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Research Paper - Invited

Biosynthesis of ethyl (S)-4-chloro-3-hydroxybutanoate with an NADH-dependent reductase (ClCR) discovered by genome data mining using a modified colorimetric screening strategy

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Pages 170-174 | Received 23 Jan 2015, Accepted 05 Feb 2015, Published online: 01 Apr 2015

Figures & data

Figure 1. Proposed color-generating mechanism (a). Effects of asorbance wavelength (b), FeCl3 concentration (c), incubation temperature (d), and incubation time (e) on color-developing.

Figure 1. Proposed color-generating mechanism (a). Effects of asorbance wavelength (b), FeCl3 concentration (c), incubation temperature (d), and incubation time (e) on color-developing.

Figure 2. SDS–PAGE analysis of recombinant protein of ClCR. Line 1: Marker. Line 2: supernatant (soluble proteins) after sonication of E. coli CCZU-T15.

Figure 2. SDS–PAGE analysis of recombinant protein of ClCR. Line 1: Marker. Line 2: supernatant (soluble proteins) after sonication of E. coli CCZU-T15.

Figure 3. Effects of the organic solvent (a) and potential cosubstrate (b) on the reductase activity.

Figure 3. Effects of the organic solvent (a) and potential cosubstrate (b) on the reductase activity.

Figure 4. Time courses for the biotransformation of COBE into (S)-CHBE. 50–200 mM COBE in the monophasic aqueous media; 500–1000 mM COBE in the biphasic media.

Figure 4. Time courses for the biotransformation of COBE into (S)-CHBE. 50–200 mM COBE in the monophasic aqueous media; 500–1000 mM COBE in the biphasic media.

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