TY  - JOUR
U1  - Zeitschriftenartikel, wissenschaftlich - begutachtet (reviewed)
A1  - Trautwein-Schult, Anke
A1  - Jankowska, Dagmara
A1  - Cordes, Arno
A1  - Hoferichter, Petra
A1  - Klein, Christina
A1  - Matros, Andrea
A1  - Mock, Hans-Peter
A1  - Baronian, Keith
A1  - Bode, Rüdiger
A1  - Kunze, Gotthard
T1  - Arxula adeninivorans Recombinant Guanine Deaminase and Its Application in the Production of Food with Low Purine Content
JF  - Journal of Molecular Microbiology and Biotechnology
N2  - Purines of exogenous and endogenous sources are degraded to uric acid in human beings. Concentrations >6.8 mg uric acid/dl serum cause hyperuricemia and its symptoms. Pharmaceuticals and the reduction of the intake of purine-rich food are used to control uric acid levels. A novel approach to the latter proposition is the enzymatic reduction of the purine content of food by purine-degrading enzymes. Here we describe the production of recombinant guanine deaminase by the yeast Arxula adeninivorans LS3 and its application in food. In media supplemented with nitrogen sources hypoxanthine or adenine, guanine deaminase (AGDA) gene expression is induced and intracellular accumulation of guanine deaminase (Agdap) protein occurs. The characteristics of the guanine deaminase isolated from wild-type strain LS3 and a transgenic strain expressing the AGDA gene under control of the strong constitutive TEF1 promoter were determined and compared. Both enzymes were dimeric and had temperature optima of 55°C with high substrate specificity for guanine and localisation in both the cytoplasm and vacuole of yeast. The enzyme was demonstrated to reduce levels of guanine in food. A mixture of guanine deaminase and other purine degradation enzymes will allow the reduction of purines in purine-rich foods.
KW  - -
KW  - Hyperuricemia
KW  - Recombinant guanine deaminase
KW  - Treatment of food
Y1  - 2014
UN  - https://nbn-resolving.org/urn:nbn:de:gbv:9-opus-32665
SN  - 1464-1801
SS  - 1464-1801
SN  - 1660-2412
SS  - 1660-2412
U6  - https://doi.org/10.1159/000357674
DO  - https://doi.org/10.1159/000357674
PM  - 24481069
VL  - 24
IS  - 2
SP  - 67
EP  - 81
PB  - S. Karger AG
CY  - Basel, Switzerland
ER  -