A large-scale isolation of native β-lactoglobulin: characterization of physicochemical properties and comparison with other methods

An improved method for isolation of β-lactoglobulin

“…Changes in native structure affect functional properties, so there has been a renewed interest in developing efficient separation and purification processes that do not cause denaturation and loss of their biological activity (Konrad, Lieske, & Faber, 2000;Neyestani, Djalali, & Pezeshki, 2003;Ye, Yoshida, & Ng, 2000).…”

“…Among the methods frequently used to separate it from whey are precipitation at low pH (Konrad et al, 2000), peptic hydrolysis followed by selective membrane filtration (Konrad et al, 2000), gel filtration chromatography (Neyestani et al, 2003), other chromatographic methods (Schlatterer, Baeker, & Schlatterer, 2004;Ye et al, 2000), salting out and selective solubility (Neyestani et al, 2003). However, some of these methods induce b-lactoglobulin denaturation or produce low yields with other proteins or salts as contaminants, making them useless in some cases and expensive and time consuming in others.…”

Effect of pectin adsorption on the hydrophobic binding sites of β-lactoglobulin in solution and in emulsion systems

“…Materials bLG was isolated and purified (!98% purity) from skim milk using a salting-out method with ammonium sulphate (Konrad, Lieske, & Faber, 2000). Citrus pectin (CM-203, degree of esterification !…”

Trends in whey protein fractionation

“…Afterwards, IgG was concentrated in whey by selectively removing ALA, BLG and BSA using the same anionexchanger at pH 7.0 followed by a 100 kDa Amicon YM membrane. Konrad et al (2000) isolated BLG from whey through a peptic treatment of whey and membrane UF. BLG was produced with a recovery of 67% and a purity of 94%.…”