Abstract
We report the in situ and real-time monitoring of the interconversion of l- and d-alanine-d3 by alanine racemase from Bacillus stearothermophilus directly observed by 2H NMR spectroscopy in anisotropic phase. The enantiomers are distinguished by the difference of their 2H quadrupolar splittings in a chiral liquid crystal containing short DNA fragments. The proof-of-principle, the reliability, and the robustness of this new method is demonstrated by the determination of the turnover rates of the enzyme using the Michaelis-Menten model.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4694-4697 |
| Number of pages | 4 |
| Journal | Analytical Chemistry |
| Volume | 85 |
| Issue number | 9 |
| DOIs | |
| State | Published - May 7 2013 |
| Externally published | Yes |
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