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2003•Unpublished venueRequires access

Kinetic Resolution of Glycidyl Esters Catalyzed by Lipase in a Biphasic Reaction System

Zhi Wang

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Abstract

The stereoselective hydrolysis of racemic glycidyl esters catalyzed by lipase in a biphasic system was studied. The results show that porcine pancreatic lipase (PPL) shows a high enantioselectivity towards glycidyl butyrate. The results also show (1) the optimal pH value was 7.6, (2) the optimal reaction temperature was 27 ℃ and (3) the optimal reaction time was 4 h. Under all above optimal conditions, Rglycidyl butyrate with more than 93.3% ee was prepared and the hydrolysis degree of racemic glycidyl butyrate was 60.6%. 

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What this paper is about

The stereoselective hydrolysis of racemic glycidyl esters catalyzed by lipase in a biphasic system was studied. The results show that porcine pancreatic lipase (PPL) shows a high enantioselectivity towards glycidyl butyrate. The results also show (1) the optimal pH value was 7.6, (2) the optimal reaction temperature was 27 ℃ and (3) the optimal reaction time was 4 h. Under all above optimal conditions, Rglycidyl butyrate with more than 93.3% ee was prepared and the hydrolysis degree of racemic glycidyl butyrate was 60.6%. 

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Available abstract

The stereoselective hydrolysis of racemic glycidyl esters catalyzed by lipase in a biphasic system was studied. The results show that porcine pancreatic lipase (PPL) shows a high enantioselectivity towards glycidyl butyrate. The results also show (1) the optimal pH value was 7.6, (2) the optimal reaction temperature was 27 ℃ and (3) the optimal reaction time was 4 h. Under all above optimal conditions, Rglycidyl butyrate with more than 93.3% ee was prepared and the hydrolysis degree of racemic glycidyl butyrate was 60.6%. 

Key concepts: Lipase, Butyrate, Kinetic resolution, Hydrolysis, Chemistry, Catalysis, Organic chemistry, Reaction conditions

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