431940-27-1Relevant articles and documents
Biotransformation of new racemic (R,S)-5-benzylhydantoin derivatives by D-hydantoinases from adzuki bean
Latacz, Gniewomir,Kie?-Kononowicz, Katarzyna
, p. 117 - 124 (2014/04/17)
In the present work the scope of D-hydantoinase enzyme application was increased towards new racemic (R,S)-5-benzylhydantoin derivatives. Five new substrates for the D-hydantoinase (R,S)-5-(3′-carboxybenzyl)hydantoin, (R,S)-5-(4′-carboxybenzyl)hydantoin, (R,S)-5-(2′-carbomethoxybenzyl) hydantoin, (R,S)-5-(3′-carbomethoxybenzyl)hydantoin and (R,S)-5-(4′(4-ethoxycarboxy)propoxybenzyl)hydantoin were synthesised and converted using a two-step hydantoinase process into their corresponding D-phenylalanine derivatives. In this study two D-hydantoinases from Vigna angularis (adzuki bean) obtained from commercial sources were used: pure, isolated directly from Vigna angularis (V.a.D-HYD) 494 U/g and immobilised, recombinant, cloned and expressed in Escherichia coli (rD-HYD) 53.1 U/g. The results obtained showed that the examined enzymes catalysed hydrolysis of all new substrates into their corresponding N-carbamoyl-D-phenylalanine derivatives. High enantiomeric purities of the resulting D-phenylalanine derivatives were also determined. However, very low conversion yields of (R,S)-5-(3′- carboxybenzyl)hydantoin and (R,S)-5-(2′-carbomethoxybenzyl)hydantoin to corresponding N-carbamoyl-D amino acid were observed. Three D-phenylalanine derivatives: 4-carboxy-D-phenylalanine, 3-carbomethoxy-D-phenylalanine and 4-carbopropoxy-D-phenylalanine were obtained and isolated from the reaction mixtures using ion-exchange chromatography.
