Skip to main content
SpringerLink
Log in

The Myofibrillar Proteins in Seafoods

  • Chapter
Seafood Proteins

Abstract

Very concise and informative reviews on the myofibrillar proteins have been published by Maruyama (1985), Squire and Vibert (1987), Nakai and Li-Chan (1988), and Morrissey, Mulvihill, and O’Neill (1987). They describe not only the chemical structure, properties, and location of myosin and actin, of the regulatory proteins, and of the scaffold proteins in the ultrastructure of muscles but also the functional characteristics of several of these proteins.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Buttkus, H. 1970. “The Sulfhydryl Content of Rabbit and Trout Myosins in Relation to Protein Stability.” Can. J. Biochem 49: 97–107.

    Article  Google Scholar 

  • Careche, M., Currall, J., and Mackie, I. M. 1991. “A Study of the Effects of Different Factors on the Heat-Induced Gelation of Cod (Gadus morhua, L.) Actomyosin Using Response Surface Methodology.” Food Chem. 42: 39–55.

    Article  CAS  Google Scholar 

  • Carlier, M. F. 1991. “Actin: Protein Structure and Filament Dynamics.” J. Biol. Chem 266: 1–4.

    PubMed  CAS  Google Scholar 

  • Chen, C. S., Hwang, D. C., and Jiang, S. T. 1988. “Purification and Characterization of Milkfish (Chanos chanos) myosin.” Nippon Suisan Gakkaishi. 54: 1423 1427.

    Article  CAS  Google Scholar 

  • Connell, J. J. 1961. “The Relative Stabilities of the Skeletal–Muscle Myosins of Some Animals.” Biochem. J 80: 503–509.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Davies, J. R., Bardsley, R. G., Ledward, A. A., and Poulter, R. G. 1988. “Myosin Thermal Stability in Fish Muscle.” J. Sci. Food Agric 45: 61–68.

    Article  CAS  Google Scholar 

  • Demaille, J., Dutruge, E., Eisenberg, E., Capony, J. P., and Pechere, J. F. 1974. “Troponins C from Reptile and Fish Muscles and Their Relation to Muscular Parvalbumins.” FEBS Lett. 42: 173–178.

    Article  CAS  PubMed  Google Scholar 

  • Howell, B. K., Matthews, A. D., and Donnelly, A. P. 1991. “Thermal Stability of Fish Myofibrils: A Differential Scanning Calorimetric Study.” Internat. J. Food Sci. Technol 26: 283–295.

    Article  Google Scholar 

  • Ishioroshi, M., Samejima, K., and Yasui, T. 1981. “Further Studies on the Roles of the Head and Tail Regions of the Myosin Molecule in Heat-Induced Gelation.” J. Food Sci 47: 114–120, 124.

    Google Scholar 

  • Jiang, S. T., Wang, F. J., and Chen, C. S. 1989. “Properties of Actin and Stability of the Actomyosin Reconstituted from Milkfish (Chanos chanos) Actin and Myosin.” J. Agric. Food Chem 37: 1232–1235.

    Article  CAS  Google Scholar 

  • Kantha, S. S., Watabe, S., and Hashimoto, K. 1990. “Comparative Biochemistry of Paramyosin—A Review.” J. Food Biochem 14: 61–88.

    Article  CAS  Google Scholar 

  • Kelley, C. A., Sellers, J. R., Goldsmith, P. K., and Adelstein, R. S. 1992. “Smooth Muscle Myosin is Composed of Homodimeric Heavy Chains.”J. Biol. Chem 267: 2127–2130.

    Google Scholar 

  • Kimura, I., Yoshitomi, B., Konno, K., and ARAI, K. 1980. “Preparation of Highly Purified Myosin from Mantle Muscle of Squid. Ommastrephes sloani pacificus.” Bull. Japan. Soc. Sci. Fish 46: 885–92.

    Article  CAS  Google Scholar 

  • Kimura, S., Miyaki, T., Takema, Y., and Kubota, M. 1981. “Electrophoretic Analysis of Connectin from the Muscles of Aquatic Animals.” Bull. Japan. Soc. Sci. Fish 47: 787–791.

    Article  CAS  Google Scholar 

  • Lee, N., Seki, N., Kato, N., Nakagawa, N., Terui, S., and Arai, K. 1990a. “Gel Forming Ability and Cross-linking Ability of Myosin Heavy Chain in Salted Meat Paste from Threadfin Bream.” Nippon Suisan Gakkaishi. 56: 329–336.

    Article  CAS  Google Scholar 

  • Lee, N., Seki, N., Kato, N., Nakagawa, N., Terui, S., and Arai, K. 1990b. “Changes in Myosin Heavy Chain and Gel Forming Ability of Salt-Ground Meat from Hoki.” Nippon Suisan Gakkaishi. 56: 2093–2101.

    Article  CAS  Google Scholar 

  • Lo, J. R., Mochizuki, Y., Nagashima, Y., Tanaka, M., ISO, N., and TAGUCHI, T. 1991. “Thermal Transitions of Myosins/Subfragments from Black Marlin (Makaira mazara) Ordinary and Dark Muscles.” J. Food Sci 56: 954–957.

    Article  CAS  Google Scholar 

  • Macdonald, G. A., Lelievre, J., and Wilson, N. D. C. 1990. “Strength of Gels Prepared from Washed and Unwashed Minces of Hoki (Macruronus novaezelandiae) Stored in Ice. J. Food Sci 55: 976–978.

    Google Scholar 

  • Maita, T., Yajima, E., Nagata, S., Miyanishi, T., Nakayama, S., and Matsuda,G. 1991. “The Primary Structure of Skeletal Muscle Myosin Heavy Chain: IV. Sequence of the Rod, and the Complete 1,938-Residue Sequence of the Heavy Chain.” J. Biochem 110: 75–87.

    Article  CAS  PubMed  Google Scholar 

  • Malencik, D. A., Heizmann, C. W., and Fischer, E. H. 1975. “Structural Proteins of Dogfish Skeletal Muscle.” Biochemistry 14: 715–721.

    Article  CAS  PubMed  Google Scholar 

  • Martinez, I. 1989. “Water Retention Properties and Solubility of the Myofibrillar Proteins: Interrelationships and Possible Value as Indicators of the Gel Strength in Cod Surimi by a Multivariate Data Analysis. J, Sci. Food Agric 46: 469–479.

    Article  CAS  Google Scholar 

  • Martinez, I., Olsen, R. L., Ofstad, R., Janmot, C., and D’aldbis. A. 1989. “Myosin Isoforms in Mackerel (Scomber scombrus) Red and White Muscles.” FEBS Lett. 252 (1,2): 69–72.

    Article  Google Scholar 

  • Martone, C. B., Busconi, L., Folco, E. J., Trucco, R. E., and Sanchez, J. J. 1986. “A Simplified Myosin Preparation from Marine Fish Species.J. Food Sci 51:1554–1555.

    Article  CAS  Google Scholar 

  • Maruyama, K. 1985. “Myofibrillar Cytoskeletal Proteins of Vertebrate Striated Muscle.” Pp. 25–50. In Developments in Meat Science, Vol. 3, edited by R. Lawrie. London/New York: Elsevier Applied Science.

    Google Scholar 

  • Mccubbin, W. D., Oikawa, K., Sykes, K., and Kay, C. M. 1982. “Purification and Characterization of Troponin C from Pike Muscle: A Comparative Spectroscopic Study with Rabbit Skeletal Troponin C.” Biochemistry 21: 5948–5956.

    Article  CAS  PubMed  Google Scholar 

  • Miyazaki, J. I., Isimoda-Takagi, T., Sekigucho, K., and Hirabayashi, T. 1989.

    Google Scholar 

  • Comparative Study of Horseshoe Crab Tropomyosin.“ Comp. Biochem. Physiol 93B:681–687.

    Google Scholar 

  • Morrissey, P. A., Mulvihill, D. M., and O’neill, E. M. 1987. “Functional Properties of Muscle Proteins. Pp. 195–256. In Developments in Food Proteins, Vol. 7, edited by B. J. F. Hudson. London/New York: Elsevier Applied Science.

    Google Scholar 

  • Nakagawa, T., and Nagayama, F. 1989. “Interaction of Fish Muscle GlycolyticThe Myofibrillar Proteins in Seafoods 55 Enzymes with F-actin and Actomyosin.” Nippon Suisan Gakkaishi. 55: 165171.

    Article  CAS  Google Scholar 

  • Nakagawa, T., Nagayama, F., Ozaki, H., Watabe, S., and Hashimoto, K. 1989. “Effect of Glycolytic Enzymes on the Gel-forming Ability of Fish Muscle.” Nippon Suisan Gakkaishi. 55: 1945.

    Google Scholar 

  • Nakai, S., and LI-Chan, S. 1988. Hydrophobic Interactions in Food Systems. Boca Raton, FL: CRC Press.

    Google Scholar 

  • Nishita, K., and Ojima, T. 1990. “American Lobster Troponin.” J. Biochem 108: 677–683.

    Article  CAS  PubMed  Google Scholar 

  • Nishita, K., Takeda, Y., and Arai, K. 1981. “Biochemical Characteristics of Actomyosin from Antarctic Krill.” Bull. Japan. Soc. Sci. Fish 47: 1237–1244.

    Article  CAS  Google Scholar 

  • Niwa, E. 1992. “Chemistry of Surimi Gelation.” Pp. 389–427. In: Surimi Technology, edited by T. C. Lanier and C. M. Lee. New York. Basel, Hong Kong: Marcel Dekker.

    Google Scholar 

  • Nyitray, L., Goodwin, E. B., and Szent-Gy©Rgyi, A. G. 1991. “Complete Primary Structure of a Scallop Striated Muscle Myosin Heavy Chain.” J. Biol. Chem 266: 18469–18476.

    Google Scholar 

  • Oghiai, Y., Kobayashi, T., Handa, A., Watabe, S., and Hashimoto, K. 1990. “Possible Presence of the Difference Peptide in Alkali Light Chain 1 of the Fish Fast Skeletal Myosin.” Comp. Biochem. Physiol 97B: 794–801.

    Google Scholar 

  • Offer, G. 1987. “Myosin Filaments.” Pp. 307–357. In Fibrous Protein Structure, edited by J. M. Squire and Peter J. Vibert. London: Academic Press.

    Google Scholar 

  • Paredi, M. E., Mattio, N. V., and Crupkin, M. 1990. “Biochemical Properties of Actomyosin of Cold Stored Striated Muscles of Aulacomya ater ater (Molina).” J. Food Sci 55: 1567–1570.

    Article  CAS  Google Scholar 

  • Park, J. W., and Lanier, T. C. 1989. “Scanning Calorimetric Behavior of Tilapia Myosin and Actin Due to Processing of Muscle and Protein Purification.” J. Food Sci 54: 49–51.

    Article  CAS  Google Scholar 

  • Peyun, J. H., Hashimoto, K., and Matsuura, F. 1973. “Isolation and Characterization of Abalone Paramyosin.” Bull. Japan. Soc. Sci. Fish 39: 395–402.

    Article  Google Scholar 

  • Roussel, H., and Cheftel, J. C. 1990. “Mechanisms of Gelation of Sardine Proteins: Influence of Thermal Processing and of Various Additives on the Texture and Protein Solubility of Kamaboko Gels. Internat. J. Food Sci. Technol 25: 260–280.

    Article  Google Scholar 

  • Samejima, K., Ishioroshi, M., and Yasu!, T. 1981. “Relative Roles of the Head and Tail Portions of the Molecule in Heat-Induced Gelation of Myosin.” J. Food Sci 46: 1412–1418.

    Article  CAS  Google Scholar 

  • Sano, T., NoGucHI, S. F., Tsuchiya, T., and Matsumoto, J. J. 1986. “Contribution of Paramyosin to Marine Meat Gel Characteristics.J. Food Sci 51:946950.

    Article  CAS  Google Scholar 

  • Sano, T., Noguchi, S. F., Tsuchiya, T., and Matsumoto, J. J. 1988. “Dynamic Viscoelastic Behavior of Natural Actomyosin and Myosin During Thermal Gelation.” J. Food Sci 53: 924–928.

    Article  CAS  Google Scholar 

  • Sano, T., Nogucus, S. F., Matsumoto, J. J., and Tsuchiya, T. 1989a. “Role of

    Google Scholar 

  • F-actin in Thermal Gelation of Fish Actomyosin.“ J. Food Sci 54:800–804.

    Google Scholar 

  • Sano, T., Noguchi, S. F., Tsuchiya, T., and Matsumoto, J. J. 1989b. “Effect

    Google Scholar 

  • of Two-Step Heating on Gel Properties of a Paramyosin-Myosin System.“

    Google Scholar 

  • Sano, T., Noguchi, S. F., Tsuchiya, T., and Matsumoto, J. J. 1989c. “Paramyosin-Myosin-Actin Interactions in Gel Formation of Invertebrate Muscle.” J. Food Sci 54: 796–799, 842.

    Google Scholar 

  • Sano, T., Noguchi, S. F., Tsuchiya, T., and Matsumoto, J. J. 1989d. “Contribution of Tropomyosin to Fish Muscle Gel Characteristics.” J. Food Sci 54: 258–264, 279.

    Google Scholar 

  • Sano, T., Noguchi, S. F., Matsumoto, J. J., and Tsuchiya, T. 1989e. “Dynamic Viscoelastic Behavior of F-actin on Heating. J. Food Sci 54: 231–232.

    Article  CAS  Google Scholar 

  • Sano, T., Nocuchi, S. F., Matsumoto, J. J., and Tsuchiya, T. 1990a. “Effect of Ionic Strength on Dynamic Viscoelastic Behavior of Myosin During Thermal Gelation.” J. Food Sci 55: 51–54.

    Article  CAS  Google Scholar 

  • Sano, T., Nogughi, S. F., Matsumoto, J. J., and Tsuchiya, T. 1990b. “Thermal Gelation Characteristics of Myosin Subfragments.” J. Food Sci 55: 55–58.

    Article  CAS  Google Scholar 

  • Seki, N., and Hasegawa, E. 1978. “Comparative Studies on Fish Troponins.Bull. Japan. Soc. Sci. Fish 44:71–75.

    Article  CAS  Google Scholar 

  • Seki, N., and Iwabuchi, S. 1978. “On the Subunit Composition of Fish Tropomyosins.” Bull. Japan. Soc. Sci. Fish 44: 1333–1340.

    Article  Google Scholar 

  • Squire, J. M., and VIBERT, PETER J. (EDS.). 1987. Fibrous Protein Structure. London: Academic Press.

    Google Scholar 

  • Sugino, H., Kojima, N., Nishita, K., and Okima, T. 1989. “Characterization and Partial Amino Acid Sequence of CNBr-Fragments of Scallop Troponin C.” Nippon Suisan Gakkaishi. 55: 333–340.

    Article  CAS  Google Scholar 

  • SuzuKI, Taneko. 1981. Fish and Krill Protein: Processing Technology. London: Applied Science Publishers.

    Book  Google Scholar 

  • Taguchi, T., Ishizaki, S., Tanaka, M., Nagashima, Y., and Amano, K. 1989.

    Google Scholar 

  • Effectof Ultraviolet Irradiation on Thermal Gelation of Muscle Pastes.“ J. Food Sci 54:1438–1440.

    Google Scholar 

  • Takagi, T., and Konishi, K. 1983. “Amino Acid Sequence of Troponin C Obtained from Ascidian (Halocynthia roretzi) Body Wall Muscle.” J. Biochem 94: 1753–1760.

    Article  CAS  PubMed  Google Scholar 

  • Tanaka, H., Kimura, I., Arai, K., and Watanabe, S. 1982. “The Heat Denaturation of Myosins from Fishes and Squid.” Bull. Japan. Soc. Sci. Fish 48: 445453.

    Google Scholar 

  • Torley, P. J., Ingram, J., Young, O. A., and Meyer-Rochow, V. B. 1991. “Salt-

    Google Scholar 

  • Induced, Low-Temperature Setting of Antarctic Fish Muscle Proteins.“ J. Food Sci. 56: 251–252.

    Google Scholar 

  • Tsuchiya, T., Shinohara, T., and Matsumoto, J. J. 1980. “Physico-chemical Properties of Squid Tropomyosin.” Bull. Japan. Soc. Sci. Fish 46: 893–896.

    Article  CAS  Google Scholar 

  • Tsuchiya, T., Suzuki, H., and Matsumoto, J. J. 1977. “Isolation and Purification of Squid Actin.” Bull. Japan. Soc. Sci. Fish 43: 1233–40.

    Article  CAS  Google Scholar 

  • Tsuchiya, T., Yamada, N., and Matsumoto, J. J. 1978. “Extraction and Purification of Squid Myosin.” Bull. Japan. Soc. Sci. Fish 44: 175–179.

    Article  CAS  Google Scholar 

  • Tsuchimoto, M., Tanaka, N., Uesugi, Y., Misima, T., Tachibana, K., YADA, S., SENTA, T., and YASUDA, M. 1988a. “The Influence of Rearing Water Temperature on the Relative Thermostability of Myofibrillar Cat+ATPase and on the Lowering Speed of Freshness in Carp.” Nippon Suisan Gakkaishi. 54: 117–122.

    Article  CAS  Google Scholar 

  • Tsuchimoto, M., Tanaka, N., Misima, T., Yada, S., Senta, T., and YASUDA, M. 1988b. “The Influence of Habitat Water Temperature on the Relative Thermostability of Myofibrillar Cat+—ATPase in Fishes Collected in the Waters from Tropical to Frigid Zones.” Nippon Suisan Gakkaishi. 54: 787793.

    Article  CAS  Google Scholar 

  • Watabe, S., Dihn, T. N. L., Ochiai, Y., and Hashimoto, K. 1983. “Immunochemical Specificity of Myosin Light Chains from Mackerel Ordinary and Dark Muscles.” J. Biochem 94: 1409–1419.

    Article  CAS  PubMed  Google Scholar 

  • Watabe, S., and Hartshorne, D. J. 1990. “Paramyosin and the Catch Mechanism.” Comp. Biochem. Physiol 96B: 639–646.

    CAS  Google Scholar 

  • Watabe, S., Hashimoto, K., and Watanabe, S. 1983. “The pH Dependency of Myosin ATPases from Yellowtail Ordinary and Dark Muscles.” J. Biochem 94: 1867–1875.

    Article  CAS  PubMed  Google Scholar 

  • Watabe, S., Hwang, G. C., Nakaya, M., Guo, X. F., and OKAMOTO, Y. 1992. “Fast Skeletal Myosin Isoforms in Thermally Acclimated Carp.” J. Biochem 111: 113–122.

    Article  CAS  PubMed  Google Scholar 

  • Wicker, L., Lanier, T. C., KNOPP, J. A., and Hamann, D. D. 1989. “Influence of Various Salts on Heat-Induced ANS Fluorescence and Gel Rigidity Development of Tilapia (Serotherodon aureus) Myosin.” J. Agric. Food Chem 37: 18–22.

    Article  CAS  Google Scholar 

  • Wu, M., C., Lanier, T. C., and Hamann, D. D. 1985. “Rigidity and Viscosity Changes of Croacker Actomyosin During Thermal Gelation.” J. Food Sci 50: 14–19, 25.

    Google Scholar 

Download references

Authors
  1. Zdzisław E. Sikorski
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Department of Food Preservation, Technical University Politechnika Gdańska, 80-952, Gdańska, Poland

    Zdzisław E. Sikorski Ph.D., D.Sc., (Professor and Head) (Professor and Head)

  2. College of Fisheries Science, National Taiwan Ocean University, Keelung, Taiwan 202, Republic of China

    Bonnie Sun Pan Ph.D. (Professor and Dean) (Professor and Dean)

  3. Departments of Biochemistry and Chemistry, Memorial University of Newfoundland, A1B3X9, St. John’s, Newfoundland, Canada

    Fereidoon Shahidi Ph.D. (Professor) (Professor)

Rights and permissions

Reprints and permissions

Copyright information

© 1994 Chapman & Hall, Inc.

About this chapter

Cite this chapter

Sikorski, Z.E. (1994). The Myofibrillar Proteins in Seafoods. In: Sikorski, Z.E., Pan, B.S., Shahidi, F. (eds) Seafood Proteins. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-7828-4_4

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-7828-4_4

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4615-7830-7

  • Online ISBN: 978-1-4615-7828-4

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation