Arxula adeninivorans recombinant adenine deaminase and its application in the production of food with low purine content

Aims Construction of a transgenic Arxula adeninivorans strain that produces a high concentration of adenine deaminase and investigation into the application of the enzyme in the production of food with low purine content. Methods and Results The A. adeninivorans AADA gene, encoding adenine deaminase...

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Published in:Journal of applied microbiology Vol. 115; no. 5; pp. 1134 - 1146
Main Authors: Jankowska, D.A., Faulwasser, K., Trautwein‐Schult, A., Cordes, A., Hoferichter, P., Klein, C., Bode, R., Baronian, K., Kunze, G.
Format: Journal Article
Language:English
Published: Oxford Blackwell 01-11-2013
Oxford University Press
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Summary:Aims Construction of a transgenic Arxula adeninivorans strain that produces a high concentration of adenine deaminase and investigation into the application of the enzyme in the production of food with low purine content. Methods and Results The A. adeninivorans AADA gene, encoding adenine deaminase, was expressed in this yeast under the control of the strong inducible nitrite reductase promoter using the Xplor®2 transformation/expression platform. The recombinant enzyme was biochemically characterized and was found to have a pH range of 5·5–7·5 and temperature range of 34–46°C with medium thermostability. A beef broth was treated with the purified enzyme resulting in the concentration of adenine decreasing from 70·4 to 0·4 mg l−1. Conclusions It was shown that the production of adenine deaminase by A. adeninivorans can be increased and that the recombinant adenine deaminase can be used to lower the adenine content in the food. Significance and Impact of the Study Adenine deaminase is one component of an enzymatic system that can reduce the production of uric acid from food constituents. This study gives details on the expression, characterization and application of the enzyme and thus provides evidence that supports the further development of the system.
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ISSN:1364-5072
1365-2672
DOI:10.1111/jam.12317