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Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage.

Author(s) : LEBLANC E. L., LEBLANC R. J.

Type of article: Article

Summary

Possibles sources for denaturation or reticulation of proteins are studied by inducing texture changes. Measured are surface hydrophobicity and contents of SH-, SS-, NH2-free and aldehyde groups of sarcoplasmic fractions, rich in myosin or SDS soluble, isolated from the frozen fillet and stored at -30, -22, -15 or -12 deg C for 300 days. Hydrophobicity changes could be related to the increase in SS bridges, ester bindings and aldehyde and NH2-free groups.

Details

  • Original title: Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage.
  • Record ID : 1992-2866
  • Languages: English
  • Source: J. agric. Food Chem. - vol. 43 - n. 1
  • Publication date: 1992

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