Increased availability of NADH in metabolically engineered baker’s yeast improves transaminase-oxidoreductase coupled asymmetric whole-cell bioconversion

Table 2 Specific biocatalyst activities and stereo-selectivities

Strain	Description	Specific whole-cell transamination activity^a (µmol (S)-1-PEA/h/od)	ee (R)-phenylethylamine (%)	Specific whole-cell reduction activity^b (µmol ACP/h/od)	ee (S)-1-phenylethanol (%)	Specific SADH activity in cell extract (mU/mg total protein)
TMB4140	Empty plasmid	0	0	n.a.	n.a.	11 ± 3
TMB4144	Empty plasmid, gpd1Δgpd2Δ	0	0	n.a.	n.a.	n.a.
TMB4160	SADH	0	0	n.a.	>99 %	846 ± 76
TMB4161	SADH, gpd1Δgpd2Δ	0	0	n.a.	>99 %	380 ± 34
TMB4162	VAMT and SADH	2.4 ± 0.6	3.6 ± 0.1	45.7 ± 1.3	>99 %	248 ± 37
TMB4163	VAMT and SADH, gpd1Δgpd2Δ	7.5 ± 0.6	21.7 ± 1.0	138.1 ± 2.1	>99 %	511 ± 37

Mean values and standard deviations are calculated from two different whole-cell bioconversions
ee at the end of the reaction
^a First 4 h of whole-cell bioconversion of rac-1-phenylethylamine to acetophenone
^b First 4 h of whole-cell bioconversion of acetophenone to (S)-1-phenylethanol

ISSN: 1475-2859