C12Y101/01282

Bioproduction of phenethyl alcohol, aldehyde, acid, amine, and related compounds

This invention relates to the bioproduction of substituted or unsubstituted phenylacetaldehyde, 2-phenylethanol, phenylacetic acid or phenylethylamine by subjecting a starting material comprising glucose, L-phenylalanine, substituted L-phenylalanine, styrene or substituted styrene to a plurality of enzyme catalyzed chemical transformations in a one-pot reaction system, using recombinant microbial cells overexpressing the enzymes. To produce phenylacetaldehyde from styrene, the cells are modified to overexpress styrene monooxygenase (SMO) and styrene oxide isomerase (SOI). To produce phenylacetic acid from styrene, SMO, SOI and aldehyde dehydrogenase are overexpressed. Alternatively, to produce 2-phenylethanol, SMO, SOI and aldehyde reductase or alcohol dehydrogenase are overexpressed, while to produce phenylethylamine, SMO, SOI and transaminase are overexpressed.

BIOPRODUCTION OF PHENETHYL ALCOHOL, ALDEHYDE, ACID, AMINE, AND RELATED COMPOUNDS

This invention relates to the bioproduction of substituted or unsubstituted phenylacetaldehyde, 2-phenylethanol, phenylacetic acid or phenylethylamine by subjecting a starting material comprising glucose, L-phenylalanine, substituted L-phenylalanine, styrene or substituted styrene to a plurality of enzyme catalyzed chemical transformations in a one-pot reaction system, using recombinant microbial cells overexpressing the enzymes. To produce phenylacetaldehyde from styrene, the cells are modified to overexpress styrene monooxygenase (SMO) and styrene oxide isomerase (SOI). To produce phenylacetic acid from styrene, SMO, SOI and aldehyde dehydrogenase are overexpressed. Alternatively, to produce 2-phenylethanol, SMO, SOI and aldehyde reductase or alcohol dehydrogenase are overexpressed, while to produce phenylethylamine, SMO, SOI and transaminase are overexpressed.

Recombinant Escherichia coli for Producing Chlorogenic Acid and Application Thereof
20240327880 · 2024-10-03 ·

The present disclosure provides a recombinant Escherichia coli for producing chlorogenic acid and application thereof. In the present disclosure, tyrosine ammonia-lyase FjTAL derived from Flavobacterium johnsoniae, hpaBC derived from E. coli, 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase mutant aroG.sup.fbr, chorismate mutase tyrC derived from Zymomonas mobilis, quinic acid/shikimate-5 dehydrogenase ydiB derived from E. coli, hydroxycinnamoyl CoA:quinic acid transferase NtHQT derived from Nicotiana tabacum, and 4-coumarate:CoA ligase At4CL1 derived from Arabidopsis thaliana are expressed in the recombinant E. coli, thereby constructing a chlorogenic acid biosynthesis pathway in E. coli. Then, the aroB gene and gldA gene derived from E. coli are overexpressed, and an endogenous gene menI is knocked out from the recombinant E. coli. The recombinant strain produced chlorogenic acid by fermentation at a titer of up to 638.2 mg/L in a shake flask or at a titer of 2.8 g/L in a 5-L fermenter.