Sunday, July 29, 2007
P123

Comparison of various b-carotene monooxygenase for retinal biosynthesis of metabolically engineered E. coli

Hee-Kyoung Ryu1, Hye-Min Park1, Hee-Jung Jang1, Sang-Hwal Yoon1, Sook-Hee Lee1, Eun-Gyeong Lee1, Chong-Long Wang1, Ji-Seon Park1, Amitabha Das1, Deok-Kun Oh2, and Seon-Won Kim1. (1) Division of Applied Life Science, Gyeongsang National University, 900 Gajwadong, Jinju, 660-701, South Korea, (2) Department of Bioscience and Biotechnology, Konkuk University, seoul, 143-503, South Korea

Retinal and its derivatives represent essential compounds in many biological systems. In animals, they are synthesized through a symmetrical cleavage of β-carotene catalyzed by a monooxygenase. We have cloned β-carotene 15,15'-monooxygenase genes from 4 bacteria of Synechococcus elongatus, Salinibacter ruber, Natronomonas pharaonis and Halobacterium salinarium and 2 vertebrates of Homo sapiens and Mus musculus. We also synthesized an artificial E. coli codon optimized gene, based on the amino acid sequence of blh gene of uncultured marine bacterium 66A03. The β-carotene 15,15'-monooxygenase expression in E. coli engineered to produce β-carotene led to accumulation of retinal at the expense of β-carotene. Retinal production of 2.2mg/L was obtained in recombinant E. coli harboring blh, monooxygenase genes of H. salinarium while the other monooxygenase genes cloned here produced trace amount of retinal. The highest retinal amount of 8.9 mg/L was produced by the artificial E. coli codon optimized monooxygenase genes.

 This work was supported by the EB-NCRC (Grant No. R15-2003-012-02001-0), BioGreen 21 Program (Grant No. 2005041034590), Brain Pool program and BK21 program of Korea.


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