Academic Journal

One-step method for isolation and purification of native beta-lactoglobulin from bovine whey

Bibliographic Details
Title: One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
Authors: Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana
Superior Title: Journal of the Science of Food and Agriculture
Publisher Information: Wiley-Blackwell, Malden
Publication Year: 2012
Collection: CHERRY - CHEMistry RepositorY, Faculty of Chemistry, University of Belgrade / Repozitorijum Hemijskog fakulteta - Cherry (Univerzitet u Beogradu - Hemijski fakultet)
Subject Terms: native ss-lactoglobulin, isolation, anion exchange chromatography, purification
Description: 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 ; 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]. ; Published version: [https://cherry.chem.bg.ac.rs/handle/123456789/1275]
Document Type: article in journal/newspaper
Language: unknown
ISSN: 0022-5142
Relation: info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//; info:eu-repo/grantAgreement/EC/FP7/256716/EU//; https://cherry.chem.bg.ac.rs/handle/123456789/1275; https://doi.org/10.1002/jsfa.4722; http://cherry.chem.bg.ac.rs/handle/123456789/5261; 000302468200015; 2-s2.0-84859419583; http://cherry.chem.bg.ac.rs/bitstream/id/30278/One-step_method_acc_2012.pdf
DOI: 10.1002/jsfa.4722
Availability: https://doi.org/10.1002/jsfa.4722
https://cherry.chem.bg.ac.rs/handle/123456789/1275
http://cherry.chem.bg.ac.rs/handle/123456789/5261
http://cherry.chem.bg.ac.rs/bitstream/id/30278/One-step_method_acc_2012.pdf
Rights: embargoedAccess ; https://creativecommons.org/licenses/by-nc-nd/4.0/ ; BY-NC-ND
Accession Number: edsbas.585BFC9E
Database: BASE
Description
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