Tk. Maiti et Sp. Chatterjee, L-PHENYLALANINE PRODUCTION BY DOUBLE AUXOTROPHIC MULTIANALOGUE-RESISTANT MUTANT OF ARTHROBACTER-GLOBIFORMIS, Folia microbiologica, 39(5), 1994, pp. 387-391
Tryptophan-plus-tyrosine double auxotrophic mutants resistant to fluor
ophenylalanine (PFP) and beta-2-thienylalanine (TA) were isolated from
a biotin-requiring glutamate-producing Arthrobacter globiformis. The
mutants were found to produce L-phenylalanine in mineral salts medium.
Further improvement of L-phenylalanine production was achieved by iso
lation of mutants resistant to 5-methyltryptophan (MT) and 3-nitrotyro
sine (NT) from a double auxotrophic PFP' and TA' mutant. Under optimal
cultural condition one mutant yielded 9.6 g phenylalanine per L mediu
m in flask culture. Enzymic activity of regulatory enzymes (deoxy-D-ar
abino-heptulosonate-7-phosphate synthase, chorismate mutase and prephe
nate dehydratase) were observed in the wild type, double auxotroph and
double-auxotrophic multianalogue-resistant mutant.