An optimized fractionation method in the pilot scale for production of isolated α-lactalbumin (α-La) and βlactoglobulin (β-Lg) was developed. The method comprises following steps: (1) selective thermal precipitation of α-La, (2) aging of the formed particles, (3) separation of native β-Lg from the precipitate via microfiltration and ultrafiltration, (4) purification of β-Lg, (5) resolubilization of the precipitate, and (6) purification of α-La. The native status of the isolated fractions was confirmed by reversed-phase high-performance liquid chromatography (RP-HPLC), sodium dodecyl sulfate– polyacrylamide gel electrophoresis (SDS-PAGE), and differential scanning calorimetry (DSC). Protein fractions with a purity of 91.3% for α-La and 97.2% for β-Lg were produced. These valueswere based on the native protein detectable in RP-HPLC.High overall yields forα-La between 60.7%and 80.4% and for β-Lg between 80.2% and 97.3%, depending on membrane operation parameters, were achieved. The method offers potential for pilot plant scale and possibly industrial application to produce pure native fractions of α-La and/or β-Lg.      «

An optimized fractionation method in the pilot scale for production of isolated α-lactalbumin (α-La) and βlactoglobulin (β-Lg) was developed. The method comprises following steps: (1) selective thermal precipitation of α-La, (2) aging of the formed particles, (3) separation of native β-Lg from the precipitate via microfiltration and ultrafiltration, (4) purification of β-Lg, (5) resolubilization of the precipitate, and (6) purification of α-La. The native status of the isolated fractions was con...     »