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| Content Provider | Springer Nature Link |
|---|---|
| Author | Zhang, Feiwei Qiao, Dairong Xu, Hui Liao, Chong Li, Shilin Cao, Yi |
| Copyright Year | 2009 |
| Abstract | Xylose reductase (XR) is a key enzyme in xylose metabolism because it catalyzes the reduction of xylose to xylitol. In order to study the characteristics of XR from Candida tropicalis SCTCC 300249, its XR gene (xyll) was cloned and expressed in Escherichia coli BL21 (DE3). The fusion protein was purified effectively by Ni$^{2+}$-chelating chromatography, and the kinetics of the recombinant XR was investigated. The Km values of the C. tropicalis XR for NADPH and NADH were 45.5 μM and 161.9 μM, respectively, which demonstrated that this XR had dual coenzyme specificity. Moreover, this XR showed the highest catalytic efficiency (kcat=1.44×l0$^{4}$ min$^{−1}$) for xylose among the characterized aldose reductases. Batch fermentation was performed with Saccharomyces serivisiae W303-lA:pYES2XR, and resulted in 7.63 g/L cell mass, 93.67 g/L xylitol, and 2.34 g/L · h xylitol productivity. This XR coupled with its dual coenzyme specificity, high activity, and catalytic efficiency proved its utility in in vitro xylitol production. |
| Starting Page | 351 |
| Ending Page | 357 |
| Page Count | 7 |
| File Format | |
| ISSN | 12258873 |
| Journal | Journal of Microbiology |
| Volume Number | 47 |
| Issue Number | 3 |
| e-ISSN | 19763794 |
| Language | English |
| Publisher | The Microbiological Society of Korea |
| Publisher Date | 2009-06-26 |
| Publisher Place | Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Candida tropicalis xylose reductase coenzyme specificity catalytic efficiency Microbiology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Microbiology Applied Microbiology and Biotechnology |
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