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Conformational changes in ovalbumin at acid pH.

T Koseki1, N Kitabatake, E Doi

  • 1Research Institute for Food Science, Kyoto University.

Journal of Biochemistry
|March 1, 1988
PubMed
Summary
This summary is machine-generated.

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Ovalbumin retains its globular structure at low pH but becomes more flexible and prone to denaturation. This acidic state may resemble the molten-globule state seen in other proteins.

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Physical Chemistry

Background:

  • Ovalbumin, a major protein in egg white, is known to undergo conformational changes under varying pH conditions.
  • Understanding these changes is crucial for food processing and protein stability studies.

Purpose of the Study:

  • To investigate the physicochemical properties of ovalbumin at acidic pH.
  • To determine if ovalbumin adopts a molten-globule state in acidic conditions.

Main Methods:

  • Circular Dichroism (CD) spectroscopy (near and far UV) to assess secondary and tertiary structure.
  • Difference absorption spectroscopy to detect changes in aromatic amino acid environments.
  • Fluorescence spectroscopy to probe micro-environmental changes.
  • Measurement of intrinsic viscosity and sulfhydryl group reactivity.

Related Experiment Videos

  • Assessing denaturation rates using urea and surface tension decay.

    • Main Results:

    • Intrinsic viscosity and far UV-CD spectra remained unchanged at pH 2 compared to pH 7, indicating preserved globular conformation.
    • Near UV-CD, difference absorption, and fluorescence spectra revealed alterations in the microenvironment of aromatic residues at acidic pH.
    • Sulfhydryl group reactivity increased below pH 5.
    • Denaturation by urea and surface tension decay rates were elevated in the low pH range.

    Conclusions:

    • Ovalbumin maintains its native globular conformation at pH ~2.
    • Acidic conditions increase chain flexibility and susceptibility to denaturation.
    • The observed state at low pH is potentially analogous to the molten-globule state.