Pressure and temperature stability of the main apple allergen Mal d1

Judit Somkuti, Milan Houska, László Smeller

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

High-pressure Fourier-transform infrared (FTIR) spectroscopy was used to determine the pressure and temperature stability of Mal d1. This study was triggered by contradictory results in the literature regarding the success of pressure treatment in the destruction of the allergen. The protein unfolded at 55 °C when heated at normal atmospheric pressure. We also studied the effect exerted on pressure stability by environmental factors, which can be important for the stability of the protein in the apple. The pressure unfolding was measured under different pD conditions, and the effect of sugar mixture similar to that of the apple and the effect of ionic strength were also studied. In all cases the allergen unfolded with a transition midpoint in the range of 150-250 MPa. Unfolding was irreversible and was followed by aggregation of the unfolded protein. Lowering the pD destabilized the protein, while addition of sugar mixture and of KCl had stabilizing effect.

Original languageEnglish
Pages (from-to)143-151
Number of pages9
JournalEuropean Biophysics Journal
Volume40
Issue number2
DOIs
Publication statusPublished - Feb 1 2011

Keywords

  • Allergen
  • FTIR spectroscopy
  • High pressure
  • Unfolding

ASJC Scopus subject areas

  • Biophysics

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