Deng_2016_Appl.Biochem.Biotechnol_180_228

Reference

Title : Functional Characterization of a Novel Dactylosporangium Esterase and Its Utilization in the Asymmetric Synthesis of (R)-Methyl Mandelate - Deng_2016_Appl.Biochem.Biotechnol_180_228
Author(s) : Deng D , Zhang Y , Sun A , Hu Y
Ref : Appl Biochem Biotechnol , 180 :228 , 2016
Abstract : One novel esterase DAEst6 was identified from the genome of Dactylosporangium aurantiacum subsp. Hamdenensis NRRL 18085. DAEst6 was further characterized to be an esterase which exhibited high resistance to high pH values. Esterase DAEst6 could resolve racemic methyl mandelate and generate (R)-methyl mandelate, one key drug intermediate, with an enantiomeric excess and a conversion of 99 and 49 %, respectively, after process optimization. The optimal working condition for the preparation of (R)-methyl mandelate through DAEst6 was found to be 10-mM racemic methyl mandelate, no organic co-solvents, pH 7.5, and 40 degrees C, for 5 h. Our work was the first report about the functional characterization of one novel Dactylosporangium esterase and the utilization of one Dactylosporangium esterase in kinetic resolution. Dactylosporangium esterases represented by DAEst6 possess great potential in the generation of valuable chiral drug intermediates and chemicals.
ESTHER : Deng_2016_Appl.Biochem.Biotechnol_180_228
PubMedSearch : Deng_2016_Appl.Biochem.Biotechnol_180_228
PubMedID: 27118549
Gene_locus related to this paper: 9actn-DAEst6

Related information

Gene_locus related to this paper: 9actn-DAEst6

Citations formats

Deng D, Zhang Y, Sun A, Hu Y (2016)
Functional Characterization of a Novel Dactylosporangium Esterase and Its Utilization in the Asymmetric Synthesis of (R)-Methyl Mandelate
Appl Biochem Biotechnol 180 :228

Deng D, Zhang Y, Sun A, Hu Y (2016)
Appl Biochem Biotechnol 180 :228