ArticleEuropean biophysics journal : EBJ2011
Pressure and temperature stability of the main apple allergen Mal d1.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Biomolecules under Pressure: Phase Diagrams, Volume Changes, and High Pressure Spectroscopic Techniques.International journal of molecular sciences · 2022Review
- Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.Scientific reports · 2021Article
- Article
- Tiered approach for the identification of Mal d 1 reduced, well tolerated apple genotypes.Scientific reports · 2020Article
- Structure of the Major Apple Allergen Mal d 1.Journal of agricultural and food chemistry · 2017Article
- NMR resonance assignments of the major apple allergen Mal d 1.Biomolecular NMR assignments · 2016Article
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Authors and funding
3 authors.
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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.
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