2005•Journal of Zhejiang University of TechnologyRequires access

Catalytic resolution of (R,S)-glycidyl butyrate by yeast-lipase

Kuang Chun-lan

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Abstract

A strain of microorganism capable of optically resolving racemic glycidyl butyrate has been isolated from soil and identified to be a yeast-lipase. The properties of the fermentative liquid in the optical resolution of glycidyl butyrate were investigated. The stereoselectivity was higher at pH 5.5, 30 ℃, 200 r/min,0.50 g substrate added in the fermentative liquid, when the racemic substrate was enzymatically hydrolyzed to 50.5%, the optical purity of recovered (R)-ester was 81.4% ee (enantiomeric excess).

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What this paper is about

A strain of microorganism capable of optically resolving racemic glycidyl butyrate has been isolated from soil and identified to be a yeast-lipase. The properties of the fermentative liquid in the optical resolution of glycidyl butyrate were investigated. The stereoselectivity was higher at pH 5.5, 30 ℃, 200 r/min,0.50 g substrate added in the fermentative liquid, when the racemic substrate was enzymatically hydrolyzed to 50.5%, the optical purity of recovered (R)-ester was 81.4% ee (enantiomeric excess).

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Available abstract

A strain of microorganism capable of optically resolving racemic glycidyl butyrate has been isolated from soil and identified to be a yeast-lipase. The properties of the fermentative liquid in the optical resolution of glycidyl butyrate were investigated. The stereoselectivity was higher at pH 5.5, 30 ℃, 200 r/min,0.50 g substrate added in the fermentative liquid, when the racemic substrate was enzymatically hydrolyzed to 50.5%, the optical purity of recovered (R)-ester was 81.4% ee (enantiomeric excess).

Key concepts: Lipase, Butyrate, Substrate (aquarium), Enantiomeric excess, Chemistry, Yeast, Hydrolysis, Resolution (logic)

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