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

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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

Fingerprint

lactoglobulins
Lactoglobulins
beta-lactoglobulin
Sonication
Vitamin A
milk allergy
Milk Hypersensitivity
vitamin A
allergenicity
Monophenol Monooxygenase
monophenol monooxygenase
allergens
crosslinking
milk
Allergens
circular dichroism spectroscopy
basophils
Temperature
Basophils
binding properties

Keywords

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

Cite this

Stanic-Vucinic, D., Stojadinovic, M., Atanaskovic-Markovic, M., Ognjenovic, J., Grönlund, H., van Hage, M., ... 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
Stanic-Vucinic, D. ; Stojadinovic, M. ; Atanaskovic-Markovic, M. ; Ognjenovic, J. ; Grönlund, H. ; van Hage, M. ; Lantto, Raija ; Sancho, A.I. ; Velickovic, T.C. / Structural changes and allergenic properties of ß-lactoglobulin upon exposure to high-intensity ultrasound. In: Molecular Nutrition and Food Research. 2012 ; Vol. 56, No. 12. pp. 1894-1905.
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author = "D. Stanic-Vucinic and M. Stojadinovic and M. Atanaskovic-Markovic and J. Ognjenovic and H. Gr{\"o}nlund and {van Hage}, M. and Raija Lantto and A.I. Sancho and T.C. Velickovic",
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Stanic-Vucinic, D, Stojadinovic, M, Atanaskovic-Markovic, M, Ognjenovic, J, Grönlund, H, van Hage, M, Lantto, R, Sancho, AI & Velickovic, TC 2012, 'Structural changes and allergenic properties of ß-lactoglobulin upon exposure to high-intensity ultrasound', Molecular Nutrition and Food Research, vol. 56, no. 12, pp. 1894-1905. https://doi.org/10.1002/mnfr.201200179

Structural changes and allergenic properties of ß-lactoglobulin upon exposure to high-intensity ultrasound. / Stanic-Vucinic, D.; Stojadinovic, M.; Atanaskovic-Markovic, M.; Ognjenovic, J.; Grönlund, H.; van Hage, M.; Lantto, Raija; Sancho, A.I.; Velickovic, T.C. (Corresponding Author).

In: Molecular Nutrition and Food Research, Vol. 56, No. 12, 2012, p. 1894-1905.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Structural changes and allergenic properties of ß-lactoglobulin upon exposure to high-intensity ultrasound

AU - Stanic-Vucinic, D.

AU - Stojadinovic, M.

AU - Atanaskovic-Markovic, M.

AU - Ognjenovic, J.

AU - Grönlund, H.

AU - van Hage, M.

AU - Lantto, Raija

AU - Sancho, A.I.

AU - Velickovic, T.C.

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

KW - Beta-lactoglobulin

KW - cow's milk allergy

KW - food allergy

KW - food processing

KW - ultrasound

U2 - 10.1002/mnfr.201200179

DO - 10.1002/mnfr.201200179

M3 - Article

VL - 56

SP - 1894

EP - 1905

JO - Molecular Nutrition and Food Research

JF - Molecular Nutrition and Food Research

SN - 1613-4125

IS - 12

ER -

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