A novel enzymatic approach in the production of food with low purine content using Arxula adeninivorans endogenous and recombinant purine degradative enzymes

References

• Burkard M, Huth K. Hyperurikämie und Gicht. Ernährung und Fasten als Therapie. Berlin: Springer, 2010. 255-270. ISBN-13 978-3-540-88809-3
   Google Scholar
• Masseoud D, Rott K, Liu-Bryan R, Agudelo C. Overview of hyperuricaemia and gout. Curr Pharm Des 2005; 11:4117-24; PMID:16375732; http://dx.doi.org/10.2174/138161205774913318
   PubMedGoogle Scholar
• Schlesinger N. Dietary factors and hyperuricaemia. Curr Pharm Des 2005; 11:4133-8; PMID:16375734; http://dx.doi.org/10.2174/138161205774913273
   PubMedGoogle Scholar
• Saag KG, Choi H. Epidemiology, risk factors, and lifestyle modifications for gout. Arthritis Res Therapy 2006; 8 Suppl 1:S2; PMID:16820041; http://dx.doi.org/10.1186/ar1907
   PubMed Web of Science ®Google Scholar
• Terkeltaub R. Update on gout: new therapeutic strategies and options. Nat Rev Rheumatol 2010; 6:30-8; PMID:20046204; http://dx.doi.org/10.1038/nrrheum.2009.236
   PubMed Web of Science ®Google Scholar
• Mandell BF. Clinical manifestations of hyperuricemia and gout. Cleveland Clinic J Med 2008; 75 Suppl 5:S5-8; http://dx.doi.org/10.3949/ccjm.75.Suppl_5.S5
   PubMedGoogle Scholar
• Eggebeen AT. Gout: an update. Am Fam Physician 2007; 76:801-8; PMID:17910294
   PubMed Web of Science ®Google Scholar
• Burns CM, Wortmann RL. Gout therapeutics: new drugs for an old disease. Lancet 2011; 377:165-77; PMID:20719377; http://dx.doi.org/10.1016/S0140-6736(10)60665-4
   PubMed Web of Science ®Google Scholar
• Schlesinger N, Dalbeth N, Perez-Ruiz F. Gout–what are the treatment options? Expert Opin Pharmacother 2009; 10:1319-28; PMID:19463070; http://dx.doi.org/10.1517/14656560902950742
   PubMed Web of Science ®Google Scholar
• Jankowska DA, Faulwasser K, Trautwein-Schult A, Cordes A, Hoferichter P, Klein C, Bode R, Baronian K, Kunze G. Arxula adeninivorans recombinant adenine deaminase and its application in the production of food with low purine content. J Appl Microbiol 2013; 115:1134-46; PMID:23902582; http://dx.doi.org/10.1111/jam.12317
   PubMedGoogle Scholar
• Jankowska DA, Trautwein-Schult A, Cordes A, Hoferichter P, Klein C, Bode R, Baronian K, Kunze G. Arxula adeninivorans xanthine oxidoreductase and its application in the production of food with low purine content. J Appl Microbiol 2013; 115:796-807; PMID:23773263; http://dx.doi.org/10.1111/jam.12284
   PubMedGoogle Scholar
• Trautwein-Schult A, Jankowska D, Cordes A, Hoferichter P, Klein C, Matros A, Mock HP, Baronian K, Bode R, Kunze G. Arxula adeninivorans recombinant urate oxidase and its application in the production of food with low uric acid content. J Mol Microbiol Biotechnol 2013; 23:418-30; PMID:24022585; http://dx.doi.org/10.1159/000353847
   PubMedGoogle Scholar
• Trautwein-Schult A, Jankowska D, Cordes A, Hoferichter P, Klein C, Matros A, Mock HP, Baronian K, Bode R, Kunze G. Arxula adeninivorans recombinant guanine deaminase and its application in the production of food with low purine content. J Mol Microbiol Biotechnol 2014; 24:67-81; PMID:24481069; http://dx.doi.org/10.1159/000357674
   PubMedGoogle Scholar
• Scazzocchio C. The purine degradation pathway, genetics, biochemistry and regulation. Prog Ind Microbiol 1994; 29:221-57; PMID:7765126
   PubMedGoogle Scholar
• Vogels GD, Van der Drift C. Degradation of purines and pyrimidines by microorganisms. Bacteriol Rev 1976; 40:403-68; PMID:786256
   PubMedGoogle Scholar
• Kunze G, Gaillardin C, Czernicka M, Durrens P, Martin T, Böer E, Gabaldón T, Cruz J, Talla E, Marck C, et al. The complete genome of Blastobotrys (Arxula) adeninivorans LS3 – a yeast of biotechnological interest. Nat Biotechnol 2014; 7:66; PMID:24834124; http://dx.doi.org/10.1186/1754-6834-7-66
   PubMedGoogle Scholar
• Kahn K, Tipton PA. Kinetic mechanism and cofactor content of soybean root nodule urate oxidase. Biochemistry 1997; 36:4731-8; PMID:9125493; http://dx.doi.org/10.1021/bi963184w
   PubMedGoogle Scholar
• Cendron L, Berni R, Folli C, Ramazzina I, Percudani R, Zanotti G. The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation. J Biol Chem 2007; 282:18182-9; PMID:17428786; http://dx.doi.org/10.1074/jbc.M701297200
   PubMedGoogle Scholar
• Vogel C, Marcotte EM. Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nat Rev Genet 2012; 13:227-32; PMID:22411467
   PubMed Web of Science ®Google Scholar
• Scazzocchio C, Darlington AJ. The induction and repression of the enzymes of purine breakdown in Aspergillus nidulans. Biochim Biophys Acta 1968; 166:557-68; PMID:5680610; http://dx.doi.org/10.1016/0005-2787(68)90243-8
   PubMedGoogle Scholar
• Griffith AB, Garrett RH. Xanthine dehydrogenase expression in Neurospora crassa does not require a functional nit-2 regulatory gene. Biochem Genet 1988; 26:37-52; PMID:2967694; http://dx.doi.org/10.1007/BF00555487
   PubMedGoogle Scholar
• Cecchetto G, Richero M, Oestreicher N, Muro-Pastor MI, Pantano S, Scazzocchio C. Mutations in the basic loop of the Zn binuclear cluster of the UaY transcriptional activator suppress mutations in the dimerisation domain. Fungal Genet Biol 2012; 49:731-43; PMID:22760060; http://dx.doi.org/10.1016/j.fgb.2012.06.009
   PubMedGoogle Scholar
• MacPherson S, Larochelle M, Turcotte B. A fungal family of transcriptional regulators: the zinc cluster proteins. Microbiol Mol Biol Rev 2006; 70:583-604; PMID:16959962; http://dx.doi.org/10.1128/MMBR.00015-06
   PubMed Web of Science ®Google Scholar
• Wartmann T, Kruger A, Adler K, Duc BM, Kunze I, Kunze G. Temperature-dependent dimorphism of the yeast Arxula adeninivorans LS3. Antonie Van Leeuwenhoek 1995; 68:215-23; PMID:8572679; http://dx.doi.org/10.1007/BF00871818
   PubMedGoogle Scholar
• Böer E, Bode R, Mock HP, Piontek M, Kunze G. Atan1p-an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme. Yeast 2009; 26:323-37; PMID:19387973; http://dx.doi.org/10.1002/yea.1669
   PubMedGoogle Scholar
• Middelhoven WJ, De Kievit H, Biesbroek AL. Yeast species utilizing uric acid, adenine, n-alkylamines or diamines as sole source of carbon and energy. Antonie Van Leeuwenhoek 1985; 51:289-301; PMID:4091535; http://dx.doi.org/10.1007/BF02439938
   PubMedGoogle Scholar
• Middelhoven WJ, de Jong IM, de Winter M. Arxula adeninivorans, a yeast assimilating many nitrogenous and aromatic compounds. Antonie Van Leeuwenhoek 1991; 59:129-37; PMID:1854187; http://dx.doi.org/10.1007/BF00445657
   PubMedGoogle Scholar
• Middelhoven WJ, Hoogkamer-Te Niet MC, Kreger-Van Rij NJ. Trichosporon adeninovorans sp. nov., a yeast species utilizing adenine, xanthine, uric acid, putrescine and primary n-alkylamines as the sole source of carbon, nitrogen and energy. Antonie Van Leeuwenhoek 1984; 50:369-78; PMID:6543110; http://dx.doi.org/10.1007/BF00394651
   PubMedGoogle Scholar
• Böer E, Breuer FS, Weniger M, Denter S, Piontek M, Kunze G. Large-scale production of tannase using the yeast Arxula adeninivorans. Appl Microbiol Biotechnol 2011; 92:105-14; PMID:21559827; http://dx.doi.org/10.1007/s00253-011-3320-5
   PubMed Web of Science ®Google Scholar
• Sakai T, Jun HK. Purification and characterisation of adenine deaminase in Pseudomonas synxantha. J Ferment Technol 1978; 56:257-65.
   Google Scholar
• Cheng X, Yang B, Liu D, Chen G, Chen Y, Huang RF, Jiang YS. Genetic engineering of bacteria that can produce urate oxidase. Intern Med 2012; 2:4; http://dx.doi.org/10.4172/2165-8048.1000114
   Google Scholar