A study towards efficient l-threonine aldolase-catalyzed enantio- and diastereoselective aldol reactions of glycine with substituted benzaldehydes: biocatalyst production and process development

The development of aldol reactions of glycine with substituted benzaldehydes in the presence of recombinant l-threonine aldolases from Escherichia coli or Saccharomyces cerevisiae, which were obtained with excellent overexpression data, has been carried out. When using glycine and ortho-chlorobenzaldehyde, a high conversion of >95%, an enantioselectivity of >99% ee, and a diastereoselectivity with d.r.(syn/anti) = 80:20 was obtained for the resulting β-hydroxy α-amino acid in such a biotransformation. It should be noted that this enzymatic process can be conducted at an elevated substrate concentration of 250 mM.

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