130464-07-2Relevant academic research and scientific papers
Adrenaline profiling of lipases and esterases with 1,2-diol and carbohydrate acetates
Wahler, Denis,Boujard, Olivier,Lefèvre, Fabrice,Reymond, Jean-Louis
, p. 703 - 710 (2007/10/03)
The adrenaline test for enzymes is a general back-titration procedure to detect 1,2-diols, 1,2-aminoalcohols and α-hydroxyketones reaction products of enzyme catalysis by colorimetry. The method was used to profile a series of esterases and lipases for their esterolytic activity on a series of carbohydrate and polyol acetates. Substrates were prepared by peracetylation and used for parallel microtiter-plate analysis of enzyme activities. This method can be used to achieve a rapid and automated characterization of a set of enzymes during HTS screening.
Kinetic resolution of trans-2-acetoxycycloalkan-1-ols by lipase-catalysed enantiomerically selective acylation
Bodai, Viktoria,Orovecz, Oliver,Szakacs, Gyoergy,Novak, Lajos,Poppe, Laszlo
, p. 2605 - 2612 (2007/10/03)
Kinetic resolution of a series of racemic trans-cycloalkane-1,2-diol monoacetates rac-2a-d was performed by enantiomerically selective transesterification with vinyl acetate catalysed by commercial and our own-prepared fungal lipases to yield diacetates (
Dispiroketals in synthesis. Part 24. Preparation and use of chiral 2,2′-bis(triisopropylsilyloxymethyl)bi(dihydropyran)s as new protecting and resolving agents for 1,2-diols
Laine, Dramane,Fujita, Morifumi,Ley, Steven V.
, p. 1639 - 1645 (2007/10/03)
C2 symmetric chiral 2,2′-bis(triisopropylsilyloxymethyl)bi(dihydropyran)s (S,S)-1 and (R,R)-1 were prepared from the corresponding glycidols and selectively reacted with 1,2-diols to give dispiroketals. The products of these reactions could be deprotected following treatment with fluoride, oxidation and reductive cleavage with samarium(II) iodide.
Enantioselective acylation of alcohols catalyzed by lipase QL from Alcaligenes sp.: A predictive active site model for lipase QL to identify the faster reacting enantiomer of an alcohol in this acylation
Naemura,Murata,Tanaka,Yano,Hirose,Tobe
, p. 1581 - 1584 (2007/10/03)
Lipase QL-catalyzed acylation of secondary alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether gave preferentially the corresponding acetate with an R configuration. On the basis of the results, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a secondary alcohol reacts faster in this reaction.
Enantioselective acylation of primary and secondary alcohols catalyzed by lipase QL from Alcaligenes sp.: A predictive active site model for lipase QL to identify which enantiomer of an alcohol reacts faster in this acylation
Naemura, Koichiro,Murata, Masaki,Tanaka, Rie,Yano, Masashi,Hirose, Keiji,Tobe, Yoshito
, p. 3285 - 3294 (2007/10/03)
Lipase QL (from Alcaligenes sp.)-catalyzed acylation of alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether converted preferentially primary alcohols with an S configuration and secondary alcohols with an R configuration into the corresponding homochiral acetates. On the basis of observed enantiomer selectivities, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation. Copyright (C) 1996 Published by Elsevier Science Ltd.
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.
Enzymatic Preparation of Optically Pure trans-1,2-Cycloalkanediols
Seemayer, R.,Schneider, M. P.
, p. 49 - 50 (2007/10/02)
trans-1,2-Cycloalkanediols (R,R)-1,4 and (S,S)-1,3 of high optical purities are prepared by enzymatic hydrolysis and estrification catalyzed by a lipase from Pseudomonas sp. (SAM II).
