Development of an Escherichia coli whole cell biocatalyst for the production of hyperoside.

Objective: To produce high concentrations of hyperoside from quercetin using recombinant Escherichia coli with in situ regeneration of UDP-galactose.

Results: Sucrose synthase from Glycine max (GmSUS) was co-expressed with UDP-glucose epimerase from E. coli (GalE) in E.

Combined Biosynthetic Pathway Engineering and Storage Pool Expansion for High-Level Production of Ergosterol in Industrial .

Ergosterol, a terpenoid compound produced by fungi, is an economically important metabolite serving as the direct precursor of steroid drugs. Herein, ergsosterol biosynthetic pathway modification combined with storage capacity enhancement was proposed to synergistically improve the production of ergosterol in . strain S1 accumulated the highest amount of ergosterol [7.

Engineering a heterologous synthetic pathway in Escherichia coli for efficient production of biotin.

Objective: To enhance biotin production in Escherichia coli by engineering a heterologous biotin synthetic pathway.

Results: Biotin operon genes from Pseudomonas putida, which consisted of a bioBFHCD cluster and a bioA gene, was engineered into Escherichia coli for biotin production. The introduction of bioW gene from Bacillus subtilis, encoding pimeloyl-CoA synthetase and sam2 gene from Saccharomyces cerevisiae, encoding S-adenosyl-L-methionine (SAM) synthetase contributed to the heterologous production of biotin in recombinant E.

Increased productivity of L-2-aminobutyric acid and total turnover number of NAD/NADH in a one-pot system through enhanced thermostability of L-threonine deaminase.

Objective: To strengthen NADH regeneration in the biosynthesis of L-2-aminobutyric acid (L-ABA).

Results: L-Threonine deaminase (L-TD) from Escherichia coli K12 was modified by directed evolution and rational design to improve its endurance to heat treatment. The half-life of mutant G323D/F510L/T344A at 42 °C increased from 10 to 210 min, a 20-fold increase compared to the wild-type L-TD, and the temperature at which the activity of the enzyme decreased by 50% in 15 min increased from 39 to 53 °C.