Isolation of Bovine Immunoglobulins and Lactoferrin from Whey Proteins by Gel Filtration Techniques

Abstract

Whey is a suitable source of immunoglobulins and lactoferrin to enrich infant formulas. Gel filtration on Sephacryl S-300 and on Fractogel TSK HW-55 was used to isolate immunoglobulins from colostral whey, acid whey, and Cheddar cheese whey. The SDS-PAGE and immunoelectrophoresis techniques indicated that the purity of the fractions from fractionation on Sephacryl S-300 was better than that by fractionation on TSK HW-55 column. Biological activity of fractions from the Sephacryl S-300 column as assessed by immunochemical analysis was 99, 83.3, and 92% for colostral, acid, and sweet wheys. The well-proven antimicrobial agent, lactoferrin, was isolated from sweet whey by heparin-attached Sepharose. Lactoferrin selectively adsorbed to the column was subsequently eluted with 5 mM Veronal-HCl containing .5 M NaCl, pH 7.4. Purity of the isolated protein was confirmed by SDS-PAGE and immunoelectrophoresis.

Detection of the hepatotoxic microcystins in 36 kinds of cyanobacteriaSpirulinafood products in China

“…The stationary phase for gel filtration has a fractionation range, meaning that molecules within that molecular weight range can be separated. Gel filtration chromatography is relatively amenable to protein molecules and has frequently been used in protein separation (Al-Mashikhi and Nakai 1987;Yoshida 1990;Fee 2003;Roufik et al 2005). Meanwhile, ultra-filtration is a pressure-driven membrane separation process that is increasingly being used in water and wastewater treatment processes, and in the pharmaceutical and liquid food industries.…”

Simultaneous Isolation of Lactoferrin and Lactoperoxidase from Bovine Colostrum by SPEC 70 SLS Cation Exchange Resin

“…The literature regarding the isolation and purification of the Lf during the last two decades is extensive. Reported methods have included microfiltration, gel filtration chromatography, traditional cation exchange chromatography, heparin-agarose affinity chromatography and membrane filtration [5–9]. Despite the increasing number of separation methods that were developed, most of the Lf was obtained from bovine colostrum due to its high content of Lf.…”

Isolation and purification of lactoferrin and immunoglobulin G from bovine colostrum with serial cation-anion exchange chromatography

“…Chromatography is another technology widely used in isolation of high purity LF and IgG. Some examples of chromatographic separation are ion-exchange chromatography [3,4], hydrophobic interaction chromatography [5,6], adsorption chromatography [7,8], gel permeation chromatography [9], affinity chromatography [10,11] and immunoaffinity chromatography [12,13]. Compared with the other chromatographic methods, ion-exchanger chromatography has the advantages of low cost, reduced steps, continuous feed-in, and easy to scale-up.…”