Isolation of recombinant proteins from milk

Tracy D. Wilkins, William Velander

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

Milk is a complex bio‐colloid which presents some unique problems for the protein isolation chemist, but the majority of the processing criteria for purifying recombinant proteins are the same as with any complex biological mixture. The casein micelles and fat globules behave as separate phases; they prevent filtration of the milk and interfere with the usual separation methods. The usual first step is to centrifuge the milk to remove the fat and precipitate the casein micelles with low pH or precipitating agents. Some recombinant proteins may associate to some degree with the micelles which may necessitate solubilizing them with chelating agents. If the majority of the product protein associates with either the fat or micelles, this can be used to advantage. Once the casein micelles have been removed or disrupted, the clarified milk can be processed by the usual separation methods. There also are proteases in milk which can degrade recombinant proteins. The greatest advantage of producing recombinant proteins in milk is the high concentration which can be obtained. The high levels of product protein can alleviate many problems associated with the application of classical purification strategies to transgenic milk proteins.

Original languageEnglish (US)
Pages (from-to)333-338
Number of pages6
JournalJournal of Cellular Biochemistry
Volume49
Issue number4
DOIs
StatePublished - Aug 1992

Keywords

  • Casein micelle
  • Immunopurification
  • Lactation
  • Monoclonal antibody
  • Post‐translational modification
  • proteases
  • therapeutics
  • viral inactivation
  • whey

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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