Enhanced synthesis of l - threo -3,4-dihydroxyphenylserine by high-density whole-cell biocatalyst of recombinant l -threonine aldolase from Streptomyces avelmitilis |
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| Authors: | Sang-Ho Baik and Hideki Yoshioka |
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| Affiliation: | (1) Department of Food Science and Human Nutrition, Chonbuk National University, Jeonju, Jeonbuk, 561-756, South Korea;(2) Research Institute of Human Ecology, Chonbuk National University, Jeonju, Jeonbuk, 561-756, South Korea;(3) NITE Biological Resource Center (NBRC), National Institute of Technology and Evaluation (NITE), 2-5-8 Kazusa-Kamatari, Kisarazu-shi Chiba, 292-0818, Japan |
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| Abstract: | l-threo-3,4-Dihydroxyphenylserine (DOPS) is a chiral unnatural β-hydroxy amino acid used for the treatment of Parkinson disease. We developed a continuous bioconversion system for DOPS production that uses whole-cell biocatalyst of recombinant Escherichia coli expressing l-threonine aldolase (l-TA) genes cloned from Streptomyces avelmitilis MA-4680. Maximum conversion rates were observed at 2 M glycine, 145 mM 3,4-dihydroxybenzaldehyde, 0.75% Triton-X, 5 g E. coli cells/l, pH 6.5 and 10°C. In the optimized condition, overall productivity was 8 g/l, which represents 40 times the synthesis yield possible with no optimization of conditions. |
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| Keywords: | β -Hydroxy amino acid font-variant:small-caps" >l-threo-2,3-Dihydroxyphenylserine font-variant:small-caps" >l-Threonine aldolase Whole-cell conversion |
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