139165-57-4Relevant articles and documents
Highly regio- and enantio-selective hydrolysis of two racemic epoxides by GmEH3, a novel epoxide hydrolase from Glycine max
Zhang, Chen,Li, Chuang,Zhu, Xiu-xiu,Liu, You-yi,Zhao, Jun,Wu, Min-chen
, p. 2795 - 2803 (2020/09/01)
A novel epoxide hydrolase from Glycine max, designated GmEH3, was excavated based on the computer-aided analysis. Then, gmeh3, a GmEH3-encoding gene, was cloned and successfully expressed in E. coli Rosetta(DE3). Among the ten investigated rac-epoxides, GmEH3 possessed the highest and best complementary regioselectivities (regioselectivity coefficients, αS = 93.7% and βR = 97.2%) in the asymmetric hydrolysis of rac-m-chlorostyrene oxide (5a), and the highest enantioselectivity (enantiomeric ratio, E = 55.6) towards rac-phenyl glycidyl ether (7a). The catalytic efficiency (kcatS/KmS = 2.50 mM?1 s?1) of purified GmEH3 for (S)-5a was slightly higher than that (kcatR/KmR = 1.52 mM?1 s?1) for (R)-5a, whereas the kcat/Km (5.16 mM?1 s?1) for (S)-7a was much higher than that (0.09 mM?1 s?1) for (R)-7a. Using 200 mg/mL wet cells of E. coli/gmeh3 as the biocatalyst, the scale-up enantioconvergent hydrolysis of 150 mM rac-5a at 25 °C for 1.5 h afforded (R)-5b with 90.2% eep and 95.4% yieldp, while the kinetic resolution of 500 mM rac-7a for 2.5 h retained (R)-7a with over 99% ees and 43.2% yields. Furthermore, the sources of high regiocomplementarity of GmEH3 for (S)- and (R)-5a as well as high enantioselectivity towards rac-7a were analyzed via molecular docking (MD) simulation.
Enantioselective Resolution Copolymerization of Racemic Epoxides and Anhydrides: Efficient Approach for Stereoregular Polyesters and Chiral Epoxides
Li, Jie,Ren, Bai-Hao,Wan, Zhao-Qian,Chen, Shi-Yu,Liu, Ye,Ren, Wei-Min,Lu, Xiao-Bing
supporting information, p. 8937 - 8942 (2019/06/11)
Herein we report an efficient strategy for preparing isotactic polyesters and chiral epoxides via enantioselective resolution copolymerization of racemic terminal epoxides with anhydrides, mediated by enantiopure bimetallic complexes in conjunction with a nucleophilic cocatalyst. The chirality of both the axial linker and the diamine backbones of the ligand are responsible for the chiral induction of this kinetic resolution copolymerization process. The catalyst systems exhibit exceptional levels of enantioselectivity with a kinetic resolution coefficient exceeding 300 for various racemic epoxides, affording highly isotactic copolymers (selectivity factors of more than 300) with a completely alternating structure and low polydispersity index. Most of the produced isotactic polyesters are typical semicrystalline materials with melting temperatures in the range from 77 to 160 °C.
Raw and waste plant materials as sources of fungi with epoxide hydrolase activity. Application to the kinetic resolution of aryl and alkyl glycidyl ethers
Dolcet, Marta,Torres, Mercè,Canela-Garayoa, Ramon
, p. 78 - 88 (2017/09/30)
The by-products of olive oil production can be used as sources of microbial strains. Penicillium sp., Aspergillus terreus, Penicillium aurantiogriseum, Aspergillus tubingensis and Aspergillus niger were selected on the basis of their epoxide-hydrolyzing activity towards racemic rac-glycidyl phenyl ether. We studied the effect on enzymatic activity of adding styrene oxide to the growth medium. It induced the biosynthesis of epoxide hydrolases and reduced cell growth. The resolution capacity of the five fungi was tested on rac-glycidyl phenyl ether, rac-benzyl glycidyl ether, rac-1,2-epoxyhexane and rac-1,2-epoxyoctane. The resolution of rac-glycidyl phenyl ether by A. niger, rac-benzyl glycidyl ether by P. aurantiogriseum and A. terreus, rac-1,2-epoxyhexane by A. tubingensis and rac-1,2-epoxyoctane by A. terreus provided (S)-3-phenoxy-1,2-propanediol (45.1% yield, 51.4% ee), (R)-3-benzyloxy-1,2-propanediol (40.8% yield, 43.3% ee), (S)-3-benzyloxy-1,2-propanediol (45.4% yield, 45.6% ee), (R)-1,2-hexanediol (70.4% yield, 24.4% ee) and (R)-1,2-octanediol (21.4% yield, 27.5% ee), respectively. The (R)-enantiopreference of the epoxide hydrolases from P. aurantiogriseum is unprecedented.