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Updated: Jun 4, 2026

Mapping Metabolism: Monitoring Lactate Dehydrogenase Activity Directly in Tissue
Published on: June 21, 2018
Kinetic resolution of 2-hydroxybutanoate racemic mixtures by NAD-independent L-lactate dehydrogenase
Chao Gao1, Wen Zhang, Cuiqing Ma
1State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, People's Republic of China.
Abstract:
Optically active D-2-hydroxybutanoate is an important building block intermediate for medicines and biodegradable poly(2-hydroxybutanoate). Kinetic resolution of racemic 2-hydroxybutanoate may be a green and desirable alternative for D-2-hydroxybutanoate production. In this work, D-2-hydroxybutanoate at a high concentration (0.197 M) and a high enantiomeric excess (99.1%) was produced by an NAD-independent L-lactate dehydrogenase (L-iLDH) containing biocatalyst. 2-Oxobutanoate, another important intermediate, was co-produced at a high concentration (0.193 M). Using a simple ion exchange process with the macroporous anion exchange resin D301, D-2-hydroxybutanoate was separated from the biotransformation system with a high recovery of 84.7%.
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