Enzymatic Production ofl-Tryptophan froml- anddl-5-Indolyl-methylhydantoin by Newly Isolated Bacterium

Abstract
Bacteria which can hydrolyze DL-5-indolylmethylhydantoin to L-tryptophan were isolated from various soils. The DL-5-indolylmethylhydantoin-hydrolyzing enzymes were inducible and intracellular. With intact cells, 50 mg/ml as wet base, of newly isolated bacterial strain T-523, 10 mg/ml of DL-5-indolylmethylhydantoin disappeared and 7.4 mg/ml of L-tryptophan in a molar yield of 82% was produced after 35 h incubation. Tryptophan produced was confirmed to be L-form regardless of the stereoisomer of the substrates used. A mechanism of asymmetric hydrolysis of DL-5-indolylmethylhydantoin was discussed.

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