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  • Title: The effect of thermal processing on the IgE reactivity of the non-specific lipid transfer protein from apple, Mal d 3.
    Author: Sancho AI, Rigby NM, Zuidmeer L, Asero R, Mistrello G, Amato S, González-Mancebo E, Fernández-Rivas M, van Ree R, Mills EN.
    Journal: Allergy; 2005 Oct; 60(10):1262-8. PubMed ID: 16134992.
    Abstract:
    BACKGROUND: Non-specific lipid transfer proteins (LTPs) are involved in allergy to fresh and processed fruits. We have investigated the effect of thermal treatment and glycation on the physico-chemical and IgE-binding properties of the LTP from apple (Mal d 3). METHODS: Mal d 3 was purified from apple peel and the effect of heating in the absence and presence of glucose investigated by CD spectroscopy, electrospray and MALDI-TOF mass spectrometry. IgE reactivity was determined by RAST and immunoblot inhibition, SPT and basophil histamine release test. RESULTS: The identity and IgE reactivity of purified Mal d 3 was confirmed. Mild heat treatment (90 degrees C, 20 min) in the absence or presence of glucose did not alter its IgE reactivity. More severe heat treatment (100 degrees C, 2 h) induced minor changes in protein structure, but a significant decrease in IgE-binding (30-fold) and biological activity (100- to 1000-fold). Addition of glucose resulted in up to four glucose residues attached to Mal d 3 and only a 2- and 10-fold decrease of IgE-binding and biological activity, respectively. CONCLUSIONS: Only severe heat treatment caused a significant decrease in the allergenicity of Mal d 3 but glycation had a protective effect. The presence of sugars in fruits may contribute to the thermostability of the allergenic activity of LTP in heat-processed foods.
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