Enzymatic synthesis of <scp>L</scp>‐lactic acid from carbon dioxide and ethanol with an inherent cofactor regeneration cycle

Tong, Xiaodong; El‐Zahab, Bilal; Zhao, Xueyan; Liu, Youyan; Wang, Ping

doi:10.1002/bit.22938

Cited by 64 publications

(46 citation statements)

References 59 publications

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“…The unique internal cofactor regeneration cycle in this synthetic route can eliminate the need for additional reagents or energy for cofactor regeneration. Up to 41% in terms of ethanol conversion can be achieved in a batch reaction, while a turnover number of 2.2 day −1 was reached for cofactor regeneration with continuous ethanol feeding [87]. Scheme 7.…”

Section: Carboxylation Of Aliphatic Substratesmentioning

confidence: 99%

“…Recently, a new multienzyme reaction system was investigated for L-lactic acid production, which is used in food, cosmetic, pharmaceutical, and chemical industries, from carbon dioxide and ethanol (shown in Scheme 7) [87]. The unique internal cofactor regeneration cycle in this synthetic route can eliminate the need for additional reagents or energy for cofactor regeneration.…”

Section: Carboxylation Of Aliphatic Substratesmentioning

confidence: 99%

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Recent Progress and Novel Applications in Enzymatic Conversion of Carbon Dioxide

et al. 2017

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Turning carbon dioxide (CO 2 ) into fuels and chemicals using chemical, photochemical, electrochemical, and enzymatic methods could be used to recycle large quantities of carbon. The enzymatic method, which is inspired by cellular CO 2 metabolism, has attracted considerable attention for efficient CO 2 conversion due to improved selectivity and yields under mild reaction conditions. In this review, the research progress of green and potent enzymatic conversion of CO 2 into useful fuels and chemicals was discussed. Furthermore, applications of the enzymatic conversion of CO 2 to assist in CO 2 capture and sequestration were highlighted. A summary including the industrial applications, barriers, and some perspectives on the research and development of the enzymatic approach to convert CO 2 were introduced.

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Section: Carboxylation Of Aliphatic Substratesmentioning

confidence: 99%

Section: Carboxylation Of Aliphatic Substratesmentioning

confidence: 99%

Recent Progress and Novel Applications in Enzymatic Conversion of Carbon Dioxide

et al. 2017

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“…Biological CO 2 fixation is one of the most important approaches to solving these problems. Enzymatic CO 2 reduction has been examined extensively as a promising approach to greenhouse gas fixation and the production of renewable fuels and chemicals [1]–[3]. The enzymatic reduction of CO 2 using FDHs has been widely studied for the production of valuable chemicals, such as formic acid and methanol [4], [5].…”

Section: Introductionmentioning

confidence: 99%

“…pyruvate decarboxylase (EC 4.1.1.1), carbonic anhydrase (EC 4.2.1.1), and FDH (EC 1.2.1.2). Pyruvate decarboxylase can catalyze the reversible conversion of pyruvate into CO 2 and acetaldehyde and thus requires equimolar acetaldehyde for the conversion of CO 2 into pyruvate [3]. It should be noted that carbonic anhydrase can catalyze the rapid interconversion of CO 2 and bicarbonate but this is not a real CO 2 reduction reaction but a CO 2 hydration reaction [12], [13].…”

Section: Introductionmentioning

confidence: 99%

Efficient CO2-Reducing Activity of NAD-Dependent Formate Dehydrogenase from Thiobacillus sp. KNK65MA for Formate Production from CO2 Gas

et al. 2014

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NAD-dependent formate dehydrogenase (FDH) from Candida boidinii (CbFDH) has been widely used in various CO2-reduction systems but its practical applications are often impeded due to low CO2-reducing activity. In this study, we demonstrated superior CO2-reducing properties of FDH from Thiobacillus sp. KNK65MA (TsFDH) for production of formate from CO2 gas. To discover more efficient CO2-reducing FDHs than a reference enzyme, i.e. CbFDH, five FDHs were selected with biochemical properties and then, their CO2-reducing activities were evaluated. All FDHs including CbFDH showed better CO2-reducing activities at acidic pHs than at neutral pHs and four FDHs were more active than CbFDH in the CO2 reduction reaction. In particular, the FDH from Thiobacillus sp. KNK65MA (TsFDH) exhibited the highest CO2-reducing activity and had a dramatic preference for the reduction reaction, i.e., a 84.2-fold higher ratio of CO2 reduction to formate oxidation in catalytic efficiency (k cat/K B) compared to CbFDH. Formate was produced from CO2 gas using TsFDH and CbFDH, and TsFDH showed a 5.8-fold higher formate production rate than CbFDH. A sequence and structural comparison showed that FDHs with relatively high CO2-reducing activities had elongated N- and C-terminal loops. The experimental results demonstrate that TsFDH can be an alternative to CbFDH as a biocatalyst in CO2 reduction systems.

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“…In recent years, the regeneration of the bio-electron donor NADH from NAD has been the topic of many studies relevant to biofuels [1], rechargeable batteries [2, 3] and bioreactors [4, 5]. The electrocatalytic reduction of NAD is more difficult than the electrocatalytic oxidation of NADH on the electrode surface [6-8].…”

Section: Introductionmentioning

confidence: 99%

In situ regeneration of NADH via lipoamide dehydrogenase-catalyzed electron transfer reaction evidenced by spectroelectrochemistry

Tam

Chen

Lei

et al. 2012

Bioelectrochemistry

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NAD/NADH is a coenzyme found in all living cells, carrying electrons from one reaction to another. We report on characterizations of in situ regeneration of NADH via lipoamide dehydrogenase (LD)-catalyzed electron transfer reaction to regenerate NADH using UV-vis spectroelectrochemistry. The Michaelis-Menten constant (Km) and maximum velocity (Vmax) of NADH regeneration were measured as 0.80 ± 0.15 mM and 1.91 ± 0.09 μM s-1 in a 1-mm thin-layer spectroelectrochemical cell using gold gauze as the working electrode at the applied potential -0.75 V (vs. Ag/AgCl). The electrocatalytic reduction of the NAD system was further coupled with the enzymatic conversion of pyruvate to lactate by lactate dehydrogenase to examine the coenzymatic activity of the regenerated NADH. Although the reproducible electrocatalytic reduction of NAD into NADH is known to be difficult compared to the electrocatalytic oxidation of NADH, our spectroelectrochemical results indicate that the in situ regeneration of NADH via LD-catalyzed electron transfer reaction is fast and sustainable and can be potentially applied to many NAD/NADH-dependent enzyme systems.

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Enzymatic synthesis of L‐lactic acid from carbon dioxide and ethanol with an inherent cofactor regeneration cycle

Cited by 64 publications

References 59 publications

Recent Progress and Novel Applications in Enzymatic Conversion of Carbon Dioxide

Recent Progress and Novel Applications in Enzymatic Conversion of Carbon Dioxide

Efficient CO2-Reducing Activity of NAD-Dependent Formate Dehydrogenase from Thiobacillus sp. KNK65MA for Formate Production from CO2 Gas

In situ regeneration of NADH via lipoamide dehydrogenase-catalyzed electron transfer reaction evidenced by spectroelectrochemistry

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