Sunday, July 26, 2009
P125

Vanillin Production Enhanced by Substrate Channeling in Recombinant E. coli

Jong-Wook Song1, Eun-Gyeong Lee1, Sang-Hwal Yoon1, Sook-Hee Lee1, Jung-Min Lee2, Seung-Goo Lee2, and Seon-Won Kim1. (1) Gyeongsang National University, Division of Applied Life Science (BK21), EB-NCRC and PMBBRC, Jinju 660-701, Korea, Jinju, South Korea, (2) Kribb, Systems Microbiology Research Center, Daejeon 305-806, Korea, Daejeon, South Korea

Vanillin (3-methoxy-4-hydroxybenzaldehyde) is quantitatively one of the most widely used aromatic molecules, particularly in food but also in the pharmaceutical, beverage and fragrance industries. Moreover, vanillin has antimicrobial and antioxidant properties. Conversion of ferulic acid to vanillin is a two step process, catalyzed by feruloyl-CoA synthase encoded by fcs and enoyl-CoA hydratase/aldolase encoded by ech, with the formation of feruloyl-CoA as an intermediate. Substrate channeling approach was performed by dimer formation between leucine- zippers of Fcs and Ech, in order to channelize feruloyl-CoA from Fcs to Ech and thereby increase vanillin production from recombinant Escherichia coli. E. coli harboring a plasmid pTBE-FP forming an efficient dimer of Bait-Ech and Fcs-Prey, produced 2.1 g/L of vanillin at an initial ferulic acid concentration of 3 g/L for 30 hours of culture, which was improved by 2.3-fold from vanillin production of 0.9 g/L of control strain harboring pTAHEF with no leucine-zipper. This result suggests that the E. coli strain harboring pTBE-FP is a potential strain for enhancing vanillin production by substrate channeling. This work was supported by the 21C Frontier Microbial Genomics and Applications Center Program, EB-NCRC (Grant No. R15-2003-012-02001-0), and BK21 program of Korea.

See more of Poster Session 1
See more of Posters

See more of The Annual Meeting and Exhibition 2009 (July 26 - 30, 2009)