74457-38-8Relevant articles and documents
Free and immobilized lecitase ultra as the biocatalyst in the kinetic resolution of (E)‐4‐arylbut‐3‐en‐2‐yl esters
Chojnacka, Anna,Drozd, Rados?aw,G?adkowski, Witold,Le?niarek, Aleksandra,Szymańska, Magdalena
, (2020/03/17)
The influence of buffer type, co‐solvent type, and acyl chain length was investigated for the enantioselective hydrolysis of racemic 4‐arylbut‐3‐en‐2‐yl esters using Lecitase Ultra (LU). Immobilized preparations of the Lecitase Ultra enzyme had
Highly enantioselective synthesis of 3-substituted furanones by palladium-catalyzed kinetic resolution of unsymmetrical allyl acetates
Mao, Bin,Ji, Yining,Fananas-Mastral, Martin,Caroli, Giuseppe,Meetsma, Auke,Feringa, Ben L.
, p. 3168 - 3173 (2012/05/05)
Resolving the issue: A near-perfect Pd-catalyzed kinetic resolution of 1,3-disubstituted unsymmetrical allylic acetates uses silyl enol ethers as nucleophiles to access the important 3-substituted-furanone scaffold (see scheme; DACH=diaminocyclohexyl, dba=dibenzylideneacetone). The reaction proceeds under mild conditions and provides the desired products with excellent chemo-, regio-, and enantioselectivity. Copyright
Asymmetric transesterification of secondary alcohols catalyzed by feruloyl esterase from Humicola insolens
Hatzakis, Nikos S.,Smonou, Ioulia
, p. 325 - 337 (2007/10/03)
A new asymmetric transesterification of secondary alcohols catalyzed by feruloyl esterase from Humicola insolens has been found. Although alcohols are not the natural substrates for this enzyme, a high R enantioselectivity was observed. Stereochemical studies showed that variations in substrate structure lead to strong variations in enantioselectivity. The highest enantioselectivities are obtained when the β-carbon of the secondary alcohol is tertiary or quaternary.