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Table 1 Enzyme activities and stereoconversions of ( R )-PED a to ( S )-enantiomer by recombinant E. coli strains

From: Efficient one-step production of (S)-1-phenyl-1,2-ethanediol from (R)-enantiomer plus NAD+–NADPH in-situ regeneration using engineered Escherichia coli

Strains/ plasmids

Specific activities (U/mg)

Biotransformation

bRCR

cSCR

dPNT

Optical purity (%e.e.)

Yield (%)

Cell-free extracts

Cell membranes

CK

NT

NT

0.010±0.001

0.021±0.001

5.4±0.05

4.8±0.05

RS

0.383±0.017e

1.871±0.043

0.013±0.002

0.021±0.005

64.3±0.07

52.7±0.04

AB

NT

NT

0.014±0.004

0.112±0.002

20.7±0.13

11.5±0.09

RSAB

0.349±0.010

1.758±0.027

0.013±0.001

0.096±0.001

93.5±0.12

87.4±0.09

  1. The stereoconversion of (R)-PED to (S)-PED was performed with the first addition of 1 mM NAD+ and 1 mM NADPH, at pH 6.5 and 35°C.
  2. Notes: a PED, 1-phenyl-1,2-ethanediol;
  3. b RCR, (R)-carbonyl reductase, the enzyme activity was measured using (R)-PED as substrate;
  4. c SCR, (S)-carbonyl reductase, the enzyme activity was measured using 2-hydroxyacetophenone as substrate;
  5. d PNT, nicotinamide nucleotide transhydrogenase;
  6. e Mean ± standard deviation;
  7. NT, no detectable enzyme activity.