Pressure-temperature stability, Ca2+ binding, and pressure-temperature phase diagram of cod parvalbumin: Gad m 1

Judit Somkuti, Merima Bublin, Heimo Breiteneder, L. Smeller

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Fish allergy is associated with IgE-mediated hypersensitivity reactions to parvalbumins, which are small calcium-binding muscle proteins and represent the major and sole allergens for 95% of fish-allergic patients. We performed Fourier transform infrared and tryptophan fluorescence spectroscopy to explore the pressure-temperature (p-T) phase diagram of cod parvalbumin (Gad m 1) and to elucidate possible new ways of pressure-temperature inactivation of this food allergen. Besides the secondary structure of the protein, the Ca2+ binding to aspartic and glutamic acid residues was detected. The phase diagram was found to be quite complex, containing partially unfolded and molten globule states. The Ca2+ ions were essential for the formation of the native structure. A molten globule conformation appears at 50 °C and atmospheric pressure, which converts into an unordered aggregated state at 75 °C. At >200 MPa, only heat unfolding, but no aggregation, was observed. A pressure of 500 MPa leads to a partially unfolded state at 27 °C. The complete pressure unfolding could only be reached at an elevated temperature (40 °C) and pressure (1.14 GPa). A strong correlation was found between Ca2+ binding and the protein conformation. The partially unfolded state was reversibly refolded. The completely unfolded molecule, however, from which Ca2+ was released, could not refold. The heat-unfolded protein was trapped either in the aggregated state or in the molten globule state without aggregation at elevated pressures. The heat-treated and the combined heat- and pressure-treated protein samples were tested with sera of allergic patients, but no change in allergenicity was found.

Original languageEnglish
Pages (from-to)5903-5911
Number of pages9
JournalBiochemistry
Volume51
Issue number30
DOIs
Publication statusPublished - Jul 31 2012

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Gadiformes
Parvalbumins
Phase diagrams
Pressure
Temperature
Hot Temperature
Molten materials
Allergens
Fish
Conformations
Fishes
Agglomeration
Allergies
Immediate Hypersensitivity
Protein Unfolding
Protein Conformation
Proteins
Atmospheric Pressure
Calcium-Binding Proteins
Muscle Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Pressure-temperature stability, Ca2+ binding, and pressure-temperature phase diagram of cod parvalbumin : Gad m 1. / Somkuti, Judit; Bublin, Merima; Breiteneder, Heimo; Smeller, L.

In: Biochemistry, Vol. 51, No. 30, 31.07.2012, p. 5903-5911.

Research output: Contribution to journalArticle

Somkuti, Judit ; Bublin, Merima ; Breiteneder, Heimo ; Smeller, L. / Pressure-temperature stability, Ca2+ binding, and pressure-temperature phase diagram of cod parvalbumin : Gad m 1. In: Biochemistry. 2012 ; Vol. 51, No. 30. pp. 5903-5911.
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