Enzymatic resolution of (R, S)-2-octanol by Ultrastable-Y molecular sieve immobilized-lipase in microaqueous media

The resolution of (R, S)-2-octanol was performed in microaqueous media by P. expansion 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°C 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.