Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound
Само за регистроване кориснике
2012
Аутори
Stanić-Vučinić, DraganaStojadinović, Marija M.
Atanasković-Marković, Marina
Ognjenović, Jana
Gronlund, Hans
van Hage, Marianne
Lantto, Raija
Sancho, Ana I.
Ćirković-Veličković, Tanja
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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.
Кључне речи:
Beta-lactoglobulin / Cow's milk allergy / Food allergy / Food processing / UltrasoundИзвор:
Molecular Nutrition and Food Research, 2012, 56, 12, 1894-1905Издавач:
- Wiley-Blackwell, Hoboken
Финансирање / пројекти:
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-MESTD-Basic Research (BR or ON)-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
- UK Biological and Biotechnological Sciences Research Council
- Swedish Research Council
- Stockholm County Council
- COST Actions [928, FA1005]
DOI: 10.1002/mnfr.201200179
ISSN: 1613-4125
PubMed: 23065770
WoS: 000312132300015
Scopus: 2-s2.0-84870691231
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Stanić-Vučinić, Dragana AU - Stojadinović, Marija M. AU - Atanasković-Marković, Marina AU - Ognjenović, Jana AU - Gronlund, Hans AU - van Hage, Marianne AU - Lantto, Raija AU - Sancho, Ana I. AU - Ćirković-Veličković, Tanja PY - 2012 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1561 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. PB - Wiley-Blackwell, Hoboken T2 - Molecular Nutrition and Food Research T1 - Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound VL - 56 IS - 12 SP - 1894 EP - 1905 DO - 10.1002/mnfr.201200179 ER -
@article{ author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Atanasković-Marković, Marina and Ognjenović, Jana and Gronlund, Hans and van Hage, Marianne and Lantto, Raija and Sancho, Ana I. and Ćirković-Veličković, Tanja", 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). 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.", publisher = "Wiley-Blackwell, Hoboken", journal = "Molecular Nutrition and Food Research", title = "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound", volume = "56", number = "12", pages = "1894-1905", doi = "10.1002/mnfr.201200179" }
Stanić-Vučinić, D., Stojadinović, M. M., Atanasković-Marković, M., Ognjenović, J., Gronlund, H., van Hage, M., Lantto, R., Sancho, A. I.,& Ćirković-Veličković, T.. (2012). Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound. in Molecular Nutrition and Food Research Wiley-Blackwell, Hoboken., 56(12), 1894-1905. https://doi.org/10.1002/mnfr.201200179
Stanić-Vučinić D, Stojadinović MM, Atanasković-Marković M, Ognjenović J, Gronlund H, van Hage M, Lantto R, Sancho AI, Ćirković-Veličković T. Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound. in Molecular Nutrition and Food Research. 2012;56(12):1894-1905. doi:10.1002/mnfr.201200179 .
Stanić-Vučinić, Dragana, Stojadinović, Marija M., Atanasković-Marković, Marina, Ognjenović, Jana, Gronlund, Hans, van Hage, Marianne, Lantto, Raija, Sancho, Ana I., Ćirković-Veličković, Tanja, "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound" in Molecular Nutrition and Food Research, 56, no. 12 (2012):1894-1905, https://doi.org/10.1002/mnfr.201200179 . .