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Research Article | Open Access

Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food

Chenghua Wanga( ), Ran Zhanga, Yu Suna, You Wena, Xiaoling Liua, Xinhui Xingb
College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, China
Key Laboratory of Industrial Biocatalysis, Ministry of Education, Institute of Biochemical Engineering, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China

Peer review under responsibility of KeAi Communications Co., Ltd.

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Abstract

This study investigated the combinatorial expression of xanthine dehydrogenase (XDH) and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in the beer, beef and yeast. Naturally occurring xdhABC gene clusters of A. baumannii CICC 10254 and R. capsulatus CGMCC 1.3366 as well as two refactored clusters constructed by exchanging their xdhC genes were overexpressed in Escherichia coli and purified to near homogeneity. RcXDH chaperoned by AbXdhC showed nearly the same catalytic performance as that by RcXdhC, except for the decreased substrate affinity. While the AbXDH co-expressed with RcXdhC displayed enhanced acidic adaptation but weakened catalytic activity. All the XDHs degraded purines in beer, beef and yeast extract effectively, indicating potential applications in low-purine foods to prevent hyperuricemia and gout. The study also presents a method for exploiting the better chaperone XdhC and novel XDHs by functional complement activity using existing XdhCs such as RcXdhC.

Keywords

Co-expressionLow purine foodUric acidXanthine dehydrogenaseXdhC

References

[1]

C.A. Woolfolk, J.S. Downard, Distribution of xanthine-oxidase and xanthine dehydrogenase specificity types among bacteria, J. Bacterio. 130 (3) (1977) 1175-1191. https://doi.org/10.1128/JB.130.3.1175-1191.1977.
Crossref Google Scholar
[2]

C.H. Wang, C. Zhang, X.H. Xing, Xanthine dehydrogenase: an old enzyme with new knowledge and prospects, Bioengineered 7 (6) (2016) 395-405. https://doi.org/10.1080/21655979.2016.1206168.
Crossref Google Scholar
[3]

P. Kalimuthu, S. Leimkuhler, P.V. Bernhardt, Low-potential amperometric enzyme biosensor for xanthine and hypoxanthine, Anal. Chem. 84 (23) (2012) 10359-10365. https://doi.org/10.1021/ac3025027.
Crossref Google Scholar
[4]

R. Hille, The mononuclear molybdenum enzymes, Chem. Rev. 96 (7) (1996) 2757-2816. https://doi.org/10.1021/cr950061t.
Crossref Google Scholar
[5]

C. Enroth, B.T. Eger, K. Okamoto, et al., Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion, Proc. Natl. Acad. Sci. 97 (20) (2000) 10723-10728. https://doi.org/10.1073/pnas.97.20.10723.
Crossref Google Scholar
[6]

U. Dietzel, J. Kuper, J.A. Doebbler, et al., Mechanism of substrate and inhibitor binding of Rhodobacter capsulatus xanthine dehydrogenase, J. Biol. Chem. 284 (13) (2009) 8768-8776. https://doi.org/10.1074/jbc.M808114200.
Crossref Google Scholar
[7]

M. Neumann, W. Stocklein, A. Walburger, et al., Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase, Biochemistry 46 (33) (2007) 9586-9595. https://doi.org/10.1021/bi700630p.
Crossref Google Scholar
[8]

S. Leimkuhler, The biosynthesis of the molybdenum cofactors in Escherichia coli, Environ. Microbiol. 22 (6) (2020) 2007-2026. https://doi.org/10.1111/1462-2920.15003.
Crossref Google Scholar
[9]

N.V. Ivanov, F. Hubalek, M. Trani, et al., Factors involved in the assembly of a functional molybdopyranopterin center in recombinant Comamonas acidovorans xanthine dehydrogenase, Eur. J. Biochem. 270 (23) (2003) 4744-4754. https://doi.org/10.1046/j.1432-1033.2003.03875.x.
Crossref Google Scholar
[10]

S. Leimkuhler, W. Klipp, Role of XDHC in molybdenum cofactor insertion into xanthine dehydrogenase of Rhodobacter capsulatus, J. Bacteriol. 181 (9) (1999) 2745-2751. https://doi.org/10.1128/JB.181.9.2745-2751.1999.
Crossref Google Scholar
[11]

M. Zarepour, K. Kaspari, S. Stagge, et al., Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent producer of superoxide anions via its NADH oxidase activity, Plant. Mol. Biol. 72 (3) (2010) 301-310. https://doi.org/10.1007/s11103-009-9570-2.
Crossref Google Scholar
[12]

S. Leimkuhler, R. Hodson, G.N. George, et al., Recombinant Rhodobacter capsulatus xanthine dehydrogenase, a useful model system for the characterization of protein variants leading to xanthinuria Ⅰ in humans, J. Biol. Chem. 278 (23) (2003) 20802-20811. https://doi.org/10.1074/jbc.M303091200.
Crossref Google Scholar
[13]

C.G. Chen, G.Y. Cheng, H.H. Hao, et al., Mechanism of porcine liver xanthine oxidoreductase mediated N-oxide reduction of cyadox as revealed by docking and mutagenesis studies, PLoS One 8 (9) (2013) e73912. https://doi.org/10.1371/journal.pone.0073912.
Crossref Google Scholar
[14]

C.H. Wang, T.X. Zhao, M. Li, et al., Characterization of a novel Acinetobacter baumannii xanthine dehydrogenase expressed in Escherichia coli, Biotechnol. Lett. 38 (2) (2016) 337-344. https://doi.org/10.1007/s10529-015-1986-y.
Crossref Google Scholar
[15]

N.V. Ivanov, M. Trani, D.E. Edmondson, High-level expression and characterization of a highly functional Comamonas acidovorans xanthine dehydrogenase in Pseudomonas aeruginosa, Protein Expr. Purif. 37 (1) (2004) 72-82. https://doi.org/10.1016/j.pep.2004.05.002.
Crossref Google Scholar
[16]

M. Neumann, S. Leimkuhler, The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria, Biochem. Res. Int. 2011 (2011) 850924. https://doi.org/10.1155/2011/850924.
Crossref Google Scholar
[17]

C.H. Wang, C. Zhang, X.H. Xing, Enhanced catalytic properties of novel (αβγ)2 heterohexameric Rhodobacter capsulatus xanthine dehydrogenase by separate expression of the redox domains in Escherichia coli, Biochem. Eng. J. 119 (2017) 1-8. https://doi.org/10.1016/j.bej.2016.12.009.
Crossref Google Scholar
[18]

D.G. Gibson, L. Young, R.Y. Chuang, et al., Enzymatic assembly of DNA molecules up to several hundred kilobases, Nat. Methods 6 (5) (2009) 343-345. https://doi.org/10.1038/nmeth.1318.
Crossref Google Scholar
[19]

N. Guex, M.C. Peitsch, SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling, Electrophoresis 18 (15) (1997) 2714-2723. https://doi.org/10.1002/elps.1150181505.
Crossref Google Scholar
[20]

S. Yoshihisa, The stability of inosine in acid and in Alkali, B. Chem. Soc. Jpn. 47 (10) (1974) 2469-2472. https://doi.org/10.1002/10.1246/bcsj.47.2469.
Crossref Google Scholar
[21]

J. Davídek, J. Velíšekg, G. Janíček, Stability of inosinic acid, inosine and hypoxanthine in aqueous solutions, J. Food Sci. 37 (5) (1972) 789-790. https://doi.org/10.1111/j.1365-2621.1972.tb02753.x.
Crossref Google Scholar
[22]

D.A. Jankowska, A. Trautwein-Schult, A. Cordes, et al., Arxula adeninivorans xanthine oxidoreductase and its application in the production of food with low purine content, J. Appl. Microbiol. 115 (3) (2013) 796-807. https://doi.org/10.1111/jam.12284.
Crossref Google Scholar
[23]

A. Trautwein-Schult, D. Jankowska, A. Cordes, et al., Arxula adeninivorans recombinant urate oxidase and its application in the production of food with low uric acid content, J. Mol. Microb. Biotech. 23 (6) (2013) 418-430. https://doi.org/10.1159/000353847.
Crossref Google Scholar
[24]

D.A. Jankowska, A. Trautwein-Schult, A. Cordes, et al., A novel enzymatic approach in the production of food with low purine content using Arxula adeninivorans endogenous and recombinant purine degradative enzymes, Bioeng. Bugs. 6 (1) (2015) 20-25. https://doi.org/10.4161/21655979.2014.991667.
Crossref Google Scholar
[25]

D. Mahor, A. Priyanka, G.S. Prasad, et al., Functional and structural characterization of purine nucleoside phosphorylase from Kluyveromyces lactis and its potential applications in reducing purine content in food, PLoS One 11 (10) (2016) e0164279. https://doi.org/10.1371/journal.pone.0164279.
Crossref Google Scholar
[26]

H. Ishikita, B.T. Eger, K. Okamoto, et al., Protein conformational gating of enzymatic activity in xanthine oxidoreductase, J. Am. Chem. Soc. 134 (2) (2012) 999-1009. https://doi.org/10.1021/ja207173p.
Crossref Google Scholar
Food Science and Human Wellness
Volume 12 Issue 4,
July 2023
Pages 1343-1350
DOI: 10.1016/j.fshw.2022.10.035
Cite this article:
Wang C, Zhang R, Sun Y, et al. Combinatorial co-expression of xanthine dehydrogenase and chaperone XdhC from Acinetobacter baumannii and Rhodobacter capsulatus and their applications in decreasing purine content in food. Food Science and Human Wellness, 2023, 12(4): 1343-1350. https://doi.org/10.1016/j.fshw.2022.10.035

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Received: 07 July 2021
Revised: 02 December 2021
Accepted: 04 January 2022
Published: 18 November 2022
© 2023 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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