| Literature DB >> 9652116 |
Abstract
A preparative-scale ion-exchange chromatographic process is described for the separation of the four major proteins and lactose from sweet dairy whey. Experiments using a commercial anion-exchange resin were carried out to determine the optimum conditions for initially separating the proteins alpha-lactalbumin, beta-lactoglobulin, bovine serum albumin, immunoglobulin G and lactose from a sweet dairy whey mixture. The separation was accomplished with simultaneous step elution changes in salt concentration and pH. It was found that the anion-exchange step was most effective in separating beta-lactoglobulin from the feed mixture. Following the anion-exchange separation, its breakthrough curve was processed using a commercial cation-exchange resin to further recover the valuable immunoglobulin G. The whey output from an east Tennessee cheese manufacturer was used as a feedstream for the preparative scale experiments and as a reference in scaling to an economically optimized production level operation.Entities:
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Year: 1998 PMID: 9652116 DOI: 10.1016/s0021-9673(98)00103-4
Source DB: PubMed Journal: J Chromatogr A ISSN: 0021-9673 Impact factor: 4.759