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Structural changes and allergenic properties of β‐lactoglobulin upon exposure to high‐intensity ultrasound
Author(s) -
StanicVucinic Dragana,
Stojadinovic Marija,
AtanaskovicMarkovic Marina,
Ognjenovic Jana,
Grönlund Hans,
van Hage Marianne,
Lantto Raija,
Sancho Ana I.,
Velickovic Tanja Cirkovic
Publication year - 2012
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.201200179
Subject(s) - sonication , chemistry , beta lactoglobulin , circular dichroism , allergen , protein secondary structure , basophil activation , whey protein , food science , biochemistry , biophysics , chromatography , allergy , basophil , immunology , antibody , biology , immunoglobulin e
Scope The aim of this work was to investigate the effects of high‐intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta‐lactoglobulin ( BLG ). Methods and results Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan emission fluorescence, hydrophobic dye and retinol binding, as well as digestibility and phenol‐oxidase cross‐linking capacity. Allergenicity was monitored in individual patients’ sera, basophil activation test, and skin prick testing in 41 cow's milk allergy patients. Uncontrolled local temperature changes induced modifications in BLG secondary structure accompanied by formation of dimers, trimers, and oligomers of BLG that were more digestible by pepsin and had reduced retinol binding. Controlled temperature conditions induced changes in secondary structure of BLG without causing formation of oligomers, or changing protein's capacity to bind retinol. Both sonicated forms of BLG had more exposed hydrophobic surfaces than native BLG and underwent facilitated cross‐linking reaction with phenol‐oxidase. Sonication had a minor effect on I g E ‐binding properties of BLG . Conclusion Sonication‐induced structural changes in major whey allergen were not clinically significant in cow's milk allergy patients. Ultrasound can be a safe procedure for dairy processing as it maintains the nutritional value and does not increase allergenic potential of BLG .

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