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Background  NAD-independent  l -lactate dehydrogenase ( l -iLDH) from  Pseudomonas stutzeri  SDM can potentially be used for the kinetic resolution of small aliphatic 2-hydroxycarboxylic acids. However, this enzyme showed rather low activity towards aromatic 2-hydroxycarboxylic acids.    Results  Val-108 of  l -iLDH was changed to Ala by rationally site-directed mutagenesis. The  l -iLDH mutant exhibited much higher activity than wide-type  l -iLDH towards  l -mandelate, an aromatic 2-hydroxycarboxylic acid. Using the engineered  Escherichia coli  expressing the mutant  l -iLDH as a biocatalyst, 40 g·L -1  of  dl -mandelic acid was converted to 20.1 g·L -1  of  d -mandelic acid (enantiomeric purity higher than 99.5%) and 19.3 g·L -1  of benzoylformic acid.    Conclusions  A new biocatalyst with high catalytic efficiency toward an unnatural substrate was constructed by rationally re-design mutagenesis. Two building block intermediates (optically pure  d -mandelic acid and benzoylformic acid) were efficiently produced by the one-pot biotransformation system.

microbial cell factories

Rationally re-designed mutation of NAD-independent l-lactate dehydrogenase: high optical resolution of racemic mandelic acid by the engineered Escherichia coli