Potential of Y. lipolytica epoxide hydrolase for efficient production of enantiopure (R)-1,2-octanediol.

ABSTRACT: The recombinant Yleh from a tropical marine yeast Yarrowia lipolytica NCIM 3589 exhibited a high epoxide hydrolase activity of 9.34 ± 1.80 µmol min^-1 mg^-1 protein towards 1,2-epoxyoctane (EO), at pH 8.0 and 30 °C. The reaction product was identified as 1,2-Octanediol (OD) by GC-MS using EO and H₂O¹⁸ as substrate, affirming the functionality of Yleh as an epoxide hydrolase. For EO, the K_m, V_max, and k_cat/K_m values were 0.43 ± 0.017 mM, 0.042 ± 0.003 mM min^-1, and 467.17 ± 39.43 mM^-1 min^-1, respectively. To optimize the reaction conditions for conversion of racemic EO by Yleh catalyst to enantiopure (R)-1,2-octanediol, initially, Response Surface Methodology was employed.

SUBMITTER: Godase VP 

PROVIDER: S-EPMC10371975 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature