Recent Advances in Enzymatic Catalysis for Preparation of High Value-Added Chemicals from Carbon Dioxide

doi:10.6023/A19060240

Acta Chimica Sinica ›› 2019, Vol. 77 ›› Issue (11): 1099-1114.DOI: 10.6023/A19060240 Previous Articles Next Articles

Review

酶法催化二氧化碳制备高附加值化学品研究进展

梁珊, 宗敏华, 娄文勇*()

华南理工大学食品科学与工程学院应用生物催化实验室广州 510640

投稿日期:2019-07-01 发布日期:2019-08-23
通讯作者: 娄文勇 E-mail:wylou@scut.edu.cn
作者简介:梁珊, 博士, 2017年毕业于暨南大学, 获工学硕士学位, 2018年进入华南理工大学应用生物催化实验室攻读博士学位, 硕士期间曾赴加拿大萨斯喀彻温大学访问交流.研究方向为新型纳米材料固定化酶及其应用生物催化, 致力于CO₂的高效捕获和转化|宗敏华, 教授, 博士生导师, 1988年博士毕业于华南理工大学, 1990~1991年在日本京都大学进修, 华南理工大学生物转化与营养工程团队负责人、广州市优秀女科技工作者, 兼任教育部化学与化工学科教学指导委员会委员, 享受国务院颁发的政府特殊津贴, 主要从事生物催化与转化方面的基础和应用研究工作|娄文勇, 教授, 博士生导师, 全国百篇优秀博士学位论文、国家优秀青年基金获得者, 入选广东省特支计划百千万工程领军人才及教育部新世纪优秀人才支持计划. 2005年毕业于华南理工大学生物化工专业, 获博士学位, 英国华威大学访问学者.现为华南理工大学食品科学与工程学院副院长, 研究方向为生物合成与应用生物催化, 主要聚焦于溶剂工程、生物催化剂的筛选与改造、酶固定化技术、生物质的高效利用与转化等方面的基础及应用研究工作
基金资助:
国家自然科学基金(21676104);国家自然科学基金(21878105);国家重点研发计划(2018YFC1603400);国家重点研发计划(2018YFC1602100);广州市科技计划项目(201904010360)

Recent Advances in Enzymatic Catalysis for Preparation of High Value-Added Chemicals from Carbon Dioxide

Liang Shan, Zong Minhua, Lou Wenyong*()

Laboratory of Applied Biocatalysis, School of Food Science and Engineering, South China University of Technology, Guangzhou 510640

Received:2019-07-01 Published:2019-08-23
Contact: Lou Wenyong E-mail:wylou@scut.edu.cn
Supported by:
the National Natural Science Foundation of China(21676104);the National Natural Science Foundation of China(21878105);the National Key R&D Program of China(2018YFC1603400);the National Key R&D Program of China(2018YFC1602100);the Science and Technology Program of Guangzhou(201904010360)

With the rapid development of modern industry, coal, petroleum, natural gas and other fossil fuels have been excessively consumed, along with an increasing large quantities of greenhouse gases (e.g. carbon dioxide, CO₂) are produced. It is urgent to develop sustainable green energy and abate the detriment of carbon dioxide on global environment. CO₂ is a cheap carbon source that can be converted into high value-added chemicals by chemical, photochemical, electrochemical or enzymatic methods to realize the recycling of CO₂. It is a win-win strategy to solve the energy and environmental crisis caused by global carbon emissions. Inspired by natural CO₂ metabolic process, enzymatic transformation provides an alternative strategy for efficient recycling of CO₂. Compared with traditional chemical, photochemical or electrochemical methods, the enzymatic route holds advantages of green, high efficiency, mild and excellent selectivity, which is expected to bring new revolutionary opportunities for efficient utilization of CO₂. Thus, in this present review, we firstly introduce the brief background about enzymatic conversion for CO₂ capture, sequestration and utilization. Next, we depict six major routes of the CO₂ metabolic process in cells, which are taken as the inspiration source for the construction of enzymatic systems in vitro. Subsequently, recent advances in enzymatic conversion of CO₂ that catalyzed by various single enzymes and multi-enzyme cascade systems are systematically reviewed. Some emerging approaches for construction of immobilized single-or multi-enzyme systems, directed evolution and artificial modification of enzymes, and cofactor regulation during the enzymatic processes are also discussed. Finally, the defects and shortcomings of enzymatic approaches are summarized, and the future perspectives are finally put forward. Based on this present review, we aim to provide theoretical reference and practical basis for more efficient enzymatic utilization of CO₂ to produce high value-added chemicals.

Key words: CO₂, enzymatic conversion, high value conversion, reduction, cascade catalysis, energy, environment

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Liang Shan, Zong Minhua, Lou Wenyong. Recent Advances in Enzymatic Catalysis for Preparation of High Value-Added Chemicals from Carbon Dioxide[J]. Acta Chimica Sinica, 2019, 77(11): 1099-1114.

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Fig. & Tab. 10

Figure 1. (A) A comparison of global different greenhouse gases emissions[4]; (B) Global CO2 emissions in different countries (including the European Union) from 1970 to 2018[6]

Figure 2. Schematics of CO2 metabolic process in cells. (A) Calvin cycle; (B) Reductive citric acid cycle; (C) Reductive acetyl-CoA route; (D) 3-Hydroxypropionate bi-cycle; (E) Dicarboxylate/4-hydroxybutyrate cycle (a) and 3-hydroxypropionate/4-hydroxybutyrate cycle (b) [7, 18~20]

Figure 3. Nitrogenase MoFe cofactor with some key amino acid residues; (B) CH4 formation as a function of time with natural or remodeled MoFe proteins; (C) The relationship between propylene formation and C2H2 partial pressure that catalyzed by α-70Ala/α-195Gln MoFe protein[39]; (D) Metabolic routes of CH4 production by R. palustris expressing wild-type Fe-only nitrogenase: electrons are originated from oxidation of thiosulfate (a) or acetate (b), and CO2 are generated from bicarbonate (a) or the oxidation of acetate (b)[41]; (E) In vitro reduction of CO2 to CO by vnfH or NifH in different forms[42]

Figure 4. (A) Depiction of the crystal structures of CA from different families, a~d represent the types of α, β, γ and ζ, respectively[45]; (B) Schematic illustration of heterologously expressed CA for promoting CaCO3 formation[54]; (C) CA stability enhancement by direct evolution: (a) Compounded fold improvement after each round of evolution; (b) The storage stability of DvCA8.0 (8 rounds evolution) when exposed to 4.2 mol/L MDEA[56]; (D) Diagrams showing the immobilization of carbonic anhydrase: (a) Dendronized polymer-CA conjugates; (b) Lipid bilayer membranes-conjugated CA[57, 59, 60]

Figure 5. (A) Sketch of FDH for catalysis of CO2 to produce HCOOH and the reverse reaction[64]; (B) The active site of the Mo-FDH in two views: focusing on the sulfido (a) and Cys196 (b) groups, respectively[66]; (C) CCGCMAQSP catalyzed arti?cial photosynthesis of HCOOH from CO2 and the photoregeneration of NADH under visible light; (D) Photocatalytic activities of various catalysts for synthesis of HCOOH from CO2 in the NADH photoregeneration system (a. Yield of NADH; b. HCOOH production)[73]; (E) Photocatalytic activities of BODIPY, CCG-BODIPY, NH2-TPP and CCG-NH-TPP (a. Yield of NADH; b. HCOOH production)[75]

Figure 6. (A) Ball-and-stick drawing of the active site of [NiFe]CODH; (B) Mechanism for reduction of CO2 to CO by [NiFe]CODH[79]; (C) [NiFe]CODH anchored on a pyrolytic graphite "edge" electrode for catalysis of rapid conversion of CO2 to CO[80]; (D) Schematic illustration of the CO2 photoreduction system using [NiFe]CODH attached to a Ru-based semiconductor photocatalyst[76]

Figure 7. (A) Biocatalytic carboxylation of epoxides with CO2 by the cell extracts or whole-cell of Xanthobacter Py2; (B) (a) Carboxylation of phenol by cell extracts of Thauera aromatica or partially purified phenylesterase; (b) Regioselective para-carboxylation of non-activated phenolic compounds catalyzed by whole-cell of Clostridium hydroxybenzoicum; (C) Carboxylation of pyrrole with CO2 by pyrrole-2-carboxylate decarboxylase; (D) Carboxylation of acetaldehyde with CO2 by pyruvate decarboxylase[85~87, 89~91]

Figure 8. (A) Schematic diagram of NADH-mediated multi-dehydrogenases (FDH, FaldDH and ADH) for cascade catalysis of CO2 to produce methanol[16, 104]; (B) (a) Capsules-in-bead scaffold for construction of multienzyme cascade system; (b) Plot of methanol formation as a function of reaction time in various enzymatic catalytic systems [102]; (C) Multienzyme cascade system based on ultrathin hybrid microcapsule for conversion of CO2 to methanol[103]

Figure 9. (A) Schematic representation of enzymatic synthesis of methanol from CO2 with in situ regeneration of NADH (GDH: glutamate dehydrogenase)[105]; (B) (a) Schematic illustration of coaxial electrospinning for construction of cationic polyelectrolyte-doped hollow nanofiber tethering of NADH for methanol synthesis from CO2; (b) Plots of methanol yield as a function of reaction time for methanol synthesis from CO2 by using different multienzyme systems (Open legends represent results from free multienzyme systems, and the filled legends represent results from the hollow nanofiber-supported multienzymes systems, respectively)[106]; (C) Schematic illustration of reduction of CO2 into methanol using multi-enzymatic cascade system with NADH regeneration by PTDH (a); Time profile of methanol production (b) and total turnover number (c) by multi-enzymatic cascade reactions (blue: ClFDH+BmFaldDH+YADH with PTDH and EMIM-Ac (1%); red: ClFDH+BmFaldDH+YADH with PTDH; purple: CbFDH+BmFaldDH+YADH with PTDH; green: ClFDH+PpFaldDH+YADH with PTDH; black: CbFDH+PpFaldDH+YADH with PTDH)[107]

Figure 10. Intracellular multi-enzymatic synthesis of isobutyraldehyde from CO2 in an engineering cyanobacterium Synechococcus elongatus PCC7942. (A) The pathway for isobutyraldehyde production. Isobutyraldehyde production as a function of time by cyanobacteria SA590 (B), and SA665 with enhanced Rubisco (C), respectively[110]

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酶法催化二氧化碳制备高附加值化学品研究进展

Recent Advances in Enzymatic Catalysis for Preparation of High Value-Added Chemicals from Carbon Dioxide

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