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.
ASJC Scopus subject areas
- Analytical Chemistry