Human tryptophan hydroxylase 2 (hTPH2) serves as the rate-limiting enzyme in the synthesis of serotonin. Studies have shown that the removing of the N-terminal 150 amino acids significantly enhances the solubility of hTPH2, allowing for high yield of soluble protein. To investigate the role of recombinant gut microbiota in the regulation of serotonin production, human tryptophan hydroxylase 2 (hTPH2) was cloned into two bacterial strains, namely Lactobacillus plantarum and Escherichia coli Bl21. The gene sequence for an N-terminal deletion mutant of hTPH2 was placed in an IPTG-inducible expression cassette and used to express the target protein. Both stains demonstrated successful production of the target product following thorough analysis using electrophoresis, western blotting and chromatography (FPLC) techniques. These findings suggest the potential for microbiome engineering aimed at investigating alterations in microbial communities and their impact on health.
