INVESTIGADORES
ZARITZKY Noemi Elisabet
artículos
Título:
Ice recrystallization in a model system and in frozen muscle tissue
Autor/es:
MARTINO M.N.; ZARITZKY NOEMI.
Revista:
CRYOBIOLOGY
Editorial:
ACADEMIC PRESS INC ELSEVIER SCIENCE
Referencias:
Lugar: Amsterdam; Año: 1989 vol. 26 p. 138 - 148
ISSN:
0011-2240
Resumen:
Recrystallization produces modifications on ice crystal sizes during storage and transport of frozen foods, reducing the advantages obtained by quick freezing and inducing physicochemical changes which alter their quality and shorten their shelf life. This process involves the growth of the larger crystals at the expense of the smaller ones, being the interfacial energy, the driving force of the phenomenon. In the present work recrystallization was analyzed using direct microscopic observation of ice crystals in a model solution (0.28 N NaCl) and indirect observation of frozen muscle tissue. The model solution allowed visualization of the interface behavior; from the analysis of the ice crystal frequency distributions, relationships between shape and size of the grains were established. A kineticmodel based on the average system curvature was proposed obtaining a satisfactory fitness of the experimental data. Values of the kinetic constants determined at different temperatures allowed the estimation of the process activation energy. In muscle tissues isothermal freeze-substitution was used to observe the holes left by the ice in frozen semitendinous beef muscle stored at -5, - 10, - 15, and -20°C during long periods of time. A different evolution of the mean ice crystal diameter was observed with respect to the model system. In meat samples, at long storage times, a limit diameter value was reached; this situation has been proved to be independent of temperature and initial size (freezingrate); a theoretical expression based on tissue characteristic parameters was proposed for its evahtation.Activation energy for recrystallization in muscle tissue was also determined, being comparable to values for protein denaturation and quality losses.