Abstract: The present invention relates to new processes useful for separating whey proteins from whey protein-containing solutions using a novel anion exchanger which comprises a water insoluble, hydrophilic, water swellable, hydroxy (C2–C4) alkylated and cross-linked regenerated cellulose, derivatized with quaternary amino (QA) groups where the level of substitution of the QA groups is 1.4 milli-equivalents per dry gram of anion exchanger (meq/g) or greater.

Abstract: The present invention is related to a new quaternary amino (QA) anion exchanger comprising QA derivatized, hydroxy (C2-C4) alkylated and cross-linked regenerated cellulose, in which the level of derivitization with the QA-groups is 1.4 milli-equivalents per dry gram (meq/g) or greater.

Abstract: This invention is directed to a process for producing an immunoglobulin enriched whey protein fraction from whey protein solutions. More particularly, it relates to the production of a whey protein fraction enriched in immunoglobulin, and optionally a whey protein isolate, using a cation exchanger under selected conditions. The selected conditions require overloading the cation exchanger with potentially absorbable protein which causes the exchanger to adsorb preferentially whey proteins other than immunoglobulin. The invention is also directed to the products produced by the process of the invention.

Abstract: The present invention provides a new quaternary amino (QA) anion exchanger comprising QA derivatised, hydroxy (C2-C4) alkylated and cross-linked regenerated cellulose, in which the level of derivatisation with the QA-groups is 1.4 meg/g or greater.

Abstract: The present invention provides new processes useful for separating whey proteins from whey protein-containing solutions using a novel anion exchanger which comprises a water insoluble, hydrophilic, water swellable, hydroxy (C2-C4) alkylated and cross-linked regenerated cellulose, derivatised with quaternary amino (QA) groups, wherein the level of substitution of the QA groups is 1.4 milli-equivalents per dry gram of anion exchanger (meq/g) or greater.

Abstract: The present invention is related to a method for the purification of glycomacropeptide (GMP) with an amino acid composition containing no greater that 0.5% (w/w) phenylalanine, comprising the steps of contacting a GMP-containing feedstock with a first anion exchanger under conditions to adsorb the GMP, eluting the adsorbed GMP from the anion exchanger and removing impurities from the GMP-containing eluate by either: (i) contacting the GMP-containing eluate with a cation exchanger in conditions under which the impurities in the eluate are adsorbed onto the cation exchanger, or (ii) precipitating the impurities in GMP-containing eluate using conditions in which the GMP remains i solution, or (iii) contacting the GMP-containing eluate with a second anion exchanger in conditions under which the impurities in the eluate are adsorbed onto the anion exchanger, and recovering the GMP from whichever one or more of the steps (i), (ii) or (iii) was used.

Abstract: A preparative method of isolating a preselected whey protein or group of whey proteins from a solution is provided. The method comprises the following steps: (a) contacting a whey protein solution with the preselected ion exchanger for a time and at a temperature sufficient to enable the preselected whey protein to be adsorbed; wherein the whey protein solution has (1) a protein content in the range of about 5% to about 20% by weight, (2) a pH of a preselected level, which is the level at which the preselected whey protein or group of whey proteins selectively binds to the preselected ion exchanger, and (3) a reduced ionic strength; and (b) recovering either or both of the following: (1) the whey protein component adsorbed in step (a), and (2) the breakthrough whey protein component not adsorbed in step (a).

Abstract: The invention relates to the use of a sulphated ion exchanger to selectively remove lipoproteins from blood plasma or serum. Although the attraction between sulphate groups and proteins has long been recognized it has now unexpectedly been found that cationic ion exchangers whose ion exchange capacity is provided by sulphate groups bind lipoproteins selectively in presence of other plasma or serum proteins and ions when they are equilibrated with solutions containing divalent cations and the same cation is added to the plasma or serum. Types of ion exchanger matrices and applications of the utlity are discussed.