<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Godase, Vijaya P. P.</style></author><author><style face="normal" font="default" size="100%">Kumar, V. Ravi</style></author><author><style face="normal" font="default" size="100%">Kumar, Ameeta Ravi</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Potential of Y. lipolytica epoxide hydrolase for efficient production of enantiopure (R)-1,2-octanediol</style></title><secondary-title><style face="normal" font="default" size="100%">AMB Express</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Deep Eutectic solvents</style></keyword><keyword><style  face="normal" font="default" size="100%">Optimization</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant epoxide hydrolase</style></keyword><keyword><style  face="normal" font="default" size="100%">Response surface methodology</style></keyword><keyword><style  face="normal" font="default" size="100%">Yarrowia lipolytica</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">13</style></volume><pages><style face="normal" font="default" size="100%">77</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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] .&lt;/p&gt;
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	Foreign&lt;/p&gt;
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	3.7&lt;/p&gt;
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