Back to Search
Start Over
Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound.
- Source :
-
Molecular nutrition & food research [Mol Nutr Food Res] 2012 Dec; Vol. 56 (12), pp. 1894-905. Date of Electronic Publication: 2012 Oct 15. - Publication Year :
- 2012
-
Abstract
- 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).<br />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 IgE-binding properties of BLG.<br />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.<br /> (© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Subjects :
- Allergens chemistry
Allergens immunology
Anilino Naphthalenesulfonates
Animals
Basophils immunology
Child
Child, Preschool
Chromatography, Gel
Circular Dichroism
Cross-Linking Reagents
Enzyme-Linked Immunosorbent Assay methods
Female
Humans
Immunoglobulin E blood
Immunoglobulin E immunology
Infant
Male
Milk chemistry
Milk Hypersensitivity diagnosis
Monophenol Monooxygenase metabolism
Pepsin A metabolism
Protein Binding
Protein Structure, Secondary
Skin Tests
Sonication methods
Temperature
Lactoglobulins chemistry
Lactoglobulins immunology
Lactoglobulins radiation effects
Milk Hypersensitivity immunology
Subjects
Details
- Language :
- English
- ISSN :
- 1613-4133
- Volume :
- 56
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Molecular nutrition & food research
- Publication Type :
- Academic Journal
- Accession number :
- 23065770
- Full Text :
- https://doi.org/10.1002/mnfr.201200179