Preliminary Study on the Resolution of (R,S)Glycidyl Butyrate \=by Crude Lipase from Rhizopus sp.Bc009

The properties of crude lipase, extracted from Rhizopus sp. Bc009 useful to optical resolution of glycidyl butyrate were preliminarily investigated. The study on the effects of pH showed that the initial rate of hydrolysis at 30C was the highest at pH 5.3; the enzyme stereoselectivity was higher at pH 5.56.0, the enantiomeric ratio (E value) was 57. The optimal temperature was at 42C. The enzyme stereoselectivity showed a slight decrease as temperature rising. Both substrate and products caused no inhibition of hydrolysis reaction. The lipase in broth showed a characteristic similar to that of crude lipase.