv. Food Res. 26:275–311. New York: Academic Press.Google Scholar
  95. Shimizu , Y., and Nisxroka, F. 1974. “Species Variations in Heat Coagulation Properties of Fish Actomyosin-Sarcoplasmic Protein Systems.” Nippon Sui-san Gakkaishi. 40:267–270.CrossRefGoogle Scholar
  96. Shimizu , Y., Toyohara, H., and Lanier, T. C. 1992. “Surimi Production from Fatty and Dark-Fleshed Fish Species. Pp. 181–208. In Surimi Technology, edited by T. Lanier and C. Lee. New York: Marcel Dekker.Google Scholar
  97. Shoji , Y. 1990. “Creamy Fish Protein. Pp. 87–93. In Proc. Internat. Gonf. on Fish By-Products,Anchorage, AK: Alaska Sea Grant College Prog. Report No. 90–07.Google Scholar
  98. Shoji , T., Saeki, H., Wakameda, A., Nakamura, M. and Nonaka, M. 1990. Gelation of salted paste of Alaska pollock by high hydrostatic pressure and change in myofibrillar protein in it. Nippon Suisan Gakkaishi 56: 2069–2076.CrossRefGoogle Scholar
  99. Spinelli , J., Koury, B., Groninger, H., and Miller, R. 1977. “Expanded Uses for Fish Protein from Underutilized Species.” Food Technol. 31(5): 184–187.Google Scholar
  100. Stauffer , C. E. 1991. “Oxidants.” Pp. 1–40. In Functional Additives for Bakery Foods. New York: Van Nostrand Reinhold.Google Scholar
  101. Stefansson , G., and Steingrimsdottir, U. 1990.“ Application of Enzymes for Fish Processing in Iceland.” Pp. 237–250. In Advances in Fisheries Technology and Biotechnology for Increased Profitability. Edited by M. N. Voigt and J. R. Botta. Lancaster, PA: Technomic Publishing Co.Google Scholar
  102. Suzuki , T. 1981. “Frozen Minced Meat (Surimi). P. 121. In Fish and Krill Protein: Processing Technology. London: Applied Science Publisher.CrossRefGoogle Scholar
  103. Suzuki , T., and Magfarlane, J. J. 1984. “Modification of the Heat-Setting Char- acteristics of Myosin by Pressure Treatment.” Meat Sci. 11:263–274.CrossRefGoogle Scholar
  104. Swafford , T. C., Babbitt, J., Reppond, K., Hardy, A., Riley, C. C., and Zetter ling, T. K. A. 1985. “Surimi Process Yield Improvements and Quality Contribution by Centrifuging.” Proceedings of the International Symposium on Engineered Seafood Including Surimi, edited by R. E. Martin. Washington, DC: National Fisheries Institute.Google Scholar
  105. Taguchi , T., Ishizaki, S., Tanaka, M., Nagashima, Y., and Amano, K. 1989. “Effect of Ultraviolet Irradiation on Thermal Gelation of Muscle Pastes.” J. Food Sci. 54: 1438–1440, 1465.CrossRefGoogle Scholar
  106. Tanaka , M., Suzuki, K., and Taguchi, T. 1983. “Recovery of Proteins as a Spun Product from Sardine Viscera and Heads.” Nippon Suisan Gakkaishi. 49:1701–1705.CrossRefGoogle Scholar
  107. Tannenbaum , S. R., Ahern, M., and Bates, R. P. 1970a. “Solubilization of Fish Protein Concentrate. 1. An Alkaline Process.” Food Technol. 24:604–607.Google Scholar
  108. Tannenbaum , S. R., Bates, R. P., and Brodfeld, L. 1970b. “Solubilization of Fish Protein Concentrate. 2. Utilization of the Alklaine-Process Product.” Food Technol. 24:607–609.Google Scholar
  109. Torley , P. J., and Lanier, T. C. 1992. “Setting Ability of Salted Beef-Pollock Surimi Mixtures.” Pp. 305–316. In Seafood Science and Technology,edited by E. G. Bligh. Oxford: Fishing News Books.Google Scholar
  110. Tsai , S-J., Yamashita, M., Arai, S., and Fujimaki, M. 1972. “Effect of Substrate Concentration on Plastein Productivity and Some Rheological Properties of the Products.” Agric. Biol. Chem. 36:1045–1049.CrossRefGoogle Scholar
  111. Tsen , C. C., and Busnux, W. 1963. “Changes in Sulfhydryl and Disulfide Contents of Doughs During Mixing Under Various Conditions.” Cereal Chem. 40:339.Google Scholar
  112. Utsumi , S., and Kito, M. 1991. “Improvement of Food Protein Functions by Chemical, Physical, and Biological Modifications.” Comments Agric. Food Chem. 2:261–278.Google Scholar
  113. Wu , M. C., Lanier, T. C., and Hamann, D. D. 1985. “Thermal Transitions of Admixed Starch/Fish Protein Systems During Heating.”J. Food Sci. 50:20–25.CrossRefGoogle Scholar
  114. Wu , Y.J., Atallah, M. T., and Hultin, H. O. 199la. “The Proteins of Washed, Minced Fish Muscle Have Significant Solubility in Water.” J. Food Biochem. 15:209–218.CrossRefGoogle Scholar
  115. Wu , Y.J., Atallah, MT., Hultin, H. O., and Bakir, H. 1991b. “Relation of Water Solubility of Fish Muscle Proteins to Gel Formation in the Absence of Salt.” Pp. 275–284. In Proc. Tropical Subtropical Fish. Technol. Conf., Raleigh, NC: Florida Sea Grant Prog. SGR-110, Gainesville, FL.Google Scholar
  116. Yoshinaka , R., Sniraisni, M., and Ikeda, S. 1972. “Effect of Ascorbic Acid on the Gel Formation of Fish Meat.” Nippon Suisan Gakkaishi. 38:511–515.CrossRefGoogle Scholar

Copyright information

© Chapman & Hall, Inc. 1994

Authors and Affiliations

  • Tyre C. Lanier

There are no affiliations available

Personalised recommendations