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The effect of freezing and aldehydes on the interaction between fish myoglobin and myofibrillar proteins

Manat Chaijan1, Soottawat Benjakul, Wonnop Visessanguan

  • 1Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, 90112, Thailand.

Journal of Agricultural and Food Chemistry
|May 10, 2007
PubMed

Insights

Fish myoglobin (Mb) interaction with actomyosin (NAM) is reduced in frozen fish and affected by aldehyde oxidation products. Aldehydes cause cross-linking, impacting solubility and whiteness, with varying effects on Ca2+-ATPase activity.

Area of Science:

  • Food Science
  • Biochemistry
  • Protein Chemistry

Background:

  • Fish myoglobin (Mb) and natural actomyosin (NAM) are key proteins influencing fish quality.
  • Frozen storage and oxidation can alter protein interactions and quality attributes.
  • Understanding these interactions is crucial for improving fish product stability.

Purpose of the Study:

  • To investigate the interaction between fish myoglobin (Mb) and natural actomyosin (NAM) from fresh and frozen fish.
  • To assess the impact of aldehyde oxidation products on Mb-NAM interactions and fish quality indicators.
  • To elucidate the mechanisms of aldehyde-induced cross-linking between Mb and myofibrillar proteins.

Main Methods:

  • Extraction and quantification of soluble Mb in Mb-NAM complexes from fresh and frozen fish.
  • Measurement of metmyoglobin (MetMb) formation in Mb-NAM and control Mb.
  • In vitro studies using aldehyde oxidation products (hexenal, hexanal) to evaluate effects on Mb solubility, NAM whiteness, and Ca2+-ATPase activity.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to analyze protein cross-linking.

Main Results:

  • Soluble Mb quantity was lower in frozen fish compared to fresh fish.
  • MetMb formation was generally higher in Mb-NAM than in control Mb, with the highest content in frozen whole fish extracts.
  • Aldehydes (hexenal, hexanal) reduced Mb solubility and whiteness of NAM; hexenal caused greater OxyMb oxidation than hexanal.
  • Aldehydes affected NAM Ca2+-ATPase activity, with interactions modified by the presence of Mb.
  • SDS-PAGE indicated both disulfide and nondisulfide covalent linkages in aldehyde-induced cross-linking.

Conclusions:

  • Frozen storage negatively impacts fish Mb-NAM solubility.
  • Aldehyde oxidation products significantly alter fish Mb-NAM interactions, reducing solubility and whiteness.
  • Aldehydes induce covalent cross-linking between fish Mb and myofibrillar proteins, affecting protein functionality and quality.

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