@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",
pages = "1440-1432",
number = "7",
volume = "92",
doi = "10.1002/jsfa.4722"
}