Purification of the two major proteins from whey concentrate using a cation‐exchange selective adsorption process

Abstract

The packed-bed adsorption and elution of aqueous solutions of whey concentrate powders were investigated at pH 3.7 using a 5-mL SP Sepharose FF column to separate and isolate two major proteins namely, alpha-lactalbumin (ALA) and beta-lactoglobulin (BLG) from these solutions. ALA displaced and eluted BLG from the column in a pure form. Pure ALA could then be eluted with good recovery. A novel consecutive two-stage separation process was developed to separate ALA and BLG from whey concentrate mixtures. Almost all of the BLG in the feed was recovered, with 78% being recovered at 95% purity and a further 20% at 86% purity. In addition, 67% of ALA was recovered, 48% at 54% purity and 19% at 60% purity.

Toxicity and binding analyses of Bacillus thuringiensis toxin Vip3A in Cry1Ac-resistant and -susceptible strains of Helicoverpa armigera (Hübner)

“…The purified toxin was desalted by dialysis overnight at 4℃ using a desalting column according to the manufacturer's instructions (GE Healthcare). The protoxin was incubated with 2% trypsin (wt/wt) at 37℃ for 1h to get the truncated activated toxin, which was then purified using anion-exchange chromatography (El-Sayed et al 2010).…”

Fractionation of the major whey proteins and isolation of β-Lactoglobulin variants by anion exchange chromatography

“…2 shows a single peak for a-La and BSA, and two peaks for b-Lg, corresponding to its two variants, B and A, respectively. The retention times were changed due the competitive adsorption of the proteins, which is a typical behavior of the proteins in a mixture when fractionated by IEC [39,40]. Aboudzadeh et al [41] reported that, in multicomponent solutions, factors like molecular size and protein interactions can be significant in the adsorption onto ionexchange resins.…”

Optimization of Lactoperoxidase and Lactoferrin Separation on an Ion-Exchange Chromatography Step

“…Whey proteins have been adequately separated into different fractions, the major and minor proteins [4][5][6][7][8]. Isolation and purification of major proteins, e.g., β-lactoglobulin, α-Lactalbumin and serum albumin, through various chromatographic and membrane-separation techniques have been extensively studied [7,9,10].…”

“…Isolation and purification of major proteins, e.g., β-lactoglobulin, α-Lactalbumin and serum albumin, through various chromatographic and membrane-separation techniques have been extensively studied [7,9,10]. However, the efficient purification of high-value minor proteins such as lactoperoxidase (LP) and lactoferrin (LF) still remains a challenge due to their extremely low concentrations.…”