Retinal Production From Beta-Carotene by Beta-Carotene 15,15'-dioxygenase From an Unculturable Marine Bacterium

Biotechnol Lett. 2010 Jul;32(7):957-61. doi: 10.1007/s10529-010-0239-3. Epub 2010 Mar 13.

Abstract

The conversion of beta-carotene to retinal by a recombinant beta-carotene 15,15'-dioxygenase (Blh protein) from an unculturable marine bacterium was optimized in aqueous solution. Toluene was optimal solvent for the dissolution of beta-carotene and the optimal solution for the conversion reaction contained 2.4% (w/v) Tween 20, 0.15 U enzyme/ml, and 350 mg beta-carotene/l. Under these conditions, the enzyme produced 181 mg retinal/l after 20 h. This is the highest reported value for the retinal concentration from beta-carotene.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteria / enzymology*
  • Bacteria / genetics
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Biotransformation
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Retinaldehyde / metabolism*
  • Seawater / microbiology
  • beta Carotene / metabolism*
  • beta-Carotene 15,15'-Monooxygenase / genetics
  • beta-Carotene 15,15'-Monooxygenase / isolation & purification
  • beta-Carotene 15,15'-Monooxygenase / metabolism*

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • beta Carotene
  • beta-Carotene 15,15'-Monooxygenase
  • Retinaldehyde