Purification of bovine α-lactalbumin by immobilized metal ion affinity chromatography

A. L. Blomkalns, M. R. Gomez

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The milk protein α-lactalbumin was isolated from bovine whey protein concentrate solution by immobilized metal ion affinity chromatography (IMAC) using Cu(II)-Chelating Sepharose Fast Flow. Stepwise pH (5.5-3.8) changes in sodium acetate buffer were used to elute the protein selectively, at which time it was concentrated and reapplied to an uncharged Chelating Sepharose Fast Flow column to remove the contaminating Cu(II) ions. A purity of 90% and recovery of 80% was achieved. The described method appears to be suitable for isolation of α-lactalbumin in a form adequate for milk formula engineering.

Original languageEnglish (US)
Pages (from-to)219-226
Number of pages8
JournalPreparative Biochemistry and Biotechnology
Volume27
Issue number4
DOIs
StatePublished - Jan 1 1997

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry

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