Isolation of lactoperoxidase, lactoferrin, alpha-lactalbumin, beta-lactoglobulin B and beta-lactoglobulin A from bovine rennet whey using ion exchange chromatography

Citation
Xy. Ye et al., Isolation of lactoperoxidase, lactoferrin, alpha-lactalbumin, beta-lactoglobulin B and beta-lactoglobulin A from bovine rennet whey using ion exchange chromatography, INT J BIO C, 32(11-12), 2000, pp. 1143-1150
Citations number
15
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
ISSN journal
1357-2725 → ACNP
Volume
32
Issue
11-12
Year of publication
2000
Pages
1143 - 1150
Database
ISI
SICI code
1357-2725(200011/12)32:11-12<1143:IOLLAB>2.0.ZU;2-
Abstract
A mild and rapid method is described for isolating various milk proteins fr om bovine rennet whey. beta -Lactoglobulin from bovine rennet whey was easi ly adsorbed on and desorbed from a weak anion exchanger, diethylaminoethyl- Toyopearl. However, alpha -lactalbumin could not be adsorbed onto the resin . alpha -Lactalbumin and beta -lactoglobulin from rennet whey could also be adsorbed and separated using a strong anion exchanger, quaternary aminoeth yl-Toyopearl. The rennet whey was passed through a strong cation exchanger, sulphopropyl-Toyopearl, to separate lactoperoxidase and lactoferrin, alpha -lactalbumin and beta -lactoglobulin were adsorbed onto quaternary aminoet hyl-Toyopearl. alpha -lactalbumin was eluted using a linear (0-0.15 M) conc entration gradient of NaCl in 0.05 M Tris-HCl buffer (pH 8.5). Subsequently , beta -lactoglobulin B and beta -lactoglobulin A were eluted from the colu mn with 0.05 M Tris-HCl (pH 6.8), using a linear (0.1-0.25 M) concentration gradient of NaCl. The yields were 1260 mg alpha -lactalbumin, 1290 mg beta -lactoglobulin B and 2280 mg beta -lactoglobulin A from 1 1 rennet whey. ( C) 2000 Elsevier Science Ltd. All rights reserved.