Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale

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...     »