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Muscle Polymorphism and Gelling Properties of Myofibrillar Proteins from Poultry, Mammals, and Fish

  • F. Lefèvre
  • J. Culioli
  • S. Joandel-Monier
  • A. Ouali

Abstract

Depending on their metabolic and contractile activities, muscles are classified in different types from fast-twitch glycolytic (white) to slow-twitch oxidative (red) muscles with several “intermediate” ones. Contractile proteins, especially myosins, are present in the myofibers of these various muscle types as different isoforms. The respective proportions of these isoforms give distinct functional properties. This review deals with the relation between muscle polymorphism and gelling properties of proteins which are largely involved in the elaboration of texture of meat, poultry and fish, as well as derived products in relation to water holding capacity and lipid retention ability. Protein dispersions from different muscle types exhibit distinct rheological behaviors during heating. Their sensitivities to parameters such as concentration, heating rate or physico-chemical environment (pH and ionic strength) are greatly dependent on muscle type. The influence of amino-acid composition and hydrophobicity of myosin isoforms on the functionality of muscle proteins is discussed

Keywords

Myosin Heavy Chain Muscle Protein White Muscle Myofibrillar Protein Muscle Type 
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.

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Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • F. Lefèvre
    • 1
  • J. Culioli
    • 2
  • S. Joandel-Monier
    • 2
  • A. Ouali
    • 2
  1. 1.Laboratoire de Physiologie des PoissonsINRARennes CedexFrance
  2. 2.Station de Recherches sur la ViandeINRA Centre de Clermont-Ferrand-TheixSaint-Genès ChampanelleFrance

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