950759-27-0Relevant articles and documents
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 (2013/11/06)
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.
Immobilized Manihot esculenta preparation as a novel biocatalyst in the enantioselective acetylation of racemic alcohols
Machado, Luciana L.,Lemos, Telma L.G.,de Mattos, Marcos Carlos,de Oliveira, Maria da Conceicao F.,de Gonzalo, Gonzalo,Gotor-Fernandez, Vicente,Gotor, Vicente
, p. 1418 - 1423 (2008/12/20)
The enzymatic preparation obtained from a discard of Manihot esculenta roots has been successfully immobilized on calcium alginate hydrogels. This preparation has been tested as a chiral biocatalyst in the enzymatic acylation of a set of racemic aromatic alcohols. Depending on the reaction conditions, excellent enantioselectivities can be achieved. Some parameters that can alter the biocatalytic properties of the enzyme, such as solvent, temperature, acyl donor and substrate structure have been studied exhaustively in order to establish a deeper knowledge of this novel biocatalyst.