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Background  Enantiopure 2-hydroxy acids are key intermediates for the synthesis of pharmaceuticals and fine chemicals. We present an enantioselective cascade biocatalysis using recombinant microbial cells for deracemization of racemic 2-hydroxy acids that allows for efficient production of enantiopure 2-hydroxy acids.    Results  The method was realized by a single recombinant  Escherichia coli  strain coexpressing three enzymes: ( S )-2-hydroxy acid dehydrogenase, ( R )-2-keto acid reductase and glucose dehydrogenase. One enantiomer [( S )-2-hydroxy acid] is firstly oxidized to the keto acid with ( S )-2-hydroxy acid dehydrogenase, while the other enantiomer [( R )-2-hydroxy acid] remains unchanged. Then, the keto acid obtained reduced to the opposite enantiomer with ( R )-2-keto acid reductase plus cofactor regeneration enzyme glucose dehydrogenase subsequently. The recombinant  E. coli  strain coexpressing the three enzymes was proven to be a promising biocatalyst for the cascade bioconversion of a structurally diverse range of racemic 2-hydroxy acids, giving the corresponding ( R )-2-hydroxy acids in up to 98.5 % conversion and >99 % enantiomeric excess.    Conclusions  In summary, a cascade biocatalysis was successfully developed to prepare valuable ( R )-2-hydroxy acids with an efficient three-enzyme system. The developed elegant cascade biocatalysis possesses high atom efficiency and represents a promising strategy for production of highly valued ( R )-2-hydroxy acids.    Electronic supplementary material  The online version of this article (doi:10.1186/s12934-016-0560-1) contains supplementary material, which is available to authorized users.

Enantioselective cascade biocatalysis for deracemization of 2-hydroxy acids using a three-enzyme system