synthesis |
the soluble expression of is improved in Escherichia coli through N-terminal modification, but the cell biomass is decreased. When a variant carrying an additional glycine in position 3 is fused with three N-terminus histidine residues, the volumetric activity is increased by 3.1 times and the biomass is not significant change compared with the wild type. When the N-terminal disordered region of DAAO (HSQK) is replaced with HHHG, the variant enzyme activity reaches 80.7 U/ml in a 7.5 l fermenter in 24 h |
Rhodotorula toruloides |