1103679-61-3Relevant academic research and scientific papers
Separation of enantiopure m-substituted 1-phenylethanols in high space-time yield using Bacillus subtilis esterase
Zheng, Gao-Wei,Liu, Xu-Yun,Zhang, Zhi-Jun,Tian, Ping,Lin, Guo-Qiang,Xu, Jian-He
, p. 20446 - 20449 (2013)
A recombinant Bacillus subtilis esterase (BsE) expressed in E. coli was found to exhibit excellent enantioselectivity (E was always greater than 100) towards m-substituted 1-phenylethanol acetates in the enantioselective hydrolysis reaction. An explanation for the high enantioselectivity observed towards these substrates was provided by molecular modeling. Moreover, the BsE also showed strong tolerance towards a high concentration of m-substituted 1-phenylethanol acetates (up to 1 M). Based on these excellent catalytic properties of BsE, a kind of m-substituted 1-phenylethanols, (R)-1-(3-chlorophenyl)ethanol, was efficiently synthesized in space-time yield of 920 g per L per day and 97% ee, indicating that the BsE was considered as a potentially ideal and promising biocatalyst for large-scale production of optically active m-substituted 1-phenylethanols. The Royal Society of Chemistry 2013.
Stereochemistry and mechanism of enzymatic and non-enzymatic hydrolysis of benzylic sec-sulfate esters
Toesch, Michael,Schober, Markus,Breinbauer, Rolf,Faber, Kurt
supporting information, p. 3930 - 3934 (2014/06/24)
The substrate scope of inverting alkylsulfatase Pisa1 was extended towards benzylic sec-sulfate esters by suppression of competing non-enzymatic autohydrolysis by addition of dimethyl sulfoxide as co-solvent. Detailed investigation of the mechanism of autohydrolysis in 18O-labeled buffer by using an enantiopure sec-benzylic sulfate ester as substrate revealed that from the three possible pathways (i) inverting SN2-type nucleophilic attack of [OH-] at the benzylic carbon represents the major pathway, whereas (ii) SN1-type formation of a planar benzylic carbenium ion leading to racemization was a minor event, and (iii) Retaining SN2-type nucleophilic attack at sulfur took place at the limits of detection. The data obtained are interpreted by analysis of Hammett constants of meta substituents. The enzymatic hydrolysis of benzylic sec-sulfate esters by alkylsulfatase Pisa1 proceeded with clean inversion of configuration and with excellent stereoselectivities when the competing non-enzymatic hydrolysis was suppressed by addition of dimethyl sulfoxide as co-solvent. Copyright
Rh(I)/DpenPhos catalyzed asymmetric hydrogenation of enol esters and potassium (E)-3-cyano-5-methylhex-3-enoate
Liu, Yan,Wang, Zheng,Ding, Kuiling
experimental part, p. 7581 - 7585 (2012/09/07)
Rh(I) complexes of a class of modular chiral monodentate phosphoramidites were highly efficient for the asymmetric hydrogenation of enol esters bearing α-aryl or α-alkyl groups, to afford the corresponding hydrogenation products in high enantioselectiviti
Highly efficient dynamic kinetic resolution of secondary aromatic alcohols with low-cost and easily available acid resins as racemization catalysts
Cheng, Yongmei,Xu, Gang,Wu, Jianping,Zhang, Chensheng,Yang, Lirong
experimental part, p. 2366 - 2369 (2010/06/13)
A new and efficient dynamic kinetic resolution (DKR) process of secondary aromatic alcohols was developed with acid resins as racemization catalysts. Acid resin CD8604 was shown to have excellent racemization activity and good biocompatibility. When employing CD8604 and complex acyl donors as racemization catalyst and acyl donor, respectively, enantiomerically pure aromatic acetate was obtained with excellent yield and ee values through the DKR process. It is noteworthy that the system could be reused more than 10 times with little loss of yield and ee value.
Baeyer-Villiger monooxygenase-catalyzed kinetic resolution of racemic α-alkyl benzyl ketones: enzymatic synthesis of α-alkyl benzylketones and α-alkyl benzylesters
Rodriguez, Cristina,Gonzalo, Gonzalo de,Torres Pazmino, Daniel E.,Fraaije, Marco W.,Gotor, Vicente
experimental part, p. 1168 - 1173 (2009/10/02)
The application of three BVMOs for the enantioselective oxidation of 3-phenylbutan-2-ones with different substituents in the aromatic moiety is described. By choosing the appropriate biocatalyst and substrate combination, chiral ketones and esters can be obtained with excellent enantiopurities. This methodology could also be applied to the resolution of racemic α-alkyl benzylketones with longer alkyl chains as well as with two substituted α-substituted benzylacetones. A kinetic analysis revealed that the BVMOs studied effectively convert all tested compounds showing that the enzymes are tolerant towards the substrate structure while being highly enantioselective. These properties render BVMOs as valuable biocatalysts for the preparation of compounds with high interest in organic synthesis.
