Prakash Parajuli

TL;DR: All the manipulations/engineering accomplished on the microorganisms since 2000 are described in detail along with the biosynthetic pathway enzymes, their sources, structures of the compounds, and yield of each product.

TL;DR: The acceptor substrate promiscuity of YjiC, a UDP-glycosyltransferase from Bacillus licheniformis, was explored with seven different classes of flavonoids and the enzymatic bioconversion was significantly higher with the production of multiple glucosylated derivatives.

TL;DR: Biotransformation of 7,8-DHF in a grown-induced culture of E. coli BL21 (DE3) harboring the recombinant pET-28a-SpOMT2884 stoichiometrically converted 7-hydroxy-8-methoxyflavone, suggesting that methylation enhances the stability of substrate and glycosylation has proved to increase the water solubility.

TL;DR: In this article, a UDP glucosyltransferase from Bacillus licheniformis was overexpressed, purified, and incubated with nucleotide diphosphate (NDP) d- and l-sugars to produce glucose, galactose, 2-deoxyglucose, viosamine, rhamnose, and fucose sugar-conjugated resveratrol glycosides.

TL;DR: The in vivo fermentation of the isoflavonoids by applying engineered E. coli BL21(DE3)/ΔpgiΔzwfΔushA overexpressing phosphoglucomutase (pgm) and glucose 1-phosphate uridyltransferase (galU), along with YjiC, found more than 60% average conversion of 200 μM of supplemented is oflavonoid glucosides, without any additional UDP-α