Arxula adeninivorans Recombinant Urate Oxidase and Its Application in the Production of Food with Low Uric Acid Content

被引:17
|
作者
Trautwein-Schult, Anke [1 ]
Jankowska, Dagmara [1 ]
Cordes, Arno [2 ]
Hoferichter, Petra [2 ]
Klein, Christina [2 ]
Matros, Andrea [1 ]
Mock, Hans-Peter [1 ]
Baronian, Keith [4 ]
Bode, Ruediger [3 ]
Kunze, Gotthard [1 ]
机构
[1] Leibniz Inst Plant Genet & Crop Plant Res IPK, DE-06466 Gatersleben, Germany
[2] ASA Spezialenzyme GmbH, Wolfenbuttel, Germany
[3] Ernst Moritz Arndt Univ Greifswald, Inst Microbiol, Greifswald, Germany
[4] Univ Canterbury, Sch Biol Sci, Christchurch 1, New Zealand
关键词
Arxula adeninivorans; Food; Hyperuricemia; Urate oxidase; Uric acid; MOLECULAR-CLONING; THERMOSTABLE URICASE; ESCHERICHIA-COLI; PURIFICATION; GENE; EXPRESSION; PROTEINS; GOUT; NOV; TRANSFORMATION;
D O I
10.1159/000353847
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Hyperuricemia and its symptoms are becoming increasingly common worldwide. Elevated serum uric acid levels are caused by increased uric acid synthesis from food constituents and reduced renal excretion. Treatment in most cases involves reducing alcohol intake and consumption of meat and fish or treatment with pharmaceuticals. Another approach could be to reduce uric acid level in food, either during production or consumption. This work reports the production of recombinant urate oxidase by Arxula adeninivorans and its application to reduce uric acid in a food product. The A. adeninivorans urate oxidase amino acid sequence was found to be similar to urate oxidases from other fungi (61-65% identity). In media supplemented with adenine, hypoxanthine or uric acid, induction of the urate oxidase (AUOX) gene and intracellular accumulation of urate oxidase (Auoxp) was observed. The enzyme characteristics were analyzed from isolates of the wild-type strain A. adeninivorans LS3, as well as from those of transgenic strains expressing the AUOX gene under control of the strong constitutive TEF1 promoter or the inducible AYNI1 promoter. The enzyme showed high substrate specificity for uric acid, a broad temperature and pH range, high thermostability and the ability to reduce uric acid content in food. (C) 2013 S. Karger AG, Basel
引用
收藏
页码:418 / 430
页数:13
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