152140-96-0Relevant academic research and scientific papers
Enantioselective Hydrolysis of 2-Methylcyclohexanyl Acetates with the Cultured Cells of Marchantia polymorpha
Hirata, Toshifumi,Izumi, Shunsuke,Akita, Kenji,Yoshida, Hiroaki,Gotoh, Shisei
, p. 1465 - 1466 (1993)
Enantioselectivity in the hydrolysis of trans- and cis-2-methylcyclohexanyl acetates with the cultured cells of Marchantia polymorpha was investigated.The cultured cells were found to hydrolyze preferentially the acetates having the R-configuration.
Lipase-catalyzed enantioselective acylation of alcohols: A predictive active site model for lipase YS to identify which enantiomer of an alcohol reacts faster in this acylation
Naemura,Fukuda,Murata,Konishi,Hirose,Tobe
, p. 2385 - 2394 (2007/10/03)
Primary alcohols having a hydroxymethyl group at an S sterogemic center and secondary alcohols with an R configuration are preferentially acylated to give the corresponding acetates by lipase YS (from Pseudomonas fluorescens)-catalyzed acylation using isopropenyl acetate as the acylating agent in diisopropyl ether. On the basis of enantiomer selectivities observed, a predictive active site model for lipase YS is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation.
Lipase YS-catalysed Acylation of Alcohols: a Predictive Active Site Model for Lipase YS to Identify which Enantiomer of a Primary or a Secondary Alcohol Reacts Faster in this Acylation
Naemura, Koichiro,Fukuda, Ritsuko,Konishi, Masayoshi,Hirose, Keiji,Tobe, Yoshito
, p. 1253 - 1256 (2007/10/02)
Primary alcohols having a hydroxymethyl group at an S chiral centre and secondary alcohols with an R configuration are preferentially acylated to give the corresponding acetates by lipase YS-catalysed acylation in diisopropyl ether; a predictive cubic-spaced active site model for lipase YS is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation.
