Efficient synthesis of 5-hydroxymethyl-2-furancarboxylic acid by Escherichia coli overexpressing aldehyde dehydrogenases

Zhang, Xueying; Ou, Xiao‐Yang; Fu, Yi-Jing; Zong, Min‐Hua; Li, Ning

doi:10.1016/j.jbiotec.2019.11.007

Cited by 40 publications

(35 citation statements)

References 40 publications

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“…G. oxydans DSM 50049 and C. testosteroni SC1588 enabled similar selective oxidations as P. putida KT2440. Certain membrane bound enzyme was presumably suggested responsible for this reaction in G. oxydans DSM 50049 (Sayed et al, 2019 ), while several aldehyde dehydrogenase from C. testosteroni SC1588 were identified for the oxidation of furanic aldehydes into corresponding furancarboxylic acids in E. coli (Zhang X. Y. et al, 2020 ). In our research, based on genome annotation and sequence alignment, several candidate genes of P. putida KT2440 were selected and their functions in FAL oxidation were assessed through gene disruption.…”

Section: Resultsmentioning

confidence: 99%

“…On the contrary, there is a limited amount of researches aiming at identification and characterization of the relevant enzymes. The 3-succinoylsemialdehyde-pyridine dehydrogenase and vanillin dehydrogenase from C. testosteroni SC1588 enabled recombinant E. coli to oxidize FAL and HMF into FA and HMFCA, respectively (Shi et al, 2019 ; Zhang X. Y. et al, 2020 ), which was likely due to the wide substrate scope of 3-succinoylsemialdehyde-pyridine dehydrogenase and vanillin dehydrogenase instead of their main physiological functions in vivo . The enzyme responsible for furanic aldehydes oxidation seems intriguing to unravel both in vivo and in vitro .…”

Section: Resultsmentioning

confidence: 99%

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Selective Biosynthesis of Furoic Acid From Furfural by Pseudomonas Putida and Identification of Molybdate Transporter Involvement in Furfural Oxidation

Zheng

Tan

et al. 2020

Front. Chem.

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Upgrading of furanic aldehydes to their corresponding furancarboxylic acids has received considerable interest recently. Herein we reported selective oxidation of furfural (FAL) to furoic acid (FA) with quantitative yield using whole-cells of Pseudomonas putida KT2440. The biocatalytic capacity could be substantially promoted through adding 5-hydroxymethylfurfural into media at the middle exponential growth phase. The reaction pH and cell dosage had notable impacts on both FA titer and selectivity. Based on the validation of key factors for FAL conversion, the capacity of P. putida KT2440 to produce FAL was substantially improved. In batch bioconversion, 170 mM FA was produced with selectivity nearly 100% in 2 h, whereas 204 mM FA was produced with selectivity above 97% in 3 h in fed-batch bioconversion. Particularly, the role of molybdate transporter in oxidation of FAL and 5-hydroxymethylfurfural was demonstrated for the first time. The furancarboxylic acids synthesis was repressed markedly by destroying molybdate transporter, which implied Mo-dependent enzyme/molybdoenzyme played pivotal role in such oxidation reactions. This research further highlights the potential of P. putida KT2440 as next generation industrial workhorse and provides a novel understanding of molybdoenzyme in oxidation of furanic aldehydes.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Selective Biosynthesis of Furoic Acid From Furfural by Pseudomonas Putida and Identification of Molybdate Transporter Involvement in Furfural Oxidation

Zheng

Tan

et al. 2020

Front. Chem.

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“…Because of the high toxicity of HMF, an appropriate co-substrate has proved to be crucial for enhancing the biosynthesis performance of bacteria (Shi et al, 2019;Zhang et al, 2020). The effects of co-substrates on BHMF synthesis were shown in Table 1.…”

Section: Effects Of Co-substrates On Bhmf Synthesismentioning

confidence: 99%

“…Biocatalysis is emerging as an additional pillar for green and clean valorization of HMF, due to increased chemical and regional selectivity as well as mild reaction conditions in aqueous environments (Cang et al, 2019;Wang et al, 2019). Biocatalytic reduction of HMF to BHMF with whole cells is still a great challenge because the substrate HMF is a well-known potent inhibitor to microorganisms (Shi et al, 2019;Zhang et al, 2020). Thus, the reported on biocatalytic synthesis of BHMF from HMF remain limited in the literature.…”

Section: Introductionmentioning

confidence: 99%

Improved Bio-Synthesis of 2,5-bis(hydroxymethyl)furan by Burkholderia contaminans NJPI-15 With Co-substrate

Chang

et al. 2021

Front. Chem.

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Upgrading of biomass derived 5-hydroxymethylfurfural (HMF) has attracted considerable interest recently. A new highly HMF-tolerant strain of Burkholderia contaminans NJPI-15 was isolated in this study, and the biocatalytic reduction of HMF into 2,5-bis(hydroxymethyl)furan (BHMF) using whole cells was reported. Co-substrate was applied to improve the BHMF yield and selectivity of this strain as well as HMF-tolerant level. The catalytic capacity of the cells can be substantially improved by Mn2+ ion. The strain exhibited good catalytic performance at a pH range of 6.0–9.0 and a temperature range of 25°C–35°C. In addition, 100 mM HMF could be reduced to BHMF by the B. contaminans NJPI-15 resting cells in presence of 70 mM glutamine and 30 mM sucrose, with a yield of 95%. In the fed-batch strategy, 656 mM BHMF was obtained within 48 h, giving a yield of 93.7%. The reported utilization of HMF to produce BHMF is a promising industrially sound biocatalytic process.

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“…Due to their high reactivity, these biobased furans could be readily reduced to value-added furan alcohols such as BHMF and furfuryl alcohol ( Li et al, 2016 ; He et al, 2018 ; Hu et al, 2018 ; Petri et al, 2018 ; Yan et al, 2019 ; Zhang et al, 2019 ; Amarasekara et al, 2020 ), important building blocks in polymer, food, and pharmaceutical industries. Recently, our group has focused our attention on biocatalytic valorization of biobased furans ( Qin et al, 2015 ; Li et al, 2017 ; Zhang et al, 2017 ; Jia et al, 2019b ; Zhang et al, 2020a ; Wang et al, 2020 ; Wen et al, 2020 ). To continue our interest in the furan upgrading, the reduction of HMF was used as the model reaction for evaluating the ADH activities of the engineered enzymes.…”

Section: Introductionmentioning

confidence: 99%

Engineering Promiscuous Alcohol Dehydrogenase Activity of a Reductive Aminase AspRedAm for Selective Reduction of Biobased Furans

et al. 2021

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Catalytic promiscuity is a promising starting point for improving the existing enzymes and even creating novel enzymes. In this work, site-directed mutagenesis was performed to improve promiscuous alcohol dehydrogenase activity of reductive aminase from Aspergillus oryzae (AspRedAm). AspRedAm showed the cofactor preference toward NADPH in reductive aminations, while it favored NADH in the reduction reactions. Some key amino acid residues such as N93, I118, M119, and D169 were identified for mutagenesis by molecular docking. Variant N93A showed the optimal pH and temperature of 8 and 30°C, respectively, in the reduction of 5-hydroxymethylfurfural (HMF). The thermostability was enhanced upon mutation of N93 to alanine. The catalytic efficiency of variant N93A (kcat/Km, 23.6 mM−1 s−1) was approximately 2-fold higher compared to that of the wild-type (WT) enzyme (13.1 mM−1 s−1). The improved catalytic efficiency of this variant may be attributed to the reduced steric hindrance that stems from the smaller side chain of alanine in the substrate-binding pocket. Both the WT enzyme and variant N93A had broad substrate specificity. Escherichia coli (E. coli) cells harboring plain vector enabled selective reduction of biobased furans to target alcohols, with the conversions of 35–95% and the selectivities of >93%. The introduction of variant N93A to E. coli resulted in improved substrate conversions (>98%) and selectivities (>99%).

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Efficient synthesis of 5-hydroxymethyl-2-furancarboxylic acid by Escherichia coli overexpressing aldehyde dehydrogenases

Cited by 40 publications

References 40 publications

Selective Biosynthesis of Furoic Acid From Furfural by Pseudomonas Putida and Identification of Molybdate Transporter Involvement in Furfural Oxidation

Selective Biosynthesis of Furoic Acid From Furfural by Pseudomonas Putida and Identification of Molybdate Transporter Involvement in Furfural Oxidation

Improved Bio-Synthesis of 2,5-bis(hydroxymethyl)furan by Burkholderia contaminans NJPI-15 With Co-substrate

Engineering Promiscuous Alcohol Dehydrogenase Activity of a Reductive Aminase AspRedAm for Selective Reduction of Biobased Furans

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