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SOME PROPERTIES OF MYOFIBRILLAR PROTEINS OF ANTARCTIC KRILL AND THEIR DENATURATION DURING FROZEN STORAGE.

[In Japanese. / En japonais.]

Author(s) : KONAGAYA S., WATANABE T., KANNA K.

Type of article: Article

Summary

SOME RESEARCHERS SUSPECTED THAT THE MYOFIBRILLAR PROTEINS (MP) OF MUSCLE PROTEIN OF ANTARCTIC KRILL (EUPHAUSIA SUPERBA) ARE WATER-SOLUBLE, EXTREMELY UNSTABLE IN FROZEN STATE, AND FURTHERMORE, VERY SUSCEPTIBLE TO AUTOLYSIS. IF THIS IS TRUE, THERE WILL BE PROBLEMS WHEN KRILLIS USED FOR PROCESSING PRODUCTS. FIRST OF ALL, THE EXTRACTABILITY OF THE MUSCLE PROTEINS IN WATER AND BUFFERIZED KCL SOLUTIONS (PH 7.3) WITH DIFFERENT IONIC STRENGTH (I=0.2-0.6) WERE DETERMINED. THE MOLECULAR PROPERTIES OF THE PROTEINS WHICH WERE EXTRACTED WITH KCL SOLUTION (I=0.5) WERE EXAMINED BY MEANS OF ANALYTICAL ULTRACENTRIFUGE, SDS (SODIUM DODECYLSULFATE DISC-ELECTROPHORESIS AND FLOW BIREFRINGENCE (FB) MEASUREMENT. SINCE THE PROTEINS EXTRACTED WITH KCL SOLUTION (I=0.5) ARE DIFFERENT FROM THOSE EXTRACTED WITH WATER (I=0.05), THE FORMER MUST BE MP ITSELF, AND ARE INSOLUBLE IN WATER (I=0.05). THE SALT SOLUBLE PROTEIN FRACTION CONTAINING MP SHOWED NO PEAK OF ACTOMYOSIN IN THE TERN, EVEN THOUGH IT SHOWED STRONG FB AND BOTH ACTIN AND MYOSIN WERE DETECTED BY THE SDS DISC-ELECTROPHORESIS. THESE FINDINGS SUGGEST THAT THE MOLECULAR PROPERTIES OF THE KRILL MP ARE VERY DIFFERENT FROM THOSE OF TIGER SHRIMP WHICH WAS USED AS THE REFERENCE MATERIAL. THE KRILL MP WAS FOUND TO BE STABLE AT A STORAGE TEMPERATURE OF 233 K (-40.C) FOR 9 MONTHS, BUT UNSTABLE ABOVE 246 K (-27.C), FOR INSTANCE, ABOUT HALF OF THE TOTAL MP WERE DENATURED WITHIN 3 MONTHS AT 253 K (-20.C), AND WITHIN 9 MONTHS AT 246 K.

Details

  • Original title: [In Japanese. / En japonais.]
  • Record ID : 1982-0160
  • Languages: Japanese
  • Source: Refrigeration - vol. 56 - n. 639
  • Publication date: 1981
  • Document available for consultation in the library of the IIR headquarters only.

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