Leifsonia alcohol dehydrogenase

Inoue, K., Makino, Y. and Itoh, N. (2005) Production of (A l-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (LSADH). Tetrahedron Asymmetry, 16 (15), 2539-2549. 

Mutated Rhodococcus phenylacetaldehyde reductase (PAR) or Leifsonia alcohol dehydrogenase (LSADH) were applied to water-soluble ketone substrates. For example, 4-hydroxy-2-butanone was reduced to (S)/(R)-l,3-butanediol, with a high yield and stereoselectivity. Intact E coli cells overexpressing mutated PAR (Sar268) or LSADH were directly immobilized with polyethyleneimine or 1,6-hexanediamine and glutaraldehyde and evaluated in a batch reactor. This system produced (S)-l,3-butanediol (87% ee) with a space-time yield (STY) of 12.5 mg/h/mL catalyst or (R)-l,3-butanediol (99% ee.) with an STY of 60.3 mg/h/mL catalyst. The immobilized cells in a packed bed reactor continuously produced (R)-l,3-butanediol with a yield of 99% (about 49.5 g/L) from 5% (w/v) 4-hydroxy-2-butanoate over 500 h. The concentration of PEI used for immobilization influenced the operational stability of immobilized cells, and the cells treated with 3% PEI showed better stability than those treated with lower PEI concentrations The immobilized E. coli biocatalyst could be used more than 30 times (for about 500 h) with no decrease in conversion [54]. 

Inoue K, Makino Y, Itoh N. Piuification and characterization of a novel alcohol dehydrogenase from Leifsonia sp strain S749 A promising biocatalyst for an asymmetric hydrogen transfer bioreduction. Appl. Environ. Microbiol. 2005 71 3633-3641. 

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