Isolation and Characterization of L-Tryptophan Ammonia Lyase from Rubrivivax benzoatilyticus Strain JA2

Title:Isolation and Characterization of L-Tryptophan Ammonia Lyase from Rubrivivax benzoatilyticus Strain JA2

Volume: 16 Issue: 8

Author(s): Ranjith N. Kumavath, Ch.V. Ramana, Ch. Sasikala, Debmalya Barh, Alan Prem Kumar and Vasco Azevedo

Affiliation:

Keywords: Indole-3-acrylic acid, L-tryptophan, L-tryptophan ammonia lyase, Rubrivivax benzoatilyticus JA2.

Abstract: Ammonia lyase belongs to the family of enzymes that catalyzes the deamination of amino acids. Depending on the relative activity towards the substrates, L-tryptophan ammonia lyase converts L-tryptophan to indole 3-acrylic acid and ammonia. Here, we isolated, purified, and characterized an L-tryptophan ammonia lyase from phototrophic purple non-sulfur bacterium Rubrivivax benzoatilyticus JA2. The isolated L-tryptophan ammonia lyase found to catalyze the reaction of L-tryptophan to produce indole 3-acrylic acid and NH₃. The enzyme is a heterotetramer and has the highest affinity to L-tryptophan. The optimum pH and temperature for the enzymatic action were 7.5 and 35°C, respectively and the K_m and V_max were 40.4 ± 23.1 nM and 0.964±0.2046 s^-1, respectively. These results suggest that the isolated enzyme is highly bioactive and could be a new class. Further molecular analyses are required to confirm the novelty of the enzyme.

Cite this article as:

N. Kumavath Ranjith, Ramana Ch.V., Sasikala Ch., Barh Debmalya, Prem Kumar Alan and Azevedo Vasco, Isolation and Characterization of L-Tryptophan Ammonia Lyase from Rubrivivax benzoatilyticus Strain JA2, Current Protein & Peptide Science 2015; 16 (8) . https://dx.doi.org/10.2174/1389203716666150505235929

DOI https://dx.doi.org/10.2174/1389203716666150505235929	Print ISSN 1389-2037
Publisher Name Bentham Science Publisher	Online ISSN 1875-5550