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Figure 1.

The biomass of Acetobacter sp. CCTCC M209061 and the reduction activity of AcCR during its growing process.

Biomass (▪); Reduction activity (○).

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Figure 2.

SDS-PAGE analysis of the purified AcCR.

Gel was stained with 0.05% Coomassie Blue R-250: lane 1, molecular weight markers; lane 2, the purified enzyme with a molecular mass of 27 kDa.

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Table 1.

Purification of AcCR from Acetobacter sp. CCTCC M209061.

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Figure 3.

Relative activity of AcCR at different temperatures.

(A) Reduction of 4′-chloroacetophenone using NADPH as cofactor (▪); Oxidation of isopropanol using NADP+ as cofactor (□); (B) Reduction of 4′-chloroacetophenone using NADH as cofactor (▾); Oxidation of isopropanol using NAD+ as cofactor (□); The activity was measured in the temperature range of 10–45°C. The pH value was 5.0 (NADH as cofactor) or 7.5 (NADPH as cofactor) for reduction of 4′-chloroacetophenone or 8.0 for oxidation of isopropanol, respectively. The relative activity of AcCR at each optimal temperature for reduction and oxidation reactions was defined as 100%. (C) Thermal stability (•). The residual activity of AcCR after 5 h incubation (buffer pH 6.5) at varying temperatures were measured at 25°C.

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Figure 4.

Relative activity of AcCR at different pH values.

(A) Reduction of 4′-chloroacetophenone using NADPH as cofactor (▪); (B) Oxidation of isopropanol using NADP+ as cofactor (□); (C) Reduction of 4′-chloroacetophenone using NADH as cofactor (▾); (D) Oxidation of isopropanol using NAD+ as cofactor (□). The buffers used were 50 mM citrate-phosphate (pH 4.0–8.0), Tris-HCl (pH 7.5–8.5) and glycine–NaOH (pH 8.6–9.5) buffers. The enzyme's activity was measured in the pH range of 4.0–9.5 at 25°C for reduction of 4′-chloroacetophenone and at 35°C for oxidation of isopropanol. The relative activity of AcCR at each optimal pH for reduction and oxidation reactions was defined as 100%.

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Figure 5.

The stability of AcCR.

(A) pH stability (▪); The residual activities after incubation at various pH values (pH 4.5–8.0) for 5 days at 4°C were measured at buffer pH 5.0 and 25°C (NADH as cofactor). (B) Storage stability (▾). The residual activities after incubation at pH 6.5 for 30 days at 4°C were measured at buffer pH 5.0 and 25°C (NADH as cofactor). The relative activity of AcCR without incubation was defined as 100%.

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Table 2.

Effects of various additives on the activity of AcCR.

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Figure 6.

Effects of different substrates on AcCR-catalyzed asymmetric reduction of prochiral ketones.

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Table 3.

Kinetic parameters of AcCR for reduction of 4′-chloroacetophenone and oxidation of isopropanol.

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Table 4.

Effects of coenzyme supply methods on AcCR-mediated asymmetric reduction of prochiral ketones.

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Figure 7.

The gene sequences of AcCR from Acetobacter sp. CCTCC M209061.

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