Enantioselective hydrolysis with Arthrobacter lipase

Enantioselective Hydrolysis with Arthrobacter Lipase. Reaction performance with the Arthrobacter lipase was studied in detail. The pH profile curve of the zero-order reaction exhibited a pH-optimum around 7.0, and spontaneous hydrolysis was not significant at pH... 

Enantioselective Hydrolysis with Arthrobacter Lipase. The results of the enantioselective hydrolysis of the acetate of racemic CPBA are summarized in Table V for several commercial lipases that liberate very optically pure CPBA. The experimental conditions were chosen to give approximately 50% hydrolysis for each enzyme. It is noticed that all of the lipases in Table V hydrolyzed the ester of (S)-CPBA preferentially to give the insecticidally active (S)-isomer. This is apparently different from the case of HMPC. The highest activity and optical purity were again given by the Arthrobacter lipase. Spontaneous termination of the reaction at 50% hydrolysis was observed with this enzyme as was the case of HMPC. 

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