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Aroma compounds-proteins interaction using headspace techniques.

E Jouenne1, J Crouzet

  • 1Laboratoire de Genie Biologique et Sciences des Aliments, Equipe de Microbiologie et Biochimie Industrielles associée a l'INRA, Université de Montpellier II, France.

Advances in Experimental Medicine and Biology
|September 8, 2001
PubMed
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Beta-lactoglobulin retains many volatile aroma compounds in aqueous solutions, with retention varying by compound type and hydrophobicity. Protein structural changes with pH significantly influence these volatile compound interactions.

Area of Science:

  • Food Chemistry
  • Protein Chemistry
  • Analytical Chemistry

Background:

  • Volatile compounds significantly impact food flavor and aroma.
  • Protein-food matrix interactions influence the stability and release of volatile compounds.
  • Beta-lactoglobulin is a major whey protein with known binding capabilities.

Purpose of the Study:

  • To investigate the interactions between volatile compounds and beta-lactoglobulin in aqueous solutions.
  • To quantify the retention of various volatile compounds by beta-lactoglobulin.
  • To explore the influence of pH and compound hydrophobicity on these interactions.

Main Methods:

  • Static and dynamic headspace techniques were employed to study volatile compound retention.
  • Infinite dilution activity coefficients (gamma i) were determined using exponential dilution.

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  • Interactions were assessed across a pH range of 2.0 to 11.0.

    • Main Results:

    • Beta-lactoglobulin demonstrated significant retention (8-60%) for most tested volatile compounds.
    • Retention intensity correlated with the hydrophobicity of methyl ketones and ethyl esters.
    • Limonene and myrcene showed increased relative activity coefficients with beta-lactoglobulin, unlike with other proteins.
    • pH-dependent variations in relative activity coefficients suggest protein structural influence.

    Conclusions:

    • Beta-lactoglobulin exhibits selective binding of volatile compounds, influenced by their chemical nature and hydrophobicity.
    • The protein's structural conformation, modulated by pH, plays a crucial role in volatile compound interactions.
    • These findings contribute to understanding flavor release and stability in protein-rich food systems.