13704-09-1Relevant articles and documents
Biocatalytic aminolysis of ethyl (S)-mandelate by lipase from Candida antarctica
Lima, Rafaely N.,Porto, André L.M.
, p. 157 - 163 (2017)
Enzymes play many roles in the advancement of biotechnology, discovery of new therapeutic agents and industrial processes. In this perspective, aminolysis reactions using lipase from Candida antarctica (CAL-B) were performed from ethyl (S)-mandelate and several aliphatic amines (45 °C, hexane, 3–6 h). By means of optimized conditions, amides with excellent isolated yields (60–97%) were synthetized. The biotechnological potential of CAL-B as a promising approach for the synthesis of organic compounds in a more sustainable, rapid, efficient and green chemistry perspective was verified on these results.
Biocatalysed reductions of α-ketoesters employing CyreneTM as cosolvent
de Gonzalo, Gonzalo
, (2021/02/26)
The search for novel reaction media with environmental friendly properties is an area of great interest in enzyme catalysis. Water is the medium of biocatalysed processes, but due to its properties, sometimes the presence of organic (co)solvents is required. CyreneTM represents one of the newest approaches to this medium engineering. This polar solvent has been employed for the first time in biocatalysed reductions employing purified alcohol dehydrogenases. A set of α-ketoesters has been reduced to the corresponding chiral α-hydroxyesters with high conversions and optical purities, being possible to obtain good results at Cyrene contents of 30% v/v and working at substrate concentrations of 1.0 M in presence of 2.5% v/v of this solvent. At this concentration, the presence of Cyrene has a beneficial effect in the bioreduction conversion.
Exploiting Cofactor Versatility to Convert a FAD-Dependent Baeyer–Villiger Monooxygenase into a Ketoreductase
Xu, Jian,Peng, Yongzhen,Wang, Zhiguo,Hu, Yujing,Fan, Jiajie,Zheng, He,Lin, Xianfu,Wu, Qi
, p. 14499 - 14503 (2019/09/17)
Cyclohexanone monooxygenases (CHMOs) show very high catalytic specificity for natural Baeyer–Villiger (BV) reactions and promiscuous reduction reactions have not been reported to date. Wild-type CHMO from Acinetobacter sp. NCIMB 9871 was found to possess an innate, promiscuous ability to reduce an aromatic α-keto ester, but with poor yield and stereoselectivity. Structure-guided, site-directed mutagenesis drastically improved the catalytic carbonyl-reduction activity (yield up to 99 %) and stereoselectivity (ee up to 99 %), thereby converting this CHMO into a ketoreductase, which can reduce a range of differently substituted aromatic α-keto esters. The improved, promiscuous reduction activity of the mutant enzyme in comparison to the wild-type enzyme results from a decrease in the distance between the carbonyl moiety of the substrate and the hydrogen atom on N5 of the reduced flavin adenine dinucleotide (FAD) cofactor, as confirmed using docking and molecular dynamics simulations.
