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Milk whey protein modification by coffee-specific phenolics: effect on structural and functional properties.

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This study modified proteins using phenolics to protect bioactive compounds. The resulting modified proteins show enhanced antioxidant properties and improved stability for food industry applications.

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Area of Science:

  • Food Science
  • Protein Chemistry
  • Biochemistry

Background:

  • Bioactive plant compounds often degrade easily, limiting their use in food.
  • Proteins can act as carriers for these compounds, but require modification for stability.
  • Phenolic compounds offer antioxidant benefits and can interact with proteins.

Purpose of the Study:

  • To develop a method for modifying proteins using phenolics to protect bioactive constituents.
  • To investigate the interactions between β-lactoglobulin and coffee phenolics.
  • To evaluate the functional and structural properties of the modified proteins.

Main Methods:

  • Modification of β-lactoglobulin using coffee phenolics under alkaline and polyphenol oxidase conditions.
  • Analysis of protein-phenolic interactions using tryptic digestion and MALDI-TOF-MS.
  • In silico modeling of modified β-lactoglobulin.
  • Assessment of structural properties, solubility, surface hydrophobicity, and emulsification.

Main Results:

  • Proteins were successfully modified by phenolics, enhancing antioxidative properties.
  • Polyphenol oxidase-mediated modification resulted in higher antioxidative power and thermal stability.
  • Modified proteins exhibited altered structural properties, solubility, hydrophobicity, and emulsification.
  • Emulsified lutein esters with modified protein showed increased UV light stability.

Conclusions:

  • Protein modification with phenolics is an effective strategy for protecting bioactive compounds.
  • Polyphenol oxidase-mediated modification offers superior antioxidative and stability benefits.
  • This approach provides an innovative method for protein functionalization in the food industry.