Biocatalytic resolution of glycidyl aryl ethers by Trichosporon loubierii : cell/substrate ratio influences the optical purity of (R) - epoxides.
Glycidyl aryl ethers were resolved by using lyophilized cells of Trichosporon loubierii ECU1040 having epoxide hydrolase activity. The activity and enantioselectivity depended on the structure of the aryl group. Different cell/substrate ratios also influenced the optical purity of remaining substrate. An additional stability test of the whole-cell enzyme suggests that rapid deactivation of the epoxide hydrolase was the potential reason. (R)-Epoxides were prepared in gram amounts with optical purity of 87% - 99% ee.
Xu
Yi
Y
Laboratory of Biocatalysis and Bioprocessing, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, P.R. China.
Xu
Jian-He
JH
Pan
Jiang
J
Tang
Yan-Fa
YF
D002384:Catalysis; D002452:Cell Count; D018929:Cell Culture Techniques / Q000379:methods*; D049109:Cell Proliferation; D004789:Enzyme Activation; D004795:Enzyme Stability; D004851:Epoxide Hydrolases / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D004852:Epoxy Compounds / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D013237:Stereoisomerism; D014250:Trichosporon / Q000201:enzymology* / Q000254:growth & development*
D004852:Epoxy Compounds; C020344:glycidyl ethers; D004851:Epoxide Hydrolases