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Highly Efficient Biosynthesis of Heliotropin by Engineered Escherichia coli Coexpressing Trans-Anethole Oxygenase and Formate Dehydrogenase
journal contribution
posted on 2019-12-10, 21:29 authored by Peng Wen, Dan Wu, Pu Zheng, Pengcheng Chen, Siqin Liu, Yin FuHeliotropin, a compound with important roles in the spice
and fragrance
industries and broad application prospects, is mainly produced through
chemical methods. Here, we established a novel process for the synthesis
of heliotropin by Escherichia coli whole
cells through biotransformation of isosafrole. Directed evolution
and high-throughput screening based on 2,4-dinitrophenylhydrazine
were used to improve the activity of trans-anethole oxygenase toward
isosafrole, and a mutant (TAO3G2) was obtained that had
a high ability to oxidize isosafrole. Formate dehydrogenase (FDH)
and TAO3G2 were coexpressed in E. coli, significantly increasing the catalytic efficiency by regenerating
more NADH to promote isosafrole oxidation. Furthermore, after optimizing
the molar ratio of isosafrole to the auxiliary substrate, the final
concentration of heliotropin was increased from 9.15 to 19.45 g/L,
and the maximum yield and space-time yield reached 96.02% and 3.89
g/L/h, respectively. These results suggest that the biosynthesis of
heliotropin should have excellent industrial application value.
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NADHheliotropinfragrance industriesisosafrole oxidationEscherichia colimolar ratiohigh-throughput screeningoxidize isosafroleFDHTAO 3 G 2application prospectstrans-anethole oxygenaseEngineered Escherichia coli Coexpressing Trans-Anethole OxygenaseEfficient BiosynthesisFormate Dehydrogenase Heliotropinnovel processapplication valueFormate dehydrogenasechemical methods
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