Abstract
A soluble glucoside 3-dehydrogenase (G3DH) from Stenotrophomonas maltrophilia CCTCC M 204024, recently isolated from wheat soil in our laboratory, was purified to 37.4-fold with a yield of 24.7% and was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a molecular mass of 66 kDa. 2,6-Dichlorophenolindophenol (DCPIP) and ferricyanide were able to act as artificial electron acceptors for the enzyme. The optimal pH of G3DH was in the range of 6.0–7.0 in the presence of DCPIP. The enzyme was stable in the pH range of 4.4–10.6 and was sensitive to heat. G3DH exhibited extremely broad substrate specificity by converting many sugars to their corresponding 3-ketoglucosides. They produced a characteristic spectrum by alkaline treatment with a peak at 340 nm. The apparent K m values for validoxylamine A and d-glucose were 8.3 and 1.1 mM, respectively. Cu2+, Ag2+, and Hg2Cl2 inhibited the activity of G3DH.
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Acknowledgements
This work was supported by the National Fund of the Major Basic Research Development Program 973 of China (2003CB716005), the National Natural Science Foundation of China (20176055), and the Natural Science Foundation of Zhejiang Province (ZB0106).
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Zhang, JF., Zheng, YG., Xue, YP. et al. Purification and characterization of the glucoside 3-dehydrogenase produced by a newly isolated Stenotrophomonas maltrophilia CCTCC M 204024. Appl Microbiol Biotechnol 71, 638–645 (2006). https://doi.org/10.1007/s00253-005-0201-9
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DOI: https://doi.org/10.1007/s00253-005-0201-9