AI Article Synopsis
- The study replaced the signal peptide of AlkL with other options to boost its ability to transport dodecanoic acid methyl ester (DAME) into E. coli, finding that the FadL signal peptide improved transport activity.
- Promoter optimization enhanced the heterologous expression of AlkL and the alkane monooxygenase system (AlkBGT), leading to greater ω-oxygenation activity.
- Bioinformatics identified a new monooxygenase from Pseudomonas pelagia with 20% higher activity towards DAME, and combining this with a chimeric transporter yielded significant production of 12-hydroxy dodecanoic acid methyl ester (HADME) and dodecanedioic acid mon
Article 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 (AlkL) showed higher transport activity toward DAME. Furthermore, the promoter optimization for the efficient heterologous expression of the transporter AlkL 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 ± 7.5 mM of 12-hydroxy dodecanoic acid methyl ester (HADME) and 31.8 ± 1.7 mM of dodecanedioic acid monomethyl ester (DDAME) in a two-phase reaction system.
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| http://dx.doi.org/10.1016/j.biortech.2019.121812 | DOI Listing |
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