Bovine lactoferrin purification from whey using Yellow HE-4R as the chromatographic affinity ligand

J Sep Sci. 2014 Mar;37(5):484-7. doi: 10.1002/jssc.201301086. Epub 2014 Jan 21.

Abstract

The worldwide production of whey increases by around 186 million tons each year and it is generally considered as a waste, even when several whey proteins have important economic relevance. For its valorization, inexpensive ligands and integrated chromatography methods need to be developed for specific and low-cost protein purification. Here, we describe a novel affinity process with the dye Yellow HE-4R immobilized on Sepharose for bovine lactoferrin purification. This approach based on a low-cost ligand showed an efficient performance for the recovery and purification of bovine lactoferrin directly from whey, with a yield of 71% and a purification factor of 61.

Keywords: Bovine lactoferrin; Dye affinity chromatography; Sweet whey; Triazine dyes.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Chromatography, Affinity / instrumentation
  • Chromatography, Affinity / methods*
  • Coloring Agents / chemistry
  • Lactoferrin / chemistry
  • Lactoferrin / isolation & purification*
  • Ligands
  • Milk Proteins / chemistry
  • Milk Proteins / isolation & purification*
  • Whey Proteins

Substances

  • Coloring Agents
  • Ligands
  • Milk Proteins
  • Whey Proteins
  • Lactoferrin