175897-66-2Relevant academic research and scientific papers
Biocatalytic racemization of (hetero)aryl-aliphatic α- hydroxycarboxylic acids by Lactobacillus spp. proceeds via an oxidation-reduction sequence
Nestl, Bettina M.,Glueck, Silvia M.,Hall, Melanie,Kroutil, Wolfgang,Stuermer, Rainer,Hauer, Bernhard,Faber, Kurt
, p. 4573 - 4577 (2007/10/03)
The biocatalytic racemization of a range of (hetero)aryl- and (di)aryl-aliphatic α-hydroxycarboxylic acids has been achieved by using whole resting cells of Lactobacillus spp. The essentially mild (physiological) reaction conditions ensure the suppression of undesired side reactions, such as elimination, decomposition or condensation. Cofactor/inhibitor studies using a cell-free extract of Lactobacillus paracasei DSM 20207 reveal that the addition of redox cofactors (NAD+/NADH) leads to a distinct increase in the racemization rate, while strong inhibition is observed in the presence of Thio-NAD+, which suggests that the racemization proceeds by an oxidation-reduction sequence rather than involvement of a "racemase" enzyme. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.
Deracemisation of aryl substituted α-hydroxy esters using Candida parapsilosis ATCC 7330: Effect of substrate structure and mechanism
Baskar,Pandian,Priya,Chadha, Anju
, p. 12296 - 12306 (2007/10/03)
Candida parapsilosis ATCC 7330 was found to be an efficient biocatalyst for the deracemisation of aryl α-hydroxy esters (65-85% yield and 90-99% ee). A variety of aryl and aryl substituted α-hydroxy esters were synthesized to reflect steric and electronic effects on biocatalytic deracemisation. The mechanism of this biocatalytic deracemisation was found to be stereoinversion.
