Seafood Proteins pp 84-98 | Cite as
The Effect of Heat-Induced Changes in Nitrogenous Constituents on the Properties of Seafoods
Abstract
Heating, as applied in seafood technology, affects the rate of enzymatic processes, brings about denaturation and subsequent interactions of proteins, and accelerates chemical reactions of different tissue components. Therefore, heated seafoods change in color and in rheological properties, lose part of their water-retention capacity, and develop new, mostly very desirable flavor characteristics. The character and extent of these changes are affected by the rate, duration, and temperature of heating, as well as by the composition, biochemical state, and integrity of the food structure, the pH of the environment, the presence of different added substances, mainly salts, macromolecular extenders, and polyols, and the access of air (Aitken and Connell, 1979; Pan, 1990). Investigations on the effect of these factors should provide the fish processor with knowledge necessary to control the quality of cooked seafood products. Proper choice of heating rate, duration, temperature, and humidity may prevent losses in hot smoking of fish (Sikorski et al., 1984). Applying high enough time/temperature in cooking of crab may minimize leaching losses of soluble proteins and discoloration as well as facilitates the picking of the meat (Zaitsev et al., 1969; Dowdie and Biede, 1983).
Keywords
Hydrogen Sulfide Crucian Carp Paralytic Shellfish Poison Cooking Loss Fish MeatPreview
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References
- Aitken, A., and Connell, J. J. 1979. “Fish.” Pp. 219–253. In Effects of Heating on Foodstuffs, edited by R. J. Priestley. London: Applied Science Publishers.Google Scholar
- Babbitt, J. K. 1982. “Blueing Discoloration of Dungeness Crabmeat.” Pp. 423428. In Chemistry and Biochemistry of Marine Food Products, edited by R. E. Martin, G. J. Flick, C. E. Hebard, and D. R. Ward. New York: Van Nostrand Reinhold.Google Scholar
- Bailey, M. E., and Einig, R. G. 1986. “Reaction Flavors of Meat.” In Thermal Generation of Aromas, edited by T. H. Parliment, R. J. McGorrin, and Ch. T. Ho. Chap. 39. Washington, DC: American Chemical Society.Google Scholar
- Beas, V. E., Wagner, J. R., Crupkin, M., and Anon, M. C. 1990. “Thermal Denaturation of Hake (Merluccius hubbsi) Myofibrillar Proteins. A Differential Scanning Calorimetric and Electrophoretic StudyJ. Food Sci. 55:683–687.Google Scholar
- Beraquet, N. J., Mann, J., and Aitken, A. 1984. “Heat Processing of Herring. I. Release of Water and Oil.” J. Food Technol. 19: 437–446.CrossRefGoogle Scholar
- Boismenu, D., Lepine, F., Gagnon, M., and Dugas, H. 1990. “Heat Inactivation of Catalase from Cod Muscle and from Some Psychrophilic Bacteria.” J. Food Sci. 55: 581–582.CrossRefGoogle Scholar
- Boon, D. D. 1977. “Coloration in Bivalves. A ReviewJ. Food Sci. 42:1008–1015.Google Scholar
- Buttkus, H. 1974. “On the Nature of the Chemical and Physical Bonds Which Contribute to Some Structural Properties of Protein Foods. A Hypothesis.” J. Food Sci. 39: 484–489.CrossRefGoogle Scholar
- Bykowski, P., and Kolodziejski, W. 1983. “Wla§ciwosci Miesa z Kryla Odskorpio- nego Metoda Rolkowa.” Bull. Sea Fish. Instit. Gdynia 14 (5–6): 53–57.Google Scholar
- Dowdie, O. G., and Biede, S. L. 1983. “Influence of Processing Temperature on the Distribution of Tissue and Water-Soluble Proteins in Blue Crabs (Callinectes sapidus).” J. Food Sci. 48: 804–807, 812.Google Scholar
- Dunajski, E. 1977. “Wplyw Temperatury, pH i Sily Jonowej na Twardosé Miesni Ryb.” P. 22. 8 Sesja Naukowa Ktchz PAN, Streszczenia Doniesien. Poznan. Komitet Technologii i Chemii Zywnosci PAN.Google Scholar
- Dunajski, E. 1979. “Texture of Fish Muscle.” J. Texture Studies 10: 301–318.CrossRefGoogle Scholar
- Dworschak, E. 1980. “Nonenzyme Browning and Its Effect on Protein Nutrition.” Crit. Rev. Food Sci. Nutr. 13: 1–40.Google Scholar
- Pr4czak, A., and Pajdowski, Z. 1955. “0 Rozkladzie Grup Sulfhydrylowych pod Wplywem Obróbki Termicznej w Miesie.” Przemyst Spozywczy. 9: 334–336.Google Scholar
- Gill, T. A., Thompson, J. W., and Gould, S. 1985. “Thermal Resistance of Paralytic Shellfish Poison in Soft-Shell Clams.” J. Food Protect. 48: 659–662.Google Scholar
- Hamann, D. D., Amato, D. 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.CrossRefGoogle Scholar
- Hayashi, T., Ibhh, H., and Shinohara, A. 1990. “Novel Model Experiment for Cooking Flavor Research on Crab Leg Meat.” Food Rev. Internat. 6: 52 1536.Google Scholar
- Hsieh, T. C. Y., Vejaphan, W., Williams, S. S., and Matiella, J. E. 1989. “Volatile Flavor Compounds in Thermally Processed Louisiana Red Swamp Crayfish and Blue Crab.” In Thermal Generation of Aromas, edited by T. H. Parliment, R. J. McGorrin, and C. T. Ho. ACS Symposium Series 409. Chap. 36. Washington, DC: American Chemical Society.Google Scholar
- Johnson, E. R., and Vickery, J. R. 1964. “Factors Influencing the Production of Hydrogen Sulphide from Meat During Heating.” J. Sci. Food Agric. 15: 695–701.CrossRefGoogle Scholar
- Kanoh, S., Polo, J. M. A., Kariya, Y., Kaneko, T., Watabe, S., and Hashimoto, K. 1988. “Heat-induced Textural and Histological Changes of Ordinary and Dark Muscles of Yellowfin Tuna.” J. Food Sci. 53: 673–678.CrossRefGoogle Scholar
- Khayat, A. 1978. “Hydrogen Sulfide Production by Heating Different Protein Fractions of Tuna Meat.” J. Food Biochem. 2: 121–131.CrossRefGoogle Scholar
- Kinoshita, M., Toyohara, H., and Shimizu, Y. 1990. “Characterization of Two Distinct Latent Proteinases Associated with Myofibrils of Crucian Carp (Carassius auratus cuvieri).” Comp. Biochem. Physiol. 97B: 315–319.Google Scholar
- Kreuzer, R. 1984. “Cephalopods: Handling, Processing, and Products.” FAO Fish Tech. Paper 254. Rome: Food and Agriculture Organization.Google Scholar
- Kubata, K., Iuchida, CH., Kurosawa, K., Komuro, A., and Kobayashi, A. 1989. “Identification and Formation of Characteristic Volatile Compounds from Cooked Shrimp.” In Thermal Generation of Aromas, edited by T. H. Parli-ment, R. J. McGorrin, and C. T. Ho. ACS Symposium Series 409. Chap. 35. Washington, DC: American Chemical Society.Google Scholar
- Kuo, J. M., and Pan, B. S. 1991. “Effects of Lipoxygenase on Formation of the Cooked Shrimp Flavor Compound 5,8,11—tetradecatrien-2-one.” Agric. Biol. Chem. 55: 847–848.CrossRefGoogle Scholar
- Lall, B. S., Manzer, A. R., and Hiltz, D. F. 1975. “Treatment for Improvement of Frozen Storage Stability at —10°C in Fillets and Minced Flesh of Silver Hake.” J. Fish. Res. Bd. Canada 32: 1450–1454.CrossRefGoogle Scholar
- Lindsay, R. C. 1990. “Fish Flavors.” Food Rev. Internat. 6: 437–455.CrossRefGoogle Scholar
- Motohiro, T. 1982. “The Effect of Heat Processing on Color Characteristics in Crustacean Blood.” Pp. 405–413. In Chemistry and Biochemistry of Marine Food Products, edited by R. E. Martin, G. J. Flick, C. E. Hebard, and D. R. Ward, New York: Van Nostrand Reinhold.Google Scholar
- Nakagawa, T., and Nagayama, F. 1989. “Interaction of Fish Muscle Glycolytic Enzymes with F-actin and Actomyosin.” Nippon Suisan Gakkaishi. 55: 165171.Google Scholar
- Opstved, J., Miller, R., Hardy, R. W., and Spinelli, J 1984. “Heat-induced Changes in Sulfhydryl Groups and Disulfide Bonds in Fish Protein and Their Effect on Protein and Amino Acid Digestibility in Rainbow Trout (Salmo gairdneri).” J. Agric. Food Chem. 32: 929–935.CrossRefGoogle Scholar
- Otwell, W. S., and Hamann, D. D. 1979. “Textural Characterization of Squid Loligo pealei.” J. Food Sci. 44: 1629–1635, 1643.Google Scholar
- Pan, B. S. 1990. “Minced Fish Technology.” Pp. 190–210. In Seafood.. Resources, Nutritional Composition, and Preservation, edited by Zdzislaw E. Sikorski. Boca Raton, FL: CRC Press.Google Scholar
- Pan, B. S., and Kuo, J. M. 1991. “Flavor of Shellfish and Kamaboko Flavorants.” Paper read at 8th World Congress of Food Science and Technology, 29 September-4 October, Toronto, Canada.Google Scholar
- Pan, B. S., Kuo, J. M., Luo, L. J., and Yang, H. M. 1986. “Effect of Endogenous Proteinases on Histamine and Honeycomb Formation in Mackerel.” J. Food Biochem. 10: 305–319.CrossRefGoogle Scholar
- Prell, P. A., and Sawyer, f. M. 1988. “Flavor Profiles of 17 Species of North Atlantic Fish.” J. Food Sci. 53: 1036–1042.CrossRefGoogle Scholar
- Sadowska, M., and Sikorski, Z. E. 1977. “Evaluation of Technological Suitability of Fish Meat by Rheological Measurements.” Lebens.-Wiss. u.-Technol. 10: 239–245.Google Scholar
- Schutte, L. 1974. “Precursors of Sulfur-Containing Flavor Compounds.” Crit. Rev. Food Technol. 4: 457–504.CrossRefGoogle Scholar
- Shahidi, F., Rubin, L. J. and D’souza, L. A. 1986. “Meat Flavor Volatiles: A Review of the Composition, Techniques of Analysis, and Sensory Evaluation.” Crit. Rev. Food Sci. Nutr. 24: 141–243.CrossRefGoogle Scholar
- Sikorski, Z. E., and Kolodziejska, I. 1986. “The Composition and Properties of Squid Meat.” Food Chem. 20: 213–224.CrossRefGoogle Scholar
- Sikorski, Z. E., Scott, D. N., and Buisson, D. H. 1984. “The Role of Collagen in the Quality and Processing of Fish.” Crit. Rev. Food Sci. Nutr. 20: 30 1343.Google Scholar
- Spinelli, J, and Koury, B. 1979. “Nonenzymic Formation of Dimethylamine in Dried Fishery Products.” J. Agric. Food Chem. 27: 1104–1108.CrossRefGoogle Scholar
- Spinelli, J, and Koury, B. 1981. “Some New Observations on the Pathways of Formation of Dimethylamine in Fish Muscle and Liver.” J. Agric. Food Chem. 29: 327–331.CrossRefGoogle Scholar
- Stanley, D. W., and Hultin, H. O. 1982. “Quality Factors in Cooked North Atlantic Squid.” Can. Inst. Food Sci. Technol. J. 15: 227–282.Google Scholar
- Suzuki, J., Ichimura, N., and Etoh, T. 1990. “Volatile Components in Boiled Scalop.” Food Rev. Internat. 6: 537–552.CrossRefGoogle Scholar
- Synowiecki, J., and Sikorski, Z. E. 1988. “Heat Induced Changes in Thiol Groups in Squid Proteins.” J. Food Biochem. 12: 127–135.CrossRefGoogle Scholar
- Synowiecki, J., and Shahidi, F. 1991. “Heat-induced Changes in Sulfhydryl Groups of Seal Muscle Protein.” J. Agric. Food Chem. 39: 2006–2009.CrossRefGoogle Scholar
- Tanaka, M., Okubo, S., Suzuki, K., and Taguchi, T. 1980. “Available Lysine Losses in Water Soluble Protein of Mackerel Meat by Heating.” Bull. Japan. Soc. Sci. Fish. 46: 1539–1543.CrossRefGoogle Scholar
- Tanaka, M., Okubo, S., Suzuki, K., and Taguchi, T. 1981. “Available Lysine Losses in Salt Soluble Proteins of Mackerel by Heating.” Bull. Japan. Soc. Sci. Fish. 47: 1075–1078.CrossRefGoogle Scholar
- Tooley, P. J., Lawrie, R. A. 1974. “Effect of Deep Fat Frying on the Availability of Lysine in Fish Fillets.” J. Food Technol. 9: 247–253.CrossRefGoogle Scholar
- Toyohara, H., Kinoshita, M., and Shimizu, Y. 1990. “Proteolytic Degradation in Threadfin-Bream Meat Gel.” J. Food Sci. 55: 259–260.CrossRefGoogle Scholar
- Toyohara, H., Sakata, T., Yamashita, K., Kimoshita, M., and Shimizu, Y. 1990a. “Degradation of Oval-Filefish Meat Gel Caused by Myofibrillar Proteinase(s). J. Food Sci. 55: 364–368.Google Scholar
- Toyohara, H., Susaki, K., Kinoshita, M., and Shimizu, Y. 1990b. “Effect of Bleeding in the Modori Phenomenon and Possible Existence of Some Modori-Inhibitor in Serum.” Nippon Suisan Gakkaishi. 56: 1245–1249.CrossRefGoogle Scholar
- Zaitsev, V., Kizevetter, I., Lagunov, L., Makarova, T., Minder, L., and Podsevalov, V. 1969. Fish Curing and Processing. Moscow: Mir Publishers.Google Scholar