Abstract

The aim of this thesis was to examine the applicability of a modified hydantoinase process to the production of chiral aromatic beta-amino acids. The hydantoinase process employs up to three enzymes for the dynamic kinetic resolution of 5beta-monosubstituted hydantoins via N-carbamoyl-beta-amino acids to beta-amino acids: a hydantoin racemase, a hydantoinase and a carbamoylase. It had to be studied whether these enzymes also show activity towards dihydropyrimidines and N-carbamoyl-beta-amino acids.

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