Production of phenylalanine ammonia-lyase (PAL): isolation and evaluation of yeast strains suitable for commercial production of l-phenylalanine

  title={Production of phenylalanine ammonia-lyase (PAL): isolation and evaluation of yeast strains suitable for commercial production of l-phenylalanine},
  author={Christopher Thomas Evans and Kim Hanna and Dayle Conrad and Wendy Peterson and Masanaru Misawa},
  journal={Applied Microbiology and Biotechnology},
SummaryPhenylalanine Ammonia-Lyase (PAL) containing microorganisms were isolated from a wide variety of natural habitats. The best 21 strains to emerge from the primary screen were screened for PAL activities in both directions using l-phenylalanine and t-cinnamate substrates. Twelve of the latter strains were compared for total cell production and PAL activity and 7 isolates were chosen for examination of the extent of PAL induction in various media. On the basis of these screens, isolate SPA… 
Strain Improvement of Rhodotorula graminis for Production of a Novel l-Phenylalanine Ammonia-Lyase
Strain GX6000 PAL showed significantly greater stability in bioreactors for the synthesis of l-phenylalanine, a finding that is consistent with the stability properties observed during fermentation.
Optimal conditions determined for yeast growth and PAL production were pH 6, 1% inoculum, 30°C for 26-28 h, and 85% conversion of substrate to product was obtained.
Novel stabilization of phenylalanine ammonia-lyase catalyst during bioconversion of trans-cinnamic acid to l-phenylalanine
SummaryProduction of l-phenylalanine from trans-cinnamic acid using isolate SPA10 cells was reduced to 26% of that observed initially when cells were reacted a second time with fresh substrate
Isolation of various hyperactive mutants of phenylalanine ammonia-lyase containing yeasts
Various strains of phenylalanine ammonia-lyase (PAL) containing yeasts were mutagenised using ultraviolet (UV) irradiation using analogues used to select the greatest frequency of mutants with the highest PAL activities: one such mutant, FP10M6, exhibited five times the PAL activity of the parent SPA 10.
Biotransformation of phenylpyruvic acid to l-phenylalanine using a strain of Pseudomonas fluorescens ATCC 11250 with high transaminase activity
Immobilisation of cells in calcium alginate and operation of a packed bed bioreactor enabled the continuous production of l-phenylalanine in concentrations greater than 15 g·l-1 after 60 days operation.
Cloning, expression and characterization of phenylalanine ammonia-lyase from Rhodotorula glutinis
The full-length gene of PAL from Rhodotorula glutinis, an anamorph of Rhodosporium toruloides, was isolated and exhibited the highest catalytic ability among the reported PALs.
Rhodotorula Glutinis: Strain Enrichment and Evaluation of Phenylalanine Ammonia Lyase
2006 NSIS Honourable Mention, Undergraduate Student Research Prize Winning Paper The enrichment of a Rhodotorula glufinis strain and the determination of its phenylalanine ammonia lyase (E.C.
Phenylalanine and tyrosine metabolism in the facultative methylotroph Nocardia sp. 239
Double mutants blocked in both phenylalanine dehydrogenase and phenylpyruvate decarboxylase completely failed to catabolize phenylAlanine and the absence of these enzymes did not affect growth on tyrosine.


Induction of L-phenylalanine ammonia-lyase during utilization of phenylalanine as a carbon or nitrogen source in Rhodotorula glutinis.
In this study, R. glutinis appeared to express a single lyase enzyme, regardless of whether induction was nitrogen signaled or carbon signaled, and Thin-layer chromatographic analysis of ether extracts prepared from cultures induced with doubly labeled L-phenylalanine provided evidence of a catabolic sequence containing cinnamic acid, benzoic acid, and 4-hydroxybenzoic Acid as degradative intermediates.
Synthesis and degradation of phenylalanine ammonia-lyase of Rhodosporidium toruloides
The synthesis of enzyme antigen by a mutant unable to metabolize phenylalanine indicated that this amino acid is the physiological inducer of the enzyme.
Microbial L-phenylalanine ammonia-lyase. Purification, subunit structure and kinetic properties of the enzyme from Rhizoctonia solani.
Steady-state rates of phenylalanine ammonia-lyase reaction in the presence of inhibitors have shown that only one molecule of each type of inhibitor binds to a molecule of the enzyme, suggesting the involvement of negative homotropic interactions in phenylAlanine ammonia -lyase.
Production of l-Phenylalanine from trans-Cinnamic Acid with Rhodotorula glutinis Containing l-Phenylalanine Ammonia-Lyase Activity
The enzyme activity was kept stable for a relatively long time during cultivation by the addition of l-isoleucine and may provide a rapid and practical way to produce l-phenylalanine useful as an essential amino acid.
Metabolism of Aromatic Amino Acid in Microorganisms: Part I. Formation of Cinnamic Acid from Phenylalanine
It was found that the enzyme activity specifically occurred in Rhodotorula and that the formation of enzyme was enhanced by culturing on the medium supplemented with phenylalanine.
Degradation of phenylalanine and tyrosine by Sporobolomyces roseus.
Ammonia-lyase activity for l-phenylalanine, m-hydroxyphenylalanines and l-tyrosine was demonstrated in cell-free extracts of Sporobolomyces roseus and 4-Hydroxycoumarin was identified as the product of o-cou maric acid metabolism by this organism.
The Production of L–Phenylalanine by Polyazetidine Immobilized Microbes
Aspartic acid was the amine donor of choice as the oxaloacetic acid produced in the reaction was readily decarboxylated to pyruvic acid under the experimental conditions thereby driving the reaction to completion.