Engineering Escherichia coli for selective geraniol production with minimized endogenous dehydrogenation

Zhou, Jia; Wang, Chonglong; Yoon, Sang-Hwal; Jang, Hui-Jeong; Choi, Eui‐Sung; Kim, Seon-Won

doi:10.1016/j.jbiotec.2013.11.009

Cited by 90 publications

(83 citation statements)

References 35 publications

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“…Then, geraniol production keeps relatively stable till 32h of culture. Considering that geraniol could be dehydrogenated and transformed into other geranoids in E. coli by YjgB, geranoids were analyzed by GC-MS. 12 Geranial, the oxidative product of geraniol, was detected after 6h of culture, while nerol, the cis-isomer of geraniol, was detected after 24h of culture in this study. Geraniol, geranial and nerol formations were sequentially observed during culture, which is consistent with the geranoid formation mechanism that geranial and nerol are formed via geraniol as proposed by Iijima et al 16 and Zhou et al 12,16 Moreover, considering the mechanism of phosphatase, it is hard to form nerol and geranial directly from GPP, Figure 1.…”

Section: Resultsmentioning

confidence: 40%

“…Geraniol production was not detected during 48h of culture by strain LWG10, though geraniol formation via endogenous dephosphorylation of GPP has been observed in E. coli with supplementation of mevalonate, which bearing both GPPS mutated form E. coli and bottom portion of MVA pathway. 12 The failure of geraniol production by strain LWG10 might be ascribed to that the supply of GPP by whole MVA pathway from glucose was lower than by the bottom portion of MVA pathway from mevalonate and the low native PhoA catalytic activity limited the conversion of GPP to geraniol in E. coli.…”

Section: Resultsmentioning

confidence: 99%

“…9 Moreover, geraniol formation via endogenous dephosphorylation of GPP has been observed in engineered E. coli and yeast. 11,12 But, whether and which phosphatases can transform GPP to geraniol has remained unanswered up till now. The catalysis ability of phosphatases toward geraniol formation was investigated in this study, and it will show a new option for geraniol biosynthesis.…”

Section: Introductionmentioning

confidence: 99%

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Utilization of alkaline phosphatase PhoA in the bioproduction of geraniol by metabolically engineered Escherichia coli

et al. 2015

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Geraniol is a valuable acyclic monoterpene alcohol and has many applications in the perfume industries, pharmacy and others. It has been hypothesized that phosphatases can convert geranyl diphosphate (GPP) into geraniol. However, whether and which phosphatases can transform GPP to geraniol has remained unanswered up till now. In this paper, the catalysis abilities of 4 different types of phosphatases were studied with GPP as substrate in vitro. They are bifunctional diacylglycerol diphosphate phosphatase (DPP1) and lipid phosphate phosphatase (LPP1) from Saccharomyces cerevisiae, ADP-ribose pyrophosphatase (NudF) and alkaline phosphatase (PhoA) from Escherichia coli. The results show that just PhoA from E. coli can convert GPP into geraniol. Moreover, in order to confirm the ability of PhoA in vivo, the heterologous mevalonate pathway and geranyl diphosphate synthase gene from Abies grandis were co-overexpressed in E. coli with PhoA gene and 5.3 § 0.2 mg/l geraniol was produced from glucose in flask-culture. Finally, we also evaluated the fed-batch fermentation of this engineered E. coli and a maximum concentration of 99.3 mg/l geraniol was produced while the conversion efficiency of glucose to geranoid (gram to gram) was 0.51%. Our results offer a new option for geraniol biosynthesis and promote the industrial bio-production of geraniol.

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Section: Resultsmentioning

confidence: 40%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Utilization of alkaline phosphatase PhoA in the bioproduction of geraniol by metabolically engineered Escherichia coli

et al. 2015

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“…The acetylation of geraniol is known to be catalyzed by the promiscuous activity of chloramphenicol acetytransfrase (Zhou et al, 2014), which is included as a selection marker on the booster plasmid that we used. We should be able to significantly reduce this activity by simply exchanging the selection marker of pMEV-GPPS-idi for the kanamycin resistance gene.…”

Section: Discussionmentioning

confidence: 99%

“…Geraniol can be dehydrogenated (Zhou et al, 2014), isomerized (Akhila, 1985), reduced (Fischer et al, 2013), or acetylated (Zhou et al, 2014), in E. coli to yield various geraniol-derived compounds. Our culture also contained a variety of geraniol-related compounds (Figs.…”

Section: Accumulation Of Geraniol-derived Compoundsmentioning

confidence: 99%

Directed evolution and expression tuning of geraniol synthase for efficient geraniol production in <i>Escherichia coli</i>

Tashiro

Fujii

Kawai-Noma

et al. 2017

J. Gen. Appl. Microbiol.

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Whole‐cell biocatalysis: Advancements toward the biosynthesis of fuels

Madavi

Chauhan

Keshri

et al. 2021

Biofuels Bioprod Bioref

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The availability of robust microbial systems has facilitated the implementation of greener technology replacing existing less sustainable chemical technologies. Whole-cell biocatalysis has empowered the biological production of chemicals and biofuels, replacing labor-intensive traditional chemical catalysis. Whole-cell biocatalysis offers new avenues to use sustainable raw/waste biomass as a substrate for biotransformation into industrially important compounds. Using a native or nonnative microbial cell system as a chassis for developing a suitable cell catalyst requires multiple-level adjustments owing to the target product. Enzymes, the critical entity of biocatalysis, are an important factor influencing biocatalysis efficiency; whole cells provide optimal conditions to the enzymes or enzyme cascades for maximum productivity. Advancements in system biology and metabolic engineering techniques have led to the rational design of whole-cell catalysts for the suitable production of green fuels. Traditional enzyme catalysts are limited by issues such as enzyme stability and repeatability, laborious downstream processing and enzyme production technicalities, but whole-cell biocatalysis could bypass those bottlenecks. Thus, the application of whole cells in the catalysis and production of fuels has progressed greatly in the past couple of decades. This review focuses on detailing the concept of whole-cell biocatalysis and its advances in the production of biofuels such as alcohols and fatty acidbased, terpenoid-derived and carbon-free fuels. The technical advancements in various hosts such as Escherichia coli, Saccharomyces cerevisiae, Corynebacterium glutamicum and Synechococcus elongatus to establish whole-cell biocatalysis are summarized. In addition, system engineering toward the optimum production of various biofuels is added to the discussion.

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Engineering Escherichia coli for selective geraniol production with minimized endogenous dehydrogenation

Cited by 90 publications

References 35 publications

Utilization of alkaline phosphatase PhoA in the bioproduction of geraniol by metabolically engineered Escherichia coli

Utilization of alkaline phosphatase PhoA in the bioproduction of geraniol by metabolically engineered Escherichia coli

Directed evolution and expression tuning of geraniol synthase for efficient geraniol production in <i>Escherichia coli</i>

Whole‐cell biocatalysis: Advancements toward the biosynthesis of fuels

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