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Structural Protein Function01:56

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A Protocol for Computer-Based Protein Structure and Function Prediction
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Structurally modified lysozyme via solvent browning: Toward functional protein-based antioxidants.

Chih-Jung Chang1, Ming-Chia Li2, Teh-Min Hu1

  • 1Department of Pharmacy, National Yang Ming Chiao Tung University, Yangming Campus, Taipei, 112304, Taiwan.

International Journal of Biological Macromolecules
|January 23, 2026
PubMed
Summary

Solvent-mediated Browning transforms hen egg white lysozyme, altering its structure and enhancing antioxidant activity while reducing antibacterial effects. This method offers a simple way to reprogram protein functionality for various applications.

Keywords:
AntioxidantsBrowning reactionLysozyme

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Area of Science:

  • Biochemistry
  • Protein Chemistry

Background:

  • Hen egg white lysozyme is a model protein with well-defined structural and functional characteristics.
  • Chemical modifications, such as the Maillard reaction, can alter protein bioactivity.
  • A novel solvent-mediated Browning reaction using dimethyl sulfoxide and acetone was previously identified.

Purpose of the Study:

  • To investigate the structural and functional changes in hen egg white lysozyme induced by solvent-mediated Browning.
  • To assess the potential of this method for protein reprogramming.

Main Methods:

  • Solvent-mediated Browning of lysozyme using dimethyl sulfoxide and acetone.
  • UV-vis spectroscopy for chromophore formation and color changes.
  • SDS-PAGE, FTIR, and CD spectroscopy for structural analysis.
  • Thiol quantification for disulfide bond assessment.
  • Fluorescence spectroscopy and surface hydrophobicity measurements.
  • Scanning Electron Microscopy (SEM) for morphological changes.
  • Antioxidant and antibacterial assays to evaluate functional properties.

Main Results:

  • Solvent-mediated Browning led to time-dependent chromophore formation and color intensification, plateauing at 48 hours.
  • Structural analysis revealed partial dimerization, disulfide bond disruption, loss of alpha-helical content, and rearrangement of beta-sheet structures.
  • Protein architecture loosened, with decreased surface hydrophobicity and altered fluorescence.
  • SEM showed increased fibrillar content.
  • Browned lysozyme exhibited enhanced antioxidant activity but reduced antibacterial efficacy.
  • Cytotoxicity remained negligible.

Conclusions:

  • Solvent-mediated Browning is an effective strategy for structurally reprogramming lysozyme.
  • This modification alters lysozyme's functional properties, enhancing antioxidant capacity and reducing antibacterial activity.
  • The method holds potential for expanding the functional versatility of proteins in food, biomedical, and pharmaceutical sectors.