Facile synthesis of chiral 2‐hydroxy acids catalyzed by a stable duck ε‐crystallin with endogenous l‐lactate dehydrogenase activity

Abstract
Duck ε‐crystallin, an abundant structural protein in lenses of some avian species, was shown to possess a genuine and stable l‐lactate dehydrogenase (l‐LDH, EC 1.1.1.27) activity suitable for the application to enzyme technology as a catalyst for the synthesis of chiral α‐hydroxy acids. Two pharmaceutically important intermediates, 2‐hydroxy acids (S)‐2‐hydroxybutanoic acid (S)‐2‐hydroxypentanoic acid) have been synthesized in high yields and Optical purity utilizing an in situ NADH regeneration system of duck ε‐crystallin coupled with formate/formate dehydrogenase. This enzyme system is also shown to offer some advantages over the conventional l‐LDH sources from several mammalian species.

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