TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1275
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5261
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
VL  - 92
IS  - 7
SP  - 1432
EP  - 1440
DO  - 10.1002/jsfa.4722
ER  - 

@article{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
volume = "92",
number = "7",
pages = "1432-1440",
doi = "10.1002/jsfa.4722"
}

Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722

Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440.
doi:10.1002/jsfa.4722 .

Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" in Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 . .

TY  - 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 . .