Conversion of phenylalanine to benzaldehyde initiated by an aminotransferase in lactobacillus plantarum.

The production of benzaldehyde from phenylalanine has been studied in various microorganisms, and several metabolic pathways have been proposed in the literature for the formation of this aromatic flavor compound. In this study, we describe benzaldehyde formation from phenylalanine by using a cell extract of Lactobacillus plantarum. Phenylalanine was initially converted to phenylpyruvic acid by an aminotransferase in the cell extract, and the keto acid was further transformed to benzaldehyde. However, control experiments with boiled cell extract revealed that the subsequent conversion of phenylpyruvic acid was a chemical oxidation step. It was observed that several cations could replace the extract in the conversion of phenylpyruvic acid to benzaldehyde. Addition of Cu(II) ions to phenylpyruvic acid resulted not only in the formation of benzaldehyde, but also in the generation of phenylacetic acid, mandelic acid, and phenylglyoxylic acid. These compounds have been considered intermediates in the biological conversion of phenylalanine. The chemical conversion step of phenylpyruvic acid was dependent on temperature, pH, the availability of cations, and the presence of oxygen.