A New Enzymatic Method for L-Phenylalanine Synthesis Using Aminoacylase and Phenylalanine Dehydrogenase

Abstract

An aminoacylase, inducibly formed in Bacillus thermoglucosidius grown with a synthetic compound, acetamidocinnamate, was used for enzymatic synthesis of L-phenylalanine from chloroacetamidocinnamate. The reaction system consisted of the hydrolysis of chloroacetamidocinnamate to phenylpyruvate by aminoacylase and the reductive amination of phenylpyruvate to L-phenylalanine by phenylalanine dehydrogenase. The coenzyme NADH consumed was regenerated by a coupled reaction with formate dehydrogenase. Under optimum conditions for L-phenylalanine production, more than 98% of the initially added chloroacetamidocinnamate was converted effectively to L-phenylalanine without appreciable decomposition or racemization.