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Production of 12-hydroxy dodecanoic acid methyl ester using a signal peptide sequence-optimized transporter AlkL and a novel monooxygenase.
Yoo, Hee-Wang; Kim, Joonwon; Patil, Mahesh D; Park, Beom Gi; Joo, Sung-Yeon; Yun, Hyungdon; Kim, Byung-Gee.
Affiliation
  • Yoo HW; Interdisciplinary Program of Bioengineering, Seoul National University, Seoul 08826, Republic of Korea; Institute of Molecular Biology and Genetics, Seoul National University, Seoul 08826, Republic of Korea.
  • Kim J; Institute of Molecular Biology and Genetics, Seoul National University, Seoul 08826, Republic of Korea; School of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of Korea.
  • Patil MD; Department of Systems Biotechnology, Konkuk University, Seoul, Republic of Korea.
  • Park BG; Institute of Molecular Biology and Genetics, Seoul National University, Seoul 08826, Republic of Korea; School of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of Korea.
  • Joo SY; Institute of Molecular Biology and Genetics, Seoul National University, Seoul 08826, Republic of Korea; School of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of Korea.
  • Yun H; Department of Systems Biotechnology, Konkuk University, Seoul, Republic of Korea.
  • Kim BG; Interdisciplinary Program of Bioengineering, Seoul National University, Seoul 08826, Republic of Korea; Institute of Molecular Biology and Genetics, Seoul National University, Seoul 08826, Republic of Korea; School of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of
Bioresour Technol ; 291: 121812, 2019 Nov.
Article in En | MEDLINE | ID: mdl-31376668
ABSTRACT
In this study, a signal peptide of AlkL was replaced with other signal peptides to improve the soluble expression and thereby facilitate the transport of dodecanoic acid methyl ester (DAME) substrate into the E. coli. Consequently, AlkL with signal peptide FadL (AlkLf) showed higher transport activity toward DAME. Furthermore, the promoter optimization for the efficient heterologous expression of the transporter AlkLf and alkane monooxygenase (AlkBGT) system was conducted and resulted in increased ω-oxygenation activity of AlkBGT system. Moreover, bioinformatic studies led to the identification of novel monooxygenase from Pseudomonas pelagia (Pel), which exhibited 20% higher activity towards DAME as substrate compared to AlkB. Finally, the construction of a chimeric transporter and the expression of newly identified monooxygenase enabled the production of 44.8 ±â€¯7.5 mM of 12-hydroxy dodecanoic acid methyl ester (HADME) and 31.8 ±â€¯1.7 mM of dodecanedioic acid monomethyl ester (DDAME) in a two-phase reaction system.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Membrane Transport Proteins / Metabolic Engineering Language: En Journal: Bioresour Technol Journal subject: ENGENHARIA BIOMEDICA Year: 2019 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Membrane Transport Proteins / Metabolic Engineering Language: En Journal: Bioresour Technol Journal subject: ENGENHARIA BIOMEDICA Year: 2019 Document type: Article