Title : Potential of Y. lipolytica epoxide hydrolase for efficient production of enantiopure (R)-1,2-octanediol - Godase_2023_AMB.Express_13_77 |
Author(s) : Godase VP , Kumar VR , Kumar AR |
Ref : AMB Express , 13 :77 , 2023 |
Abstract :
The recombinant Yleh from a tropical marine yeast Yarrowia lipolytica NCIM 3589 exhibited a high epoxide hydrolase activity of 9.34 +/- 1.80 micromol min(-1) mg(-1) protein towards 1,2-epoxyoctane (EO), at pH 8.0 and 30 degreesC. The reaction product was identified as 1,2-Octanediol (OD) by GC-MS using EO and H(2)O(18) 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. Under optimized reaction conditions of 15 mM EO, 150 microg purified Yleh at 30 degreesC a maximal diol production of 7.11 mM was attained in a short span of 65 min with a yield of 47.4%. Green technology using deep eutectic solvents for the hydrophobic substrate (EO) were tested as co-solvents in Yleh catalyzed EO hydrolysis. Choline chloride-Glycerol, produced 9.08 mM OD with an increased OD yield of 60.5%. Thus, results showed that deep eutectic solvents could be a promising solvent for Yleh-catalyzed reactions making Yleh a potential biocatalyst for the biosynthesis of enantiopure synthons. |
PubMedSearch : Godase_2023_AMB.Express_13_77 |
PubMedID: 37495892 |
Inhibitor | 1,2-Octanediol |
Substrate | p-nitrostyrene-oxide |
Godase VP, Kumar VR, Kumar AR (2023)
Potential of Y. lipolytica epoxide hydrolase for efficient production of enantiopure (R)-1,2-octanediol
AMB Express
13 :77
Godase VP, Kumar VR, Kumar AR (2023)
AMB Express
13 :77