Pressure and temperature stability of the main apple allergen Mal d1.
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.
Department of Biophysics and Radiation Biology, Semmelweis University, Tuzolto u. 37-47, PF 263, 1444 Budapest, Hungary.
Judit
J
Somkuti
Milan
M
Houska
László
L
Smeller
D000485:Allergens / Q000737:chemistry*; D027845:Malus / Q000737:chemistry* / Q000276:immunology; D009994:Osmolar Concentration; D011312:Pressure; D017433:Protein Structure, Secondary; D058767:Protein Unfolding; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D013696:Temperature
D000485:Allergens