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

A. L. Blomkalns; M. R. Gomez

doi:10.1080/10826069708001280

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

A. L. Blomkalns, M. R. Gomez

Research output: Contribution to journal › Article › peer-review

16 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 language	English (US)
Pages (from-to)	219-226
Number of pages	8
Journal	Preparative Biochemistry and Biotechnology
Volume	27
Issue number	4
DOIs	https://doi.org/10.1080/10826069708001280
State	Published - 1997

ASJC Scopus subject areas

Biotechnology
Biochemistry

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10.1080/10826069708001280

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title = "Purification of bovine α-lactalbumin by immobilized metal ion affinity chromatography",

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.",

author = "Blomkalns, {A. L.} and Gomez, {M. R.}",

note = "Funding Information: This project has been funded, in part, with federal funds from the U.S. Department of Agriculture, Agricultural Research Service under Cooperative Agreement 58-7MOZ-1-001. The contents of this publication do not necessarily reflect the view of the U.S. Department of Agriculture, nor does the mention of trade names, products or organizations imply endorsement by the U.S. Government . The authors thank Dr. Charles V. Smith for his kind assistance in the preparation of this manuscript.",

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doi = "10.1080/10826069708001280",

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AU - Blomkalns, A. L.

AU - Gomez, M. R.

N1 - Funding Information: This project has been funded, in part, with federal funds from the U.S. Department of Agriculture, Agricultural Research Service under Cooperative Agreement 58-7MOZ-1-001. The contents of this publication do not necessarily reflect the view of the U.S. Department of Agriculture, nor does the mention of trade names, products or organizations imply endorsement by the U.S. Government . The authors thank Dr. Charles V. Smith for his kind assistance in the preparation of this manuscript.

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

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

Abstract

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