Abstract
In this study, we report the cloning and expression of a functional glucoside 3-dehydrogenase (G3DH) gene from Sphingobacterium faecium ZJF-D6. This gene is 1686 bp in length and encodes a peptide of 562 amino acids. The G3DH gene was successfully expressed in E. coli, and the recombinant enzyme could oxidize glucosides, galactosides and analogues at C-3 position. The sequence and multiple alignment analysis showed that the enzyme has highest identity with G3DHs from Paraglaciecola polaris LMG 21857, Aliiglaciecola lipolytica E3 and Halomonas sp. alpha-15. The recombinant G3DH was purified on Ni–NTA column and exhibited the highest activity at pH 7.6 and 30 °C. It was sensitive to acid and alkali, and showed well thermostability. The SfG3DH could oxidize a wild range of sugars. When recombinant E. coli BL21 cells were used as catalyst, a high rate of conversion to N-p-nitrophenyl-3-ketovalidamine was achieved, and no p-nitroaniline was detected. This process offers a promising approach to fulfill substrate of 3-ketovalidoxylamine A C–N lyase production.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Asano N, Takeuchi M, Ninomiya K (1984) Microbial degration of validamycin A by Flavobacterium Saccharophilum, enzymatic cheavage of C-N linkage in validoxylamine A. J Antibiot 37:859–867
Chen XL, Zheng YG, Shen YC (2006) Voglibose (Basen (R) AO-128), one of the most important alpha-glucosidase inhibitors. Curr Med Chem 13:109–116
Fukui S, Hochster RM (1965) On the active transport of sucrose and of 3-keto-sucrose in Agrobacterium tumefaciens. Can J Biochem 43:1129–1141
Fukui S, Hayano K (1969) Micro methods for determination of 3-ketosucrose and 3-ketoglucose. Agric Biol Chem 33:1013–1017
Kojima K, Tsugawa W, Hamahuji T, Watazu Y, Sode K (1999) Effect of growth substrates on production of new soluble glucose 3-dehydrogenase in Halomonas (Deleya) sp.-15. Appl Biochem Biotech 77–79:827–834
Kojima K, Tsugawa W, Sode K (2001) Cloning and Expression of Glucose 3-Dehydrogenase from Halomonas sp. a-15 in Escherichia coli. Biochem Bioph Res C 282:21–27
Kurowski WM, Fensom AH, Pirt SJ (1975) Factors influencing the formation and stability of D-glucoside 3-dehydrogenase activity in cultures of Agrobacterium tumefaciens. J gen microbiol 90:191–202
Maeda A, Adachi S, Matsuno R (2001) Improvement of selectivity in 3-keto-cellobiose production from cellobiose by Agrobacterium tumefaciens. J Biol Chem 8:217–221
Morrison SC, Wood DA, Wood PM (1999) Characterization of a glucose 3-dehydrogenase from the cultivated mushroom (Agaricus bisporus). Appl Microbiol Biotechnol 51:58–64
Pothukuchy A, Mano N, Georgiou G, Heller A (2006) A potentially insect-implantable trehalose electrooxidizing anode. Biosens Bioelectron 22:678–684
Schuerman PL, Liu JS, Dandekar AM (1997) 3-Ketoglycoside-mediated metabolism of sucrose in E. coli as conferred by genes from Agrobacterium tumefaciens. Appl Microbiol Biotechnol 47:560–565
Sode K, Akaike E, Sugiura H, Tsugawa W (2001) Enzymatic synthesis of a novel trehalose derivative, 3, 3′-diketoneo-trehalose, and its potential application as the trehalase enzyme inhibitor. FEBS Lett 489:42–45
Takeuchi M, Asano N, Kameda Y, Matsui K (1985) Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum. J Biochem 98:1631–1638
Takeuchi M, Ninomiya K, Kawabata K, Asano N, Kameda Y, Matsui K (1986) Purification and properties of glucoside 3-dehydrogenase from Flavobacterium saccharophilum. J Biochem 100:1049–1055
Tsugawa W, Horiuchi S, Tanaka M, Wake H, Sode K (1996) Purification of a marine bacterial glucose dehydrogenase from Cytophaga marinoflava and its application for measurement of 1,5-anhydro-D-glucitol. Appl Biochem Biotech 56:301–310
Zhang JF, Zheng YG, Shen YC (2006) Purification and characterization of the glucoside 3-dehydrogenase produced by a newly isolated Stenotrophomonas maltrophilia CCTCC M 204024. Appl Microbiol Biotechnol 71:638–645
Zhang JF, Zheng YG, Liu ZQ, Shen YC (2007) Preparation of 3-keto validoxylamine A C-N lyase substrate: N-p-nitrophenyl-3-ketovalidamine by Stenotrophomonas maltrophilia CCTCC M 204024. Appl Microbiol Biotechnol 73:1275–1281
Zhang JF, Zheng YG, Shen YC (2010) Purification and characterization of 3-Ketovalidoxylamine A C-N Lyase produced by Stenotrophomonas maltrophilia. Appl Biochem Biotechnol 162:966–974
Zhang JF, Chen WQ, Ke W, Chen H (2014) Screening of a glucoside 3-dehydrogenase-producing strain, Sphingobacterium faecium, based on a high-throughput screening method and optimization of the culture conditions for enzyme production. Appl Biochem Biotechnol 172:3448–3460
Acknowledgements
This work was supported by the National Natural Science Foundation of China (No. 21102131).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Zhang, JF., Chen, WQ. & Chen, H. Gene cloning and expression of a glucoside 3-dehydrogenase from Sphingobacterium faecium ZJF-D6, and used it to produce N-p-nitrophenyl-3-ketovalidamine. World J Microbiol Biotechnol 33, 21 (2017). https://doi.org/10.1007/s11274-016-2187-0
Received:
Accepted:
Published:
DOI: https://doi.org/10.1007/s11274-016-2187-0