A NEW ENZYMATIC METHOD FOR L-PHENYLALANINE SYNTHESIS USING AMINOACYLASE AND PHENYLALANINE DEHYDROGENASE

An aminoacylase, inducibly formed in Bacillus thermoglucosidius grown with a synthetic compound, acetamidocinnamate, was used for enzymatic synthesis of L-phenylalanine from chloroacetamidocinnamate. The reacti on system consisted of the hydrolysis of chloroacetamidocinnamate to p henylpyruvate by aminoacylase and the reductive amination of phenylpyr uvate to L-phenylalanine by phenylalanine dehydrogenase. The coenzyme NADH consumed was regenerated by a coupled reaction with formate dehyd rogenase. Under optimum conditions for L-phenylalanine production, mor e than 98% of the initially added chloroacetamidocinnamate was convert ed effectively to L-phenylalanine without appreciable decomposition or racemization.