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dc.creatorStojadinović, Marija M.
dc.creatorBurazer, Lidija M.
dc.creatorErcili-Cura, Dilek
dc.creatorSancho, Ana
dc.creatorBuchert, Johanna
dc.creatorĆirković-Veličković, Tanja
dc.creatorStanić-Vučinić, Dragana
dc.date.accessioned2022-06-02T09:11:33Z
dc.date.available2012-11-14
dc.date.issued2012
dc.identifier.issn0022-5142
dc.identifier.urihttps://cherry.chem.bg.ac.rs/handle/123456789/1275
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/5261
dc.description.abstractBACKGROUND: 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 Industryen
dc.publisherWiley-Blackwell, Malden
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.relation.isversionofhttps://cherry.chem.bg.ac.rs/handle/123456789/1275
dc.relation.isversionofhttps://doi.org/10.1002/jsfa.4722
dc.rightsembargoedAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceJournal of the Science of Food and Agriculture
dc.subjectnative ss-lactoglobulinen
dc.subjectisolationen
dc.subjectanion exchange chromatographyen
dc.subjectpurificationen
dc.titleOne-step method for isolation and purification of native beta-lactoglobulin from bovine wheyen
dc.typearticle
dc.rights.licenseBY-NC-ND
dc.citation.volume92
dc.citation.issue7
dc.citation.spage1432
dc.citation.epage1440
dc.identifier.wos000302468200015
dc.identifier.doi10.1002/jsfa.4722
dc.citation.other92(7): 1432-1440
dc.citation.rankM21
dc.identifier.pmid22083849
dc.description.otherThis is the peer-reviewed version of the article: (1) Stojadinović, M. M.; Burazer, L. M.; 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. Journal of the Science of Food and Agriculture 2012, 92 (7), 1432–1440. [https://doi.org/10.1002/jsfa.4722].
dc.description.otherPublished version: [https://cherry.chem.bg.ac.rs/handle/123456789/1275]
dc.type.versionacceptedVersionen
dc.identifier.scopus2-s2.0-84859419583
dc.identifier.fulltexthttp://cherry.chem.bg.ac.rs/bitstream/id/30278/One-step_method_acc_2012.pdf


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