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Investigating the mechanisms behind magnetic field effects on shrimp myofibrillar protein conformation and

Fangqi Yuan1, Jingxu Zhao1, Chunhong Yuan2

  • 1College of Food Science and Engineering, Ningbo University, Ningbo 315211, China; Zhejiang Key Laboratory of Intelligent Food Logistic and Processing, Zhejiang-Malaysia Joint Research Laboratory for Agricultural Product Processing and Nutrition, Ningbo University, Ningbo 315211, China.

Food Chemistry
|August 22, 2025
PubMed

Insights

A 5 mT static magnetic field inhibits oxidation and preserves the structure and function of shrimp myofibrillar proteins (MP). This effect protects against denaturation and deterioration, offering insights into protein stabilization.

Area of Science:

  • Food Science
  • Biophysics
  • Protein Chemistry

Background:

  • Myofibrillar proteins (MP) are crucial for seafood texture and quality.
  • Understanding factors affecting MP stability is vital for food preservation.
  • Static magnetic fields (SMF) are explored for their potential effects on biological systems.

Purpose of the Study:

  • To investigate the regulatory mechanism of a 5 mT static magnetic field (SMF) on shrimp myofibrillar protein (MP) structure and function.
  • To elucidate how SMF influences protein oxidation, aggregation, and enzymatic activity.

Main Methods:

  • Construction of different states of MP systems under varying SMF conditions (S-MF, H-MF, L-MF).
  • Assessment of protein oxidation via sulfhydryl content and surface hydrophobicity.
  • Measurement of Ca2+-ATPase activity.
  • Analysis of structural changes using the ratio of α-helical to β-sheet structures.

Main Results:

  • The S-MF group showed inhibited protein oxidation, highest sulfhydryl content, lowest surface hydrophobicity, and minimal decrease in Ca2+-ATPase activity and α-helical/β-sheet ratio.
  • The H-MF group exhibited complete dissociation of actin and myosin, leading to increased aggregation, oxidation, and enzyme inactivation.
  • The L-MF group displayed intermediate structural stability between the S-MF and H-MF groups.

Conclusions:

  • A 5 mT static magnetic field effectively mitigates conformational denaturation and functional decline in shrimp MP.
  • SMF inhibits protein side-chain oxidation and utilizes the muscle matrix's shielding effect for stabilization.
  • This study provides a mechanism for SMF's protective role in protein preservation.
Keywords:
Biochemical propertiesMyofibrillar proteinPenaeus vannameiSecondary structureStatic magnetic field

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