| Products/Services Used | Details | Operation |
|---|---|---|
| Codon Optimization | … S50513.1) and R. capsulatus (NCBI accession No. AF022932.1) were codon-optimized and synthesized by GenScript Corporation (Nanjing, China). The tyrosine phenol-lyase genes were cloned into the vector pET-28a with restriction sites BamHI/HindIII under T7/lac promoter … | Get A Quote |
L-tyrosine is an amino acid that has been widely used in the food, agriculture and pharmaceutical industries. In order to screen a tyrosine phenol-lyase (TPL) with excellent catalytic performance for L-tyrosine production, TPL genes from Citrobacter freundii (CfTPL), Erwinia herbicola (EhTPL) and Rhodobacter capsulatus (TutA) were codon-optimized and overexpressed in Escherichia coli. The results showed that EhTPL had the highest whole cell catalysis activity and tyrosine yield (3-fold that of CfTPL). The results of RT-qPCR and a stability analysis also revealed that EhTPL had a higher transcriptional level in whole cell catalysis, while CfTPL possessed greater stability. Conditions for the production by whole ... More
