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EFFECT OF FROZEN STORAGE ON PROTEIN DENATURATION IN BOVINE MUSCLE. 1. MYOFIBRILLAR ATPASE ACTIVITY AND DIFFERENTIAL SCANNING CALORIMETRIC STUDIES.

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

Type of article: Article

Summary

MYOFIBRILLAR ATPASE ACTIVITY AND TOTAL ENTHALPY OF DENATURATION DECREASED WITH TIME OF STORAGE. THE RATE OF DECREASE WAS LOWER AT 253 K (-20 DEG C) THAN AT 268 OR 263 K (-5 OR -10 DEG C). DIFFERENCES IN BEHAVIOUR DURING STORAGE AFTER FAST OR SLOW FREEZING COULD BE ATTRIBUTED TO DIFFERENCES IN ICE RECRYSTALLIZATION. MYOSIN HEAD AND TAIL DENATURATED PROGRESSIVELY DURING STORAGE BUT THE THIN FILAMENT REMAINED UNALTERED. KINETIC ANALYSIS SUGGESTED THAT THE DENATURATION OF THE MYOFIBRILLAR PROTEINS TOOK PLACE THROUGHTWO CONSECUTIVE FIRST ORDER REACTIONS ; AN INITIAL RAPID REACTION FOLLOWED BY A SLOWER ONE.

Details

  • Original title: EFFECT OF FROZEN STORAGE ON PROTEIN DENATURATION IN BOVINE MUSCLE. 1. MYOFIBRILLAR ATPASE ACTIVITY AND DIFFERENTIAL SCANNING CALORIMETRIC STUDIES.
  • Record ID : 1986-2351
  • Languages: English
  • Source: J. Food Technol. - vol. 21 - n. 1
  • Publication date: 1986
  • Document available for consultation in the library of the IIR headquarters only.

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