Degradation of aromatic amino acids by Rhodococcus erythropolis

A Gram‐positive Rhodococcus erythropolis strain S1 was shown to assimilate aromatic amino acids such as L‐phenylalanine, L‐tyrosine, L‐tryptophan, D‐phenylalanine, D‐tyrosine and D‐tryptophan, which were utilized not only as the sole carbon source but also as a suitable nitrogen source. The highest growth on these aromatic amino acids occurred at a temperature of 30°C. L‐Phenylalanine, L‐tyrosine and L‐tryptophan degradative pathways would appear to be independent, and to be induced alternatively. The strain S1 also showed the ability to assimilate peptides which consisted of only L‐phenylalanine and L‐tyrosine.