Chem. J. Chinese Universities

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Enzymatic Resolution of (R,S)-2-Octanol by Ultrastable-Y Molecular Sieve Immobilized-lipase in Microaqueous Media

DAI Da-Zhang*, XIA Li-Ming   

  1. Institute of Bioengineering, College of Material Science and Chemical Engineering, Hangzhou 310027, China
  • Received:2007-04-17 Revised:1900-01-01 Online:2007-12-10 Published:2007-12-10
  • Contact: DAI Da-Zhang

Abstract: The resolution of (R,S)-2-octanol was performed in microaqueous media by P. expansum PED-03 lipase(PEL) immobilized onto Ultrastable-Y modified molecular sieve. It was found that conversion(c), enantiomeric excess(e.e.), and enantioselectivity(E) of the reaction catalyzed by PEL immobilized onto Ultrastable-Y modified molecular sieve were much higher, compared with free PEL and PEL immobilized by other carriers. Media type and water content played an important role in the resolution of (R,S)-2-octanol catalyzed by Ultrastable-Y modified molecular sieve immobilized-PEL, and the reaction conversion(c) reached 97.68% of the theoretical value and the enantiomeric excess(e.e.) reached 98.75% in n-hexane with 0.8% water at “memorial” pH =9.5 and 50 ℃ for 24 h. The modified Ultrastable-Y molecular sieve immobilized-PEL was a good biocatalyst with a fine enantioselectivity and stability, presenting a good promise in the enzymatic resolution of (R,S)-2-octanol.

Key words: Microaqueous media, Modified Ultrastable-Y molecular sieve, Immobilized lipase, Resolution, (R,S)-2-Octanol

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