Engineering microbial factories for synthesis of value-added products

Du, Jing; Shao, Zengyi; Zhao, Huimin

doi:10.1007/s10295-011-0970-3

Cited by 221 publications

(129 citation statements)

References 146 publications

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“…Biological synthesis of phytochemicals using Escherichia coli has been widely studied (11)(12)(13). Biological synthesis provides both regioselectivity and stereoselectivity, which are difficult to achieve using chemical synthesis.…”

mentioning

confidence: 99%

Synthesis of Flavonoid O -Pentosides by Escherichia coli through Engineering of Nucleotide Sugar Pathways and Glycosyltransferase

Han

Kim

Yoon

et al. 2014

Appl Environ Microbiol

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Plants produce two flavonoid O-pentoses, flavonoid O-xyloside and flavonoid O-arabinoside. However, analyzing their biological properties is difficult because flavonoids are not naturally produced in sufficient quantities. In this study, Escherichia coli was used to synthesize the plant-specific flavonoid O-pentosides quercetin 3-O-xyloside and quercetin 3-O-arabinoside. Two strategies were used. First, E. coli was engineered to express components of the biosynthetic pathways for UDP-xylose and UDP-arabinose. For UDP-xylose biosynthesis, two genes, UXS (UDP-xylose synthase) from Arabidopsis thaliana and ugd (UDP-glucose dehydrogenase) from E. coli, were overexpressed. In addition, the gene encoding ArnA (UDP-L-Ara4N formyltransferase/UDPGlcA C-4؆-decarboxylase), which competes with UXS for UDP-glucuronic acid, was deleted. For UDP-arabinose biosynthesis, UXE (UDP-xylose epimerase) was overexpressed. Next, we engineered UDP-dependent glycosyltransferases (UGTs) to ensure specificity for UDP-xylose and UDP-arabinose. The E. coli strains thus obtained synthesized approximately 160 mg/liter of quercetin 3-O-xyloside and quercetin 3-O-arabinoside.

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confidence: 99%

Synthesis of Flavonoid O -Pentosides by Escherichia coli through Engineering of Nucleotide Sugar Pathways and Glycosyltransferase

Han

Kim

Yoon

et al. 2014

Appl Environ Microbiol

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“…Over the last few years, the growing challenge has been the setup of industrial-scale conversion of cellulosic biomass into fermentable sugars, which can in turn be used as raw material for the production of biofuels and other biobased high-value-added products (2,10,24,26,35,47,50,55). The main bottleneck in the utilization of lignocellulosic plant material as a renewable energy source alternative to fossil fuels lies in the recalcitrance of this biomaterial to hydrolysis (15,41).…”

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confidence: 99%

Cellulose Degradation by Sulfolobus solfataricus Requires a Cell-Anchored Endo-β-1-4-Glucanase

2012

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A sequence encoding a putative extracellular endoglucanase (sso1354) was identified in the complete genome sequence of Sulfolobus solfataricus. The encoded protein shares signature motifs with members of glycoside hydrolases family 12. After an unsuccessful first attempt at cloning the full-length coding sequences in Escherichia coli, an active but unstable recombinant enzyme lacking a 27-residue N-terminal sequence was generated. This 27-amino-acid sequence shows significant similarity with corresponding regions in the sugar binding proteins AraS, GlcS, and TreS of S. solfataricus that are responsible for anchoring them to the plasma membrane. A strategy based on an effective vector/host genetic system for Sulfolobus and on expression control by the promoter of the S. solfataricus gene which encodes the glucose binding protein allowed production of the enzyme in sufficient quantities for study. In fact, the enzyme expressed in S. solfataricus was stable and highly thermoresistant and showed optimal activity at low pH and high temperature. The protein was detected mainly in the plasma membrane fraction, confirming the structural similarity to the sugar binding proteins. The results of the protein expression in the two different hosts showed that the SSO1354 enzyme is endowed with an endo-␤-1-4-glucanase activity and specifically hydrolyzes cellulose. Moreover, it also shows significant but distinguishable specificity toward several other sugar polymers, such as lichenan, xylan, debranched arabinan, pachyman, and curdlan.

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“…Recently, the stilbene resveratrol was biosynthesized at high yields (2.3 g/L) by an E. coli strain [114] that was genetically engineered to enhance the production of malonyl-CoA to increase the supply of malonyl-CoA, which is used to synthesize fatty acids (see [115] for a review). Such metabolic engineering may further improve production.…”

Section: Polyphenolsmentioning

confidence: 99%

Development of bio-based fine chemical production through synthetic bioengineering

et al. 2014

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Engineering microbial factories for synthesis of value-added products

Cited by 221 publications

References 146 publications

Synthesis of Flavonoid O -Pentosides by Escherichia coli through Engineering of Nucleotide Sugar Pathways and Glycosyltransferase

Synthesis of Flavonoid O -Pentosides by Escherichia coli through Engineering of Nucleotide Sugar Pathways and Glycosyltransferase

Cellulose Degradation by Sulfolobus solfataricus Requires a Cell-Anchored Endo-β-1-4-Glucanase

Development of bio-based fine chemical production through synthetic bioengineering

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