Fig. 6: Preliminary substrate scope of PcAOx-VPN. | Nature Communications

Fig. 6: Preliminary substrate scope of PcAOx-VPN.

From: Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis

Fig. 6: Preliminary substrate scope of PcAOx-VPN.The alternative text for this image may have been generated using AI.

General conditions: [PcAOx-VPN] = 20 μM, [substrate] = 50 mM in 50 mM KPi buffer (pH 7.5) containing DMSO (5%, v/v) as cosolvent. T = 30 °C, 500 rpm, [vinyl acetate] = 250 mM. Experiments were performed as technical duplicates (N = 2). The values given represent GC-yields estimated via peak areas. Product formation of compound 1–3 was performed indirectly based on the formation of benzyl alcohol and benzaldehyde, respectively. [a] Diester: 12%; [b] aldehyde: 29%; [c] aldehyde: 23%; [d] aldehyde: 19%; [e] aldehyde: 16%; [f] aldehyde: 25%; [g] aldehyde: 21%; [h] starting from racemate, ee was not determined; [i] starting from racemate, E < 48; [j] starting from racemate, E < 75; [k] starting from racemate, E < 61; [l] background subtracted.

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