Denaturation Kinetics of Myofibrillar Proteins in Bovine Muscle

Differential scanning calorimetry was used to monitor the thermal denaturation kinetics of myofibrillar proteins in bovine muscle at pH 5.6. The activation energy, pre‐exponential factor, rate constant and mean life time for each transition were calculated by means of a dynamic method. The kinetic v...

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Autor principal: WAGNER, J.R
Otros Autores: AÑON, M.C
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1985
Acceso en línea:Registro en Scopus
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100 1 |a WAGNER, J.R. 
245 1 0 |a Denaturation Kinetics of Myofibrillar Proteins in Bovine Muscle 
260 |c 1985 
270 1 0 |m WAGNER, J.R.; Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA), Facultad de Ciencias Exactas, Provincia de Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Buttkus, H., Accelerated denaturation of myosin in frozen solution (1970) Journal of Food Science, 35, p. 558 
504 |a Burke, M., Himmelfarb, S., Harrington, W.F., Studies on the “Hinge” region of myosin (1973) Biochemistry, 12, p. 701 
504 |a Duswalt, A.A., The practice of obtaining kinetics data by differential scanning calorimetry (1974) Thermochim. Acta, 8, p. 57 
504 |a Eyring, H., Stearn, A.E., The application of the theory of absolute reaction rates to proteins (1939) Chem. Rev., 24, p. 253 
504 |a Goodno, C.C., Harris, T.A., Swenson, C.A., Thermal transitions of myosin and its helical fragments. Regions of structural instability in the myosin molecule (1976) Biochemistry, 15, p. 5157 
504 |a Hamm, R., Water‐holding capacity of meat (1975) Meat, p. 321. , D.J.A. Cole, R.A. Lowry, Avi Publishing Co. Inc, Westport, CT 
504 |a Hamm, R., Change of muscle proteins during heating of meat (1977) Physical, Chemical and Biological Changes in Food Caused by Thermal Processing, p. 101. , T. HØyem, O. Kvle, Applied Sci. Publ, London 
504 |a Laidler, K.J., Bunting, P.S., The denaturation of proteins (1973) The Chemical Kinetics of Enzyme Action, p. 413. , Clarendon Press, Oxford 
504 |a Levy, M., Benaglia, A.E., The influence of temperature and pH upon the rate of denaturation of ricin (1950) J. Biol. Chem., 186, p. 829 
504 |a Martens, H., Stabursvik, E., Martens, M., Texture during cooking related to thermal denaturation of muscle proteins (1982) Journal of Texture Studies, 13, p. 291 
504 |a Matthews, A.D., Park, G.R., Anderson, E.M., Evidence for the formation of covalent cross‐linkend myosin in frozen‐stored cod minces (1980) Advances in Fish Science and Technology, p. 438. , Fishing News Books Ltd. Aberdeen, U.K 
504 |a Multon, J.L., Sur quelques aspects thermodynamiques de la denaturation thermique des proteines en milien solide peu hydrate (1970) C.R. Acad. Sc. Paris, t., 271, p. 601 
504 |a Ockerman, H.W., Meat proteins (1977) Food Colloids, p. 240. , Avi Publishing Co. Inc, Wesport, CT 
504 |a Ozawa, T., Kinetic analysis of derivative curves in thermal analysis J (1970) Thermal Anal., 2, p. 301 
504 |a Pelletier, G.E., Ouellet, L., Influence of pH and temperature on myosin inactivation (1961) Canadian Journal of Chemistry, 39, p. 265 
504 |a Pravisani, C.I., Califano, A.N., Calvelo, A., Kinetics of starch gelatinization in potato (1985) Journal of Food Science, 50, p. 657 
504 |a Samejima, K., Takahashi, K., Yasui, T., Heat‐induced denaturation of myosin total rod (1976) Agric. Biol. Chem., 40, p. 2455 
504 |a Stabursvik, E., Martens, H., Proteins in white and red muscle compared by differential scanning calorimetry (DSC) (1979) 25th Eur. Meet. Meat Res. Work. Budapest, 5., 21, p. 383 
504 |a Stabursvik, E., Martens, H., Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry (1980) Journal of the Science of Food and Agriculture, 31, p. 1034 
504 |a Wright, D.J., Leach, I.B., Wilding, P., Differential scanning ca‐lorimetric studies of muscle and its constituent proteins (1977) J. Sci. Fd. Agric., 28, p. 557 
504 |a Wright, D.J., Wilding, P., Differential scanning calorimetry study of muscle and its proteins: Myosin and its subfragments (1984) J. Sci. Food Agric., 35, p. 357 
520 3 |a Differential scanning calorimetry was used to monitor the thermal denaturation kinetics of myofibrillar proteins in bovine muscle at pH 5.6. The activation energy, pre‐exponential factor, rate constant and mean life time for each transition were calculated by means of a dynamic method. The kinetic values and the proposed reaction order (n= 1) were confirmed applying an isothermal method as a test. The position of the endothermal peaks proved to be pH dependent. Evidences suggest that peak III is a result of actin denaturation and possibly other thin filament proteins. Peaks I and II would represent the thermal transition of thick filaments. The number of bonds involved in each transition were estimated. Copyright © 1985, Wiley Blackwell. All rights reserved  |l eng 
593 |a Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA), Facultad de Ciencias Exactas, Provincia de Buenos Aires, Argentina 
700 1 |a AÑON, M.C. 
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