The Production of Amino Acids by Transamination

Abstract

Amino acids have numerous industrial applications, including use as feed additives, ingredients in infusion solutions and other pharmaceutical products, components in flavor compositions, and chiral intermediates. Although amino acids are produced by a range of methods including chemical and fermentation techniques, biocatalytic routes are being proposed for the production of L-amino acids with increasing frequency. For example, Chibata and co-workers as well as several other groups have developed processes for the production of L-aspartic acid from ammonium fumarate catalyzed by whole cells containing the enzyme aspartase (Tosa et al. 1973; Wood and Calton 1984; Fusee et al. 1981). Genex Corporation commercialized a process for the production of L-phenylalanine based on the stereoselective addition of ammonia to trans-cinnamic acid catalyzed by the enzyme phenylalanine ammonia lyase (Hamilton et al. 1985). The enzyme serine hydroxymethyltrans-ferase has been shown to be useful in the production of L-serine from glycine and formaldehyde (Hamilton et al. 1985). Porcine aminoacylase has been used to resolve D,L mixtures of certain amino acids such as alanine, tryptophan, valine, and methionine (Leuchtenberger et al. 1984).