@article {48792,
	title = {Potential of Y. lipolytica epoxide hydrolase for efficient production of enantiopure (R)-1,2-octanediol},
	journal = {AMB Express},
	volume = {13},
	year = {2023},
	month = {JUL },
	pages = {77},
	type = {Article},
	abstract = {<p>
	The recombinant Yleh from a tropical marine yeast Yarrowia lipolytica NCIM 3589 exhibited a high epoxide hydrolase activity of 9.34 +/- 1.80 mu mol min(-1) mg(-1) protein towards 1,2-epoxyoctane (EO), at pH 8.0 and 30 degrees 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. Under optimized reaction conditions of 15 mM EO, 150 mu g purified Yleh at 30 degrees C 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. [GRAPHICS] .</p>
},
	keywords = {Deep Eutectic solvents, Optimization, Recombinant epoxide hydrolase, Response surface methodology, Yarrowia lipolytica},
	issn = {2191-0855},
	doi = {10.1186/s13568-023-01584-1},
	author = {Godase, Vijaya P. P. and Kumar, V. Ravi and Kumar, Ameeta Ravi}
}
