152375-69-4Relevant articles and documents
Selector screening for enantioseparation of DL-α-methyl phenylglycine amide by liquid-liquid extraction
Schuur, Boelo,Blahu?iak, Marek,Vitasari, Caecilia R.,Grambli?ka, Michal,De Haan, André B.,Visser, Ton J.
, p. 123 - 130 (2015)
Enantioseparation through liquid extraction technology is an emerging field, e.g., enantioseparations of amino acids (and derivatives thereof), amino alcohols, amines, and carboxylic acids have been reported. Often, when a new selector is developed, the versatility of substrate scope is investigated. From an industrial point of view, the problem is typically approached the other way around, and for a target racemate, a selector needs to be found in order to accomplish the desired enantioseparation. This study presents such a screening approach for the separation of the enantiomers of DL-α-methyl phenylglycine amide (DL-α-MPGA), a model amide racemate with high industrial relevance. Chiral selectors that were reported for other classes of racemates were investigated, i.e., several macrocyclic selectors and Pd-BINAP complexes. It appeared very challenging to obtain both high extraction yields and good enantioselectivity for most selectors, but Pd-BINAP-based selectors performed well, with enantioselectivities up to 7.4 with an extraction yield of the desired enantiomer of 95.8%. These high enantioselectivities were obtained using dichloromethane as solvent. Using less volatile chlorobenzene or 1-chloropentane, reasonable selectivities of up to 1.7 were measured, making these the best alternative solvents for dichloromethane.
Efficient biocatalytic synthesis of highly enantiopure α-alkylated arylglycines and amides
Wang, Mei-Xiang,Lin, Shuan-Jun,Liu, Jun,Zheng, Qi-Yu
, p. 439 - 445 (2007/10/03)
A number of racemic α-alkylarylglycine amides including 1-amino-1-carbamoyl-1,2,3,4-tetrahydronaphthalene underwent efficient biocatalytic hydrolysis under very mild conditions to afford the corresponding (S)-α-alkylarylglycines and (R)-α-alkylarylglycine
Enzymatic resolution of α,α-disubstituted α-amino acid esters and amides
Kaptein,Boesten,Broxterman,Peters,Schoemaker,Kamphuis
, p. 1113 - 1116 (2007/10/02)
The scope and limitations of the enzymatic resolution of α,α-disubstituted α-amino acid amides by an amino acid amidase from Mycobacterium neoaurum and of the corresponding ethyl esters with Pig liver esterase (PLE) have been studied. Moderate enantiomeric excesses were obtained with PLE, with only a narrow substrate specificity. Mycobacterium neoaurum on the contrary yields a broad range of S-α,α-disubstituted α-amino acids 1 and the corresponding R-amides 2.