Abstract
The great advantage of producing optically pure D‐ or L‐amino acids from D,L‐5‐monosubstituted hydantoins by bioconversion is the fact that most of the substrates already racemize under reaction conditions and are totally converted to the optically pure amino acids. Three enzymes were shown to be involved in the production of L‐tryptophan from D,L‐5‐indolylmethylhydantoin in Arthrobacter spec. DSM 3747 after growth in a medium containing the chemically synthesized D.L‐5‐indolyl‐3‐N‐methlylhydantoin as effective inducer. Besides a hydantoinase and a N‐carbamoyl‐L‐amino acid amidohydrolase, a 5‐indolylmethylhydantoin racemase was found and could be separated from the former enzymes by liquid‐liquid extraction and gel filtration.