Resolution of (R,S)-2-octanol by Penicillium expansum PED-03 lipase immobilized on modified ultrastable-Y molecular sieve in microaqueous media

Da Zhang Dai, Li Ming Xia*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

The resolution of (R,S)-2-octanol was performed in microaqueous media by the lipase from Penicillium expansum PED-03 lipase (PEL) immobilized on modified ultrastable-Y (USY) molecular sieve. It was found that the conversion, enantiomeric excess (ee), and enantioselectivity (E) of the resolution catalyzed by PEL immobilized on modified USY molecular sieve were much higher than that of the reaction catalyzed by free PEL and PEL immobilized on other supports. Media type, "memorial" pH value and water content were of great importance in the resolution of (R,S)-2-octanol by immobilized PEL, and the conversion of the reaction catalyzed by PEL immobilized on modified USY molecular sieve reached 48.84% with excellent enantioselectivity (average E of eight batches > 460) in n-hexane with 0.8% (v/v) water at "memorial" pH 9.5, 50 °C for 24 h, which showed a good application potential in the production of optically pure (R,S)-2-octanol.

Original languageEnglish
Pages (from-to)1455-1460
Number of pages6
JournalProcess Biochemistry
Volume41
Issue number6
DOIs
Publication statusPublished - Jun 2006
Externally publishedYes

Keywords

  • 2-Octanol
  • Immobilized lipase
  • Microaqueous media
  • Modified ultrastable-Y molecular sieve
  • Penicillium expansum PED-03
  • Resolution

Fingerprint

Dive into the research topics of 'Resolution of (R,S)-2-octanol by Penicillium expansum PED-03 lipase immobilized on modified ultrastable-Y molecular sieve in microaqueous media'. Together they form a unique fingerprint.

Cite this