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PROTEIN DENATURATION IN BOVINE MUSCLE DURING FROZEN STORAGE.

Author(s) : WAGNER J. R., ANON M. C.

Summary

THE EFFECT OF FREEZING ON THE THERMAL TRANSITIONS IN BOVINE MUSCLE WAS STUDIED. BOTH THE ENTHALPY OF THE TOTAL ENDOTHERM AND SPECIFIC AREAS OF THE TRANSITIONS I AND II DECREASED WITH STORAGE. THE TMAX VALUES OF PEAK I ALSO DECREASED INDICATING A LOSS OF THERMAL STABILITY OF THE GLOBULAR ZONE AND AN INCREASE OF HYDROPHOBIC INTERACTIONS. MEASUREMENTS OF MYOFIBRILLAR ATPASE ACTIVITY CONFIRMED THE ALTERATION OF THE MYOSIN HEAD DURING FROZEN STORAGE. THE SOLUBILITY OF MYOFIBRILLAR PROTEINS BEGAN TO DECREASE ONLY WHEN A CERTAIN DEGREE OF MYOSIN DENATURATION WAS REACHED.

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Pages: 717-722

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Details

  • Original title: PROTEIN DENATURATION IN BOVINE MUSCLE DURING FROZEN STORAGE.
  • Record ID : 1988-2350
  • Languages: English
  • Source: Development in refrigeration, refrigeration for development. Proceedings of the XVIIth international Congress of Refrigeration.
  • Publication date: 1987/08/24
  • Document available for consultation in the library of the IIR headquarters only.

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