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One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
dc.creator | Stojadinović, Marija M. | |
dc.creator | Burazer, Lidija M. | |
dc.creator | Ercili-Cura, Dilek | |
dc.creator | Sancho, Ana | |
dc.creator | Buchert, Johanna | |
dc.creator | Ćirković-Veličković, Tanja | |
dc.creator | Stanić-Vučinić, Dragana | |
dc.date.accessioned | 2022-06-02T09:11:33Z | |
dc.date.available | 2012-11-14 | |
dc.date.issued | 2012 | |
dc.identifier.issn | 0022-5142 | |
dc.identifier.uri | https://cherry.chem.bg.ac.rs/handle/123456789/1275 | |
dc.identifier.uri | http://cherry.chem.bg.ac.rs/handle/123456789/5261 | |
dc.description.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 | en |
dc.publisher | Wiley-Blackwell, Malden | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS// | |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/256716/EU// | |
dc.relation.isversionof | https://cherry.chem.bg.ac.rs/handle/123456789/1275 | |
dc.relation.isversionof | https://doi.org/10.1002/jsfa.4722 | |
dc.rights | embargoedAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.source | Journal of the Science of Food and Agriculture | |
dc.subject | native ss-lactoglobulin | en |
dc.subject | isolation | en |
dc.subject | anion exchange chromatography | en |
dc.subject | purification | en |
dc.title | One-step method for isolation and purification of native beta-lactoglobulin from bovine whey | en |
dc.type | article | |
dc.rights.license | BY-NC-ND | |
dc.citation.volume | 92 | |
dc.citation.issue | 7 | |
dc.citation.spage | 1432 | |
dc.citation.epage | 1440 | |
dc.identifier.wos | 000302468200015 | |
dc.identifier.doi | 10.1002/jsfa.4722 | |
dc.citation.other | 92(7): 1432-1440 | |
dc.citation.rank | M21 | |
dc.identifier.pmid | 22083849 | |
dc.description.other | This 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.other | Published version: [https://cherry.chem.bg.ac.rs/handle/123456789/1275] | |
dc.type.version | acceptedVersion | en |
dc.identifier.scopus | 2-s2.0-84859419583 | |
dc.identifier.fulltext | http://cherry.chem.bg.ac.rs/bitstream/id/30278/One-step_method_acc_2012.pdf |