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Structure modification and functionality of whey proteins: quantitative structure-activity relationship approach.

S Nakai, E Li-Chan

    Journal of Dairy Science
    |October 1, 1985
    PubMed
    Summary
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    Whey protein functionality, like whipping and gelling, is linked to protein solubility and hydrophobicity. Treatments improved some properties, but angel food cake performance remained unsatisfactory.

    Area of Science:

    • Food Science
    • Protein Chemistry
    • Quantitative Structure-Activity Relationship (QSAR)

    Background:

    • Protein functionality is influenced by electric, hydrophobic, and structural parameters.
    • Protein solubility is a key functional property, often correlated with other functionalities.
    • Hydrophobic parameters, in conjunction with solubility, provide better correlations for protein functionality.

    Purpose of the Study:

    • To investigate the impact of various treatments on whey protein concentrate (WPC) functionality.
    • To achieve whipping and gelling properties comparable to egg white.
    • To explore the relationship between protein parameters and functional properties.

    Main Methods:

    • Whey protein concentrate was subjected to various treatments (e.g., heating, pepsin hydrolysis, polyphosphate treatment).

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  • Mapping simplex optimization was employed to identify optimal treatment conditions.
  • Protein solubility and hydrophobicity were measured and correlated with functional properties.

    • Main Results:

    • Pepsin hydrolysis improved whipping properties, potentially due to increased protein solubility.
    • Polyphosphate treatment enhanced gelling properties, possibly from increased exposable hydrophobicity.
    • Despite improvements, the performance in angel food cake applications remained unsatisfactory.

    Conclusions:

    • Protein solubility and hydrophobicity are critical factors influencing whey protein functionality.
    • Specific treatments can modify these parameters to enhance certain functional properties.
    • Further research is needed to optimize whey proteins for complex applications like baking.