Affinity isolation of a cold-adapted enzyme: Lactate dehydrogenase from Bacillus psychrosaccharolyticus

R. Nandakumar, B. Mattiasson

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

A simple, economical and rapid affinity chromatography procedure with dyes as the ligand has been described for the one-step purification of a cold-adapted lactate dehydrogenase. Non-specific elution of Procion blue H-ERD-modified Sepharose yielded homogeneous preparations of lactate dehydrogenase both in column based procedures and in batch wise operations. Low operational temperatures resulted in the enhanced binding of the enzyme to the blue dye. The dissociation constants of the enzyme-dye complexes were 7.2±0.2 μM and 11.2±0.2 μM at 5 °C and 20 °C respectively.

Original languageEnglish (US)
Pages (from-to)327-331
Number of pages5
JournalBioseparation
Volume7
Issue number6
StatePublished - Nov 1998

Keywords

  • Affinity chromatography
  • Cold-adapted
  • Dye-ligand
  • Lactate dehydrogenase
  • Procion blue H-ERD
  • Psychrophilic

ASJC Scopus subject areas

  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Chemical Engineering(all)

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