131320-88-2Relevant academic research and scientific papers
Mutant lipase-catalyzed kinetic resolution of bulky phenyl alkyl sec-alcohols: A thermodynamic analysis of enantioselectivity
Vallin, Michaela,Syren, Per-Olof,Hult, Karl
experimental part, p. 411 - 416 (2010/12/19)
The size of the stereoselectivity pocket of Candida antarctica lipase B limits the range of alcohols that can be resolved with this enzyme. These steric constrains have been changed by increasing the size of the pocket by the mutation W104A. The mutated enzyme has good activity and enantioselectivity toward bulky secondary alcohols, such as 1-phenylalkanols, with alkyl chains up to eight carbon atoms. The S enantiomer was preferred in contrast to the wild-type enzyme, which has R selectivity. The magnitude of the enantioselectivity changes in an interesting way with the chain length of the alkyl moiety. It is governed by interplay between entropic and enthalpic contributions and substrates with long alkyl chains are resolved best with E values higher than 100. The enantioselectivity increases with temperature for the small substrates, but decreases for the long ones.
Emerging solvent-induced homochirality by the confinement of achiral molecules against a solid surface
Katsonis, Nathalie,Xu, Hong,Haak, Robert M.,Kudernac, Tibor,Tomovic, Zeljko,George, Subi,Van Der Auweraer, Mark,Schenning, Albert P. H. J.,Meijer,Feringa, Ben L.,De Feyter, Steven
supporting information; experimental part, p. 4997 - 5001 (2009/03/11)
One hand mapping: By means of scanning tunneling microscopy, solvent-induced homochirality is shown to emerge in self-assembled monolayers of achiral molecules at the liquid-solid interface (see picture). The chirality of the solvent directs the macroscopic chirality of the monolayer. The dynamics of the monolayer structure as it evolves towards homochirality are probed by time-dependent measurements. (Figure Presented)
Enzymatic Preparation of the Enantiomers of Some 1-Phenyl-1-alkanols
Mori, Kenji,Bernotas, Rokas
, p. 87 - 96 (2007/10/02)
The acetates of racemic 1-phenyl-1-heptanol, 1-phenyl-1-octanol and 1-phenyl-1-nonanol were hydrolyzed by Pseudomonas lipase in 10percent acetone-0.1 M phosphate buffer (pH 6.9) at 30 deg C.Due to remarkable differences in the rates of hydrolysis of the e
