Biochemical and Functional Characteristics of Myosin from Red and White Muscles of Chicken as Influenced by Nutritional Stress
TLDR
In this article, the physicochemical and functional properties of myosin from red (red-myosin) and white (white-myopsin) muscles of broilers, grown at different planes of nutrition, were studied.Abstract:
Physicochemical and functional properties of myosin from red (red-myosin) and white (white-myosin) muscles of broilers, grown at different planes of nutrition, were studied. The red- and white-myosin from well-nourished broilers exhibited characteristic difference in certain physico-chemical properties. The specific viscosity of red-myosin was lower and sedimentation coefficient ( S202o,w) was higher than that of white-myosin. The transition of monomer⇌filament phase of white-myosin seemed to occur in a narrower range of ionic strength than that of red-myosin. Under identical conditions (ionic strength, pH, protein concentration, temperature) of the model system, white-myosin always exhibited greater gel strength than that of red-myosin. Characteristic differences were also observed in the three-dimensional structure of red- and white-myosin gel.Heat-induced gel strength of red-myosin from under-fed broilers was about 50% less than that of control, whereas the gelling property of white-myosin was not infl...read more
Citations
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Journal ArticleDOI
Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods
Xiang Dong Sun,Richard A. Holley +1 more
TL;DR: In this paper, the authors consolidate information on determinants of protein gel formation, examining types of muscles and fibers, the species influence and interactions of the MPs actin and myosin with each other and with fat, gelatin, starch, hydrocolloids, some protein soy, whey, and nonprotein additives such as phosphates and acidifiers, and the influences of pH, ionic strength, rates of heating, and its absence, protein oxidation, as well as the use of transglutaminase and high hydrostatic pressure.
Book ChapterDOI
The Gelation Of Proteins
TL;DR: The chapter reviews a variety of protein gel systems with a broad perspective stressing similarities between them, yet not without mentioning the important differences that make each unique.
Journal ArticleDOI
Functionality of muscle proteins in gelation mechanisms of structured meat products.
Ali Asghar,K Samejima,T Yasui +2 more
TL;DR: In this article, the role of different subunits and subfragments of myosin molecule in the gelation mechanism, and the various factors affecting heat-induced gelation of actomyosin in modal systems are also highlighted.
Journal Article
Recent Advances in Meat Science in Japan : Functionality of Muscle Proteins in Gelation Mechanisms of Structured Meat Products
Tsutomu Yasui,Kunihiko Samejima +1 more
TL;DR: The functionality of various muscle proteins, especially myosin and actin in the gelation process in modal systems which simulate structured meat products, is discussed at length and the areas which need further investigation in this discipline have been suggested.
Journal ArticleDOI
Dynamic rheological measurements on heat‐induced myosin gels: Effect of ionic strength, protein concentration and addition of adenosine triphosphate or pyrophosphate
TL;DR: In this article, the storage modulus, the loss modulus and the phase angle of myosin were measured at pH 6.0 by using dynamic rheological measurements and showed a marked dependence on ionic strength in the temperature range 25-75°C.
References
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Journal ArticleDOI
Light chains from fast and slow muscle myosins.
Susan Lowey,Dennis Risby +1 more
TL;DR: Myosin from fast skeletal muscles consists of two large subunits and approximately four smaller subunits which are heterogeneous in both size and charge, irrespective of the muscle type of origin.
Journal ArticleDOI
Distribution of polymorphic forms of troponin components and tropomyosin in skeletal muscle
G. K. Dhoot,S. V. Perry +1 more
TL;DR: Specific antibodies have been used to show that in adult skeletal muscle the slow and fast forms of the components of the troponin complex are located in type I and type II fibres respectively, α-Tropomyosin is restricted to type II cells.
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