ethyl-4-chloro-3-hydroxybutanoate has been researched along with butyl-acetate* in 3 studies
3 other study(ies) available for ethyl-4-chloro-3-hydroxybutanoate and butyl-acetate
| Article | Year |
|---|---|
An experimental modeling of trinomial bioengineering- crp, rDNA, and transporter engineering within single cell factory for maximizing two-phase bioreduction.
Topics: Acetates; Acetoacetates; Alcohol Oxidoreductases; Biotransformation; Butyrates; Candida glabrata; DNA, Ribosomal; Dose-Response Relationship, Drug; Escherichia coli; Protein Engineering; Sesquiterpenes | 2017 |
Effective biosynthesis of ethyl (R)-4-chloro-3-hydroxybutanoate by supplementation of l-glutamine, d-xylose and β-cyclodextrin in n-butyl acetate-water media.
To avoid adding NAD(+) and effectively transform ethyl 4-chloro-3-oxobutanoate, the mixture of l-glutamine (200mM) and d-xylose (250mM) was added into in n-butyl acetate-water (10:90, v/v) biphasic system instead of NAD(+) for increasing the biocatalytic efficiency. To further improve the synthesis of optically pure ethyl (R)-4-chloro-3-hydroxybutanoate (>99% ee), β-cyclodextrin was also added into this reaction media, and ethyl (R)-4-chloro-3-hydroxybutanoate (>99% ee) could be effectively synthesized from 800mM ethyl 4-chloro-3-oxobutanoate in the yield of 100% by whole-cells of recombinant E. coli CCZU-A13. Finally, the possible mechanism for improving the reductase activity by supplementation of l-glutamine, d-xylose and β-CD was proposed. In conclusion, this strategy has high potential for the effective biosynthesis of ethyl (R)-4-chloro-3-hydroxybutanoate (>99% ee). Topics: Acetates; Acetoacetates; Bacterial Proteins; beta-Cyclodextrins; Butyrates; Culture Media; Escherichia coli; Glutamine; Oxidoreductases; Water; Xylose | 2015 |
A novel reductase from Candida albicans for the production of ethyl (S)-4-chloro-3-hydroxybutanoate.
A novel NADPH-dependent reductase (CaCR) from Candida albicans was cloned for the first time. It catalyzed asymmetric reduction to produce ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE). It contained an open reading frame of 843 bp encoding 281 amino acids. When co-expressed with a glucose dehydrogenase in Escherichia coli, recombinant CaCR exhibited an activity of 5.7 U/mg with ethyl 4-chloro-3-oxobutanoate (COBE) as substrate. In the biocatalysis of COBE to (S)-CHBE, 1320 mM (S)-CHBE was obtained without extra NADP+/NADPH in a water/butyl acetate system, and the optical purity of the (S)-isomer was higher than 99% enantiomeric excess. Topics: Acetates; Acetoacetates; Amino Acid Sequence; Biocatalysis; Butyrates; Candida albicans; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Fungal Proteins; Gene Expression; Glucose Dehydrogenases; Molecular Sequence Data; NADP; Open Reading Frames; Oxidoreductases; Plasmids; Stereoisomerism; Water | 2012 |