Structural changes and allergenic properties of ß-lactoglobulin upon exposure to high-intensity ultrasound

D. Stanic-Vucinic, M. Stojadinovic, M. Atanaskovic-Markovic, J. Ognjenovic, H. Grönlund, M. van Hage, Raija Lantto, A.I. Sancho, T.C. Velickovic (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

50 Citations (Scopus)

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). 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. 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.
Original languageEnglish
Pages (from-to)1894-1905
Number of pages11
JournalMolecular Nutrition and Food Research
Volume56
Issue number12
DOIs
Publication statusPublished - 2012
MoE publication typeA1 Journal article-refereed

Keywords

  • Beta-lactoglobulin
  • cow's milk allergy
  • food allergy
  • food processing
  • ultrasound

Fingerprint Dive into the research topics of 'Structural changes and allergenic properties of ß-lactoglobulin upon exposure to high-intensity ultrasound'. Together they form a unique fingerprint.

  • Cite this

    Stanic-Vucinic, D., Stojadinovic, M., Atanaskovic-Markovic, M., Ognjenovic, J., Grönlund, H., van Hage, M., Lantto, R., Sancho, A. I., & Velickovic, T. C. (2012). Structural changes and allergenic properties of ß-lactoglobulin upon exposure to high-intensity ultrasound. Molecular Nutrition and Food Research, 56(12), 1894-1905. https://doi.org/10.1002/mnfr.201200179