State-of-the-art for alcohol dehydrogenase development and the prospect of its applications in bio-based furan compounds valorization

LIU Xiangshi; WU Yilu; ZHAN Peng; HUANG Tianhao; CAI Di; QIN Peiyong

doi:10.12211/2096-8280.2023-059

您当前的位置：

首页 >

文章列表页 >

State-of-the-art for alcohol dehydrogenase development and the prospect of its applications in bio-based furan compounds valorization

Invited Review | 更新时间：2025-03-20

- State-of-the-art for alcohol dehydrogenase development and the prospect of its applications in bio-based furan compounds valorization
- Synthetic Biology Journal Vol. 4, Issue 6, Pages: 1122-1139(2023)
- 作者机构：
  
  1.北京化工大学，国家能源生物炼制研发中心，北京 100029
  2.北京化工大学，生命科学与技术学院，北京 100029
- 作者简介：
- 基金信息：
- DOI：10.12211/2096-8280.2023-059
  CLC： Q554+.1
- Received：21 August 2023，
  
  Revised：2023-10-17，
  
  Published：31 December 2023
- 稿件说明：
移动端阅览
刘庠诗，吴奕禄，詹鹏，黄天灏，蔡的，秦培勇. 醇脱氢酶的研究进展及其催化增值生物基呋喃化合物前景展望［J］. 合成生物学， 2023， 4（6）： 1122-1139

LIU Xiangshi， WU Yilu， ZHAN Peng， HUANG Tianhao， CAI Di， QIN Peiyong. State-of-the-art for alcohol dehydrogenase development and the prospect of its applications in bio-based furan compounds valorization［J］. Synthetic Biology Journal， 2023， 4（6）： 1122-1139
刘庠诗，吴奕禄，詹鹏，黄天灏，蔡的，秦培勇. 醇脱氢酶的研究进展及其催化增值生物基呋喃化合物前景展望［J］. 合成生物学， 2023， 4（6）： 1122-1139 DOI： 10.12211/2096-8280.2023-059.

LIU Xiangshi， WU Yilu， ZHAN Peng， HUANG Tianhao， CAI Di， QIN Peiyong. State-of-the-art for alcohol dehydrogenase development and the prospect of its applications in bio-based furan compounds valorization［J］. Synthetic Biology Journal， 2023， 4（6）： 1122-1139 DOI： 10.12211/2096-8280.2023-059.

摘要

醇脱氢酶（alcohol dehydrogenase， ADH）广泛存在于生物体内，可应用于多种有机物选择性氧化还原。近年来，随着对酶的催化机理、结构认知、分子改造和反应系统构建及强化等方面研究的逐渐深入，ADH在生物基平台化合物的高选择性催化氧化还原方面展现出巨大潜力。本文综述了ADH分子设计和定向改造的前沿技术和进展，面向常见的辅因子依赖性ADH催化过程中的辅因子高成本及稳定性差等局限，聚焦酶反应过程中的辅因子再生强化技术，梳理了适用于ADH催化系统的化学驱动、酶驱动和光电驱动辅因子再生路径，并从单酶催化体系开发、多酶协同催化系统挖掘、全细胞催化技术发展与应用等多个角度概述了ADH在催化生物基呋喃化合物方向的最新研究进展。随着对ADH应用潜力的进一步挖掘，未来ADH有望成为生物基呋喃增值工业化进程中的重要组成部分，为能源生产的绿色发展提供助力。

Abstract

Alcohol dehydrogenase (ADH) is found widely in living cells

where it catalyzes the oxidation or reduction between hydroxyl group and carbonyl group. It also catalyzes redox reactions of a variety of organic compounds with high selectivity. In recent years

with the research progress of the catalytic mechanism

structural information

molecular modification

and reaction systems

ADH has shown great promise in the highly selective catalysis of various bio-based platform compounds. One example is the oxidation or reduction of furan derivatives such as furfural and 5-hydroxymethylfurfural

which are important sustainable building blocks for bio-jet fuels and biomaterials that are derived from tandem hydrolysis

isomerization

and dehydration of hemicelluloses and celluloses fractions in lignocellulose matrixes. This review focuses on the cutting-edge technologies in molecular design and directional engineering of ADH. In addition

the intensification of cofactor regeneration processes

including chemical-driven

enzyme-driven

and photo/electricity-driven pathways were also summarized. These methods could be the solutions to the negative aspects

such as expensive cost

poor stability

and the poor circulating efficiency of the nicotinamide cofactors that are indispensable assisted in typical ADH catalysis process. Moreover

the latest research progresses of ADH in catalysis of bio-based furans platform chemicals were also discussed. Apart from using ADH solely for the activation of the hydroxyl and carbonyl groups in the biobased furan derivates and the production of oxidative and reductive products

there is also of great promise in cascade ADH catalysis and other chemical or biological ca

talysis processes in one-pot under relatively mild conditions to valorize the furan derivates into valuable fine chemicals. Meanwhile

the whole-cell catalytic process that involves ADH and

in vivo

cofactors regeneration also possesses potentials in biobased furans valorization

with the advantages of low catalyst loading and processing costs. Overall

the researches of ADH in catalysis biological furans valorization has entered a new stage. With the further exploration of the potential applications of ADH

its role in the transformation of biomass resources will be increasingly important

particularly in the industrial process in the future.

关键词

Keywords

references

DONG J J , FERNÁNDEZ-FUEYO E , HOLLMANN F , et al . Biocatalytic oxidation reactions: a chemist's perspective [J ] . Angewandte Chemie International Edition , 2018 , 57 ( 30 ): 9238 - 9261 .

MAGOMEDOVA Z , GRECU A , SENSEN C W , et al . Characterization of two novel alcohol short-chain dehydrogenases/reductases from Ralstonia eutropha H16 capable of stereoselective conversion of bulky substrates [J ] . Journal of Biotechnology , 2016 , 221 : 78 - 90 .

SHANMUGANATHAN S , NATALIA D , GREINER L , et al . Oxidation-hydroxymethylation-reduction: a one-pot three-step biocatalytic synthesis of optically active α-aryl vicinal diols [J ] . Green Chemistry , 2012 , 14 ( 1 ): 94 - 97 .

STAMPFER W , KOSJEK B , MOITZI C , et al . Biocatalytic asymmetric hydrogen transfer [J ] . Angewandte Chemie International Edition , 2002 , 41 ( 6 ): 1014 - 1017 .

VELASCO-LOZANO S , ROCHA-MARTIN J , FAVELA-TORRES E , et al . Hydrolysis and oxidation of racemic esters into prochiral ketones catalyzed by a consortium of immobilized enzymes [J ] . Biochemical Engineering Journal , 2016 , 112 : 136 - 142 .

VOSS C V , GRUBER C C , FABER K , et al . Orchestration of concurrent oxidation and reduction cycles for stereoinversion and deracemisation of sec-alcohols [J ] . Journal of the American Chemical Society , 2008 , 130 ( 42 ): 13969 - 13972 .

VOSS C V , GRUBER C C , KROUTIL W . Deracemization of secondary alcohols through a concurrent tandem biocatalytic oxidation and reduction [J ] . Angewandte Chemie International Edition , 2008 , 47 ( 4 ): 741 - 745 .

KOCHIUS S , MAGNUSSON A O , HOLLMANN F , et al . Immobilized redox mediators for electrochemical NAD(P) + regeneration [J ] . Applied Microbiology and Biotechnology , 2012 , 93 ( 6 ): 2251 - 2264 .

BURNETT J W H , CHEN H , LI J W , et al . Supported Pt enabled proton-driven NAD(P) + regeneration for biocatalytic oxidation [J ] . ACS Applied Materials & Interfaces , 2022 , 14 ( 18 ): 20943 - 20952 .

LIU W F , WANG P . Cofactor regeneration for sustainable enzymatic biosynthesis [J ] . Biotechnology Advances , 2007 , 25 ( 4 ): 369 - 384 .

NISHIGAKI J I , ISHIDA T , HONMA T , et al . Oxidation of β-nicotinamide adenine dinucleotide (NADH) by Au cluster and nanoparticle catalysts aiming for coenzyme regeneration in enzymatic glucose oxidation [J ] . ACS Sustainable Chemistry & Engineering , 2020 , 8 ( 28 ): 10413 - 10422 .

WU H , TIAN C Y , SONG X K , et al . Methods for the regeneration of nicotinamidecoenzymes [J ] . Green Chemistry , 2013 , 15 ( 7 ): 1773 - 1789 .

许松伟 , 姜忠义 , 吴洪 . 醇脱氢酶结构和作用机理研究进展 [J ] . 有机化学 , 2005 , 25 ( 6 ): 629 - 633 .

XU S W , JIANG Z Y , WU H . Progress in structure and kinetic mechanism of alcohol dehydrogenase [J ] . Chinese Journal of Organic Chemistry , 2005 , 25 ( 6 ): 629 - 633 .

RADIANINGTYAS H , WRIGHT P C . Alcohol dehydrogenases from thermophilic and hyperthermophilic archaea and bacteria [J ] . FEMS Microbiology Reviews , 2003 , 27 ( 5 ): 593 - 616 .

FABER K . Biotransformations in Organic Chemistry [M/OL ] . Berlin, Heidelberg: Springer Berlin Heidelberg , 2004 [ 2023-07-01 ] . https://link.springer.com/book/10.1007/978-3-642-18537-3 https://link.springer.com/book/10.1007/978-3-642-18537-3 .

ZHANG Z B , MUSCHIOL J , HUANG Y H , et al . Efficient ionic liquid-based platform for multi-enzymatic conversion of carbon dioxide to methanol [J ] . Green Chemistry , 2018 , 20 ( 18 ): 4339 - 4348 .

李慧敏 , 李宁宁 , 翁建清 , 等 . 酶促还原过程中辅因子的再生研究 [J ] . 杭州师范大学学报(自然科学版) , 2019 , 18 ( 6 ): 605 - 609, 668 .

LI H M , LI N N , WENG J Q , et al . Regeneration of cofactors in enzymatic reduction [J ] . Journal of Hangzhou Normal University (Natural Science Edition) , 2019 , 18 ( 6 ): 605 - 609, 668 .

VAN DER DONK W A , ZHAO H M . Recent developments in pyridine nucleotide regeneration [J ] . Current Opinion in Biotechnology , 2003 , 14 ( 4 ): 421 - 426 .

吉爱国 , 高培基 . 烟酰胺类辅因子的保留和再生研究进展 [J ] . 药物生物技术 , 1997 , 4 ( 2 ): 122 - 128 .

JI A G , GAO P J . Advances in retention and regeneration of nicotinamide cofactors [J ] . Pharmaceutical Biotechnology , 1997 , 4 ( 2 ): 122 - 128 .

YEH A H W , NORN C , KIPNIS Y , et al . De novo design of luciferases using deep learning [J ] . Nature , 2023 , 614 ( 7949 ): 774 - 780 .

周柱 , 查凡 , 张琴 , 等 . Klebsiella sp.WL1316乙醇脱氢酶基因过表达提高乙醇生产效率 [J ] . 化学工程 , 2022 , 50 ( 10 ): 1 - 7 .

ZHOU Z , ZHA F , ZHANG Q , et al . Overexpression of alcohol dehydrogenase in Klebsiella sp. WL1316 to improve hydrogen production efficiency [J ] . Chemical Engineering (China) , 2022 , 50 ( 10 ): 1 - 7 .

HOLLMANN F , ARENDS I W C E , BUEHLER K . Biocatalytic redox reactions for organic synthesis: nonconventional regeneration methods [J ] . ChemCatChem , 2010 , 2 ( 7 ): 762 - 782 .

BORNSCHEUER U T , HUISMAN G W , KAZLAUSKAS R J , et al . Engineering the third wave of biocatalysis [J ] . Nature , 2012 , 485 ( 7397 ): 185 - 194 .

BÖTTCHER D , BORNSCHEUER U T . Protein engineering of microbial enzymes [J ] . Current Opinion in Microbiology , 2010 , 13 ( 3 ): 274 - 282 .

李寅 . 合成生物制造2022 [J ] . 生物工程学报 , 2023 , 39 ( 3 ): 807 - 841 .

LI Y . Biomanufacturing driven by engineered organisms (2022) [J ] . Chinese Journal of Biotechnology , 2023 , 39 ( 3 ): 807 - 841 .

曲戈 , 袁波 , 孙周通 . 工业蛋白质理性设计与应用 [J ] . 生物工程学报 , 2022 , 38 ( 11 ): 4068 - 4080 .

QU G , YUAN B , SUN Z T . Rational design and applications of industrial proteins [J ] . Chinese Journal of Biotechnology , 2022 , 38 ( 11 ): 4068 - 4080 .

韩旭 , 李倩 , 韦泓丽 , 等 . 工业应用导向的蛋白质结构与功能研究进展 [J ] . 生物工程学报 , 2022 , 38 ( 11 ): 4050 - 4067 .

HAN X , LI Q , WEI H L , et al . Application-oriented structure and function study of proteins: a review [J ] . Chinese Journal of Biotechnology , 2022 , 38 ( 11 ): 4050 - 4067 .

XU J L , ZHOU H S , YU H R , et al . Computational design of highly stable and soluble alcohol dehydrogenase for NADPH regeneration [J ] . Bioresources and Bioprocessing , 2021 , 8 : 12 .

MUSA M M , LOTT N , LAIVENIEKS M , et al . A single point mutation reverses the enantiopreference of Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase [J ] . ChemCatChem , 2009 , 1 ( 1 ): 89 - 93 .

ZIEGELMANN-FJELD K I , MUSA M M , PHILLIPS R S , et al . A Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase mutant derivative highly active and stereoselective on phenylacetone and benzylacetone [J ] . Protein Engineering , Design & Selection, 2007 , 20 ( 2 ): 47 - 55 .

FIORENTINO G , CANNIO R , ROSSI M , et al . Decreasing the stability and changing the substrate specificity of the Bacillus stearothermophilus alcohol dehydrogenase by single amino acid replacements [J ] . Protein Engineering, Design and Selection , 1998 , 11 ( 10 ): 925 - 930 .

GOIHBERG E , DYM O , TEL-OR S , et al . Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution [J ] . Proteins: Structure, Function, and Bioinformatics , 2008 , 72 ( 2 ): 711 - 719 .

WU Q A , ZONG M H , LI N . One-pot chemobiocatalytic production of 2,5-bis(hydroxymethyl)furan and its diester from biomass in aqueous media [J ] . ACS Catalysis , 2023 , 13 ( 14 ): 9404 - 9414 .

PHILLIPS R S . Tailoring the substrate specificity of secondary alcohol dehydrogenase [J ] . Canadian Journal of Chemistry , 2002 , 80 ( 6 ): 680 - 685 .

CAMPBELL E , WHEELDON I R , BANTA S . Broadening the cofactor specificity of a thermostable alcohol dehydrogenase using rational protein design introduces novel kinetic transient behavior [J ] . Biotechnology and Bioengineering , 2010 , 107 ( 5 ): 763 - 774 .

WULF H , MALLIN H , BORNSCHEUER U T . Protein engineering of a thermostable polyol dehydrogenase [J ] . Enzyme and Microbial Technology , 2012 , 51 ( 4 ): 217 - 224 .

ROSELL A , VALENCIA E , OCHOA W F , et al . Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase [J ] . Journal of Biological Chemistry , 2003 , 278 ( 42 ): 40573 - 40580 .

GOIHBERG E , PERETZ M , TEL-OR S , et al . Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms [J ] . Biochemistry , 2010 , 49 ( 9 ): 1943 - 1953 .

PIETRICOLA G , CHAMORRO L , CASTELLINO M , et al . Covalent immobilization of dehydrogenases on carbon felt for reusable anodes with effective electrochemical cofactor regeneration [J ] . ChemistryOpen , 2022 , 11 ( 11 ): e202200102 .

THOMPSON M P , TURNER N J . Two-enzyme hydrogen-borrowing amination of alcohols enabled by a cofactor-switched alcohol dehydrogenase [J ] . ChemCatChem , 2017 , 9 ( 20 ): 3833 - 3836 .

POIZAT M , ARENDS I W C E , HOLLMANN F . On the nature of mutual inactivation between[Cp*Rh(bpy)(H 2 O) ] 2+ and enzymes-analysis and potential remedies [J ] . Journal of Molecular Catalysis B: Enzymatic , 2010 , 63 ( 3/4 ): 149 - 156 .

CANIVET J , SÜSS-FINK G , ŠTĚPNIČKA P . Water-soluble phenanthroline complexes of rhodium, iridium and ruthenium for the regeneration of NADH in the enzymatic reduction of ketones [J ] . European Journal of Inorganic Chemistry , 2007 , 2007( 30 ): 4736 - 4742 .

曹礼梅 , 邱兆富 , 张巍 , 等 . 化工废催化剂污染特征及资源化途径 [J ] . 化工进展 , 2021 , 40 ( 10 ): 5293 - 5301 .

CAO L M , QIU Z F , ZHANG W , et al . Pollution and utilization of chemical industry spent catalysts [J ] . Chemical Industry and Engineering Progress , 2021 , 40 ( 10 ): 5293 - 5301 .

CHENAULT H K , WHITESIDES G M . Regeneration of nicotinamide cofactors for use in organic synthesis [J ] . Applied Biochemistry and Biotechnology , 1987 , 14 ( 2 ): 147 - 197 .

KOSJEK B , STAMPFER W , POGOREVC M , et al . Purification and characterization of a chemotolerant alcohol dehydrogenase applicable to coupled redox reactions [J ] . Biotechnology and Bioengineering , 2004 , 86 ( 1 ): 55 - 62 .

CAZELLES R , DRONE J , FAJULA F , et al . Reduction of CO 2 to methanol by a polyenzymatic system encapsulated in phospholipids-silica nanocapsules [J ] . New Journal of Chemistry , 2013 , 37 ( 11 ): 3721 - 3730 .

AKSU S , ARENDS I W C E , HOLLMANN F . A new regeneration system for oxidized nicotinamide cofactors [J ] . Advanced Synthesis & Catalysis , 2009 , 351 ( 9 ): 1211 - 1216 .

SINGH R K , SINGH R , SIVAKUMAR D , et al . Insights into cell-free conversion of CO 2 to chemicals by a multienzyme cascade reaction [J ] . ACS Catalysis , 2018 , 8 ( 12 ): 11085 - 11093 .

WANG Z J , CLARY K N , BERGMAN R G , et al . A supramolecular approach to combining enzymatic and transition metal catalysis [J ] . Nature Chemistry , 2013 , 5 ( 2 ): 100 - 103 .

TISHKOV V I , POPOV V O . Protein engineering of formate dehydrogenase [J ] . Biomolecular Engineering , 2006 , 23 ( 2/3 ): 89 - 110 .

JOHANNES T W , WOODYER R D , ZHAO H M . Efficient regeneration of NADPH using an engineered phosphite dehydrogenase [J ] . Biotechnology and Bioengineering , 2007 , 96 ( 1 ): 18 - 26 .

LOPEZ DE FELIPE F , KLEEREBEZEM M , DE VOS W M , et al . Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase [J ] . Journal of Bacteriology , 1998 , 180 ( 15 ): 3804 - 3808 .

WECKBECKER A , HUMMEL W . Glucose dehydrogenase for the regeneration of NADPH and NADH [M/OL ] //BARREDO J L. Microbial enzymes and biotransformations . Totowa, NJ: Humana Press, 2005 : 225 - 238 [2023-07-01] . https://link.springer.com/protocol/10.1385/1-59259-846-3:225 https://link.springer.com/protocol/10.1385/1-59259-846-3:225 .

RIEBEL B , GIBBS P , WELLBORN W , et al . Cofactor regeneration of NAD + from NADH: novel water-forming NADH oxidases [J ] . Advanced Synthesis & Catalysis , 2002 , 344 ( 10 ): 1156 - 1168 .

RIEBEL B , GIBBS P , WELLBORN W , et al . Cofactor regeneration of both NAD + from NADH and NADP + from NADPH: NADH oxidase from Lactobacillus sanfranciscensis [J ] . Advanced Synthesis & Catalysis , 2003 , 345 ( 6/7 ): 707 - 712 .

HUMMEL W , RIEBEL B . Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis [J ] . Biotechnology Letters , 2003 , 25 ( 1 ): 51 - 54 .

HUMMEL W , KUZU M , GEUEKE B . An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pured- tert -leucine [J ] . Organic Letters , 2003 , 5 ( 20 ): 3649 - 3650 .

GEUEKE B , RIEBEL B , HUMMEL W . NADH oxidase from Lactobacillus brevis : a new catalyst for the regeneration of NAD [J ] . Enzyme and Microbial Technology , 2003 , 32 ( 2 ): 205 - 211 .

JIANG R R , BOMMARIUS A S . Hydrogen peroxide-producing NADH oxidase (nox-1) from Lactococcus lactis [J ] . Tetrahedron: Asymmetry , 2004 , 15 ( 18 ): 2939 - 2944 .

HIRANO J I , MIYAMOTO K , OHTA H . Purification and characterization of thermostable H 2 O 2 -forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309 [J ] . Applied Microbiology and Biotechnology , 2008 , 80 ( 1 ): 71 - 78 .

HUANG L , SAYOGA G V , HOLLMANN F , et al . Horse liver alcohol dehydrogenase-catalyzed oxidative lactamization of amino alcohols [J ] . ACS Catalysis , 2018 , 8 ( 9 ): 8680 - 8684 .

NOWAK C , BEER B , PICK A , et al . A water-forming NADH oxidase from Lactobacillus pentosus suitable for the regeneration of synthetic biomimetic cofactors [J ] . Frontiers in Microbiology , 2015 , 6 : 957 .

JIA H Y , ZONG M H , ZHENG G W , et al . Myoglobin-catalyzed efficient in situ regeneration of NAD(P) + and their synthetic biomimetic for dehydrogenase-mediated oxidations [J ] . ACS Catalysis , 2019 , 9 ( 3 ): 2196 - 2202 .

JIA H Y , ZONG M H , YU H L , et al . Dehydrogenase-catalyzed oxidation of furanics: exploitation of hemoglobin catalytic promiscuity [J ] . ChemSusChem , 2017 , 10 ( 18 ): 3524 - 3528 .

LEE S H , CHOI D S , KUK S K , et al . Photobiocatalysis: activating redox enzymes by direct or indirect transfer of photoinduced electrons [J ] . Angewandte Chemie International Edition , 2018 , 57 ( 27 ): 7958 - 7985 .

MACIÁ-AGULLÓ J A , CORMA A , GARCIA H . Photobiocatalysis: the power of combining photocatalysis and enzymes [J ] . Chemistry-A European Journal , 2015 , 21 ( 31 ): 10940 - 10959 .

YANG D , ZOU H J , WU Y Z , et al . Constructing quantum Dots@Flake graphitic carbon nitride isotype heterojunctions for enhanced visible-light-driven NADH regeneration and enzymatic hydrogenation [J ] . Industrial & Engineering Chemistry Research , 2017 , 56 ( 21 ): 6247 - 6255 .

吕陈秋 , 姜忠义 , 王姣 . 烟酰型辅酶NAD(P) + 和NAD(P)H再生的研究进展 [J ] . 有机化学 , 2004 , 24 ( 11 ): 1366 - 1379 .

LÜ C Q , JIANG Z Y , WANG J . Progress in regeneration of NAD(P) + and NAD(P)H [J ] . Chinese Journal of Organic Chemistry , 2004 , 24 ( 11 ): 1366 - 1379 .

周一诺 , 杨楠 , 田瑶 , 等 . 基于辅因子的光驱动酶催化复合体系 [J ] . 科学通报 , 2020 , 65 ( 36 ): 4213 - 4222 .

ZHOU Y N , YANG N , TIAN Y , et al . Cofactor-based solar-driven enzymatic catalysis systems [J ] . Chinese Science Bulletin , 2020 , 65 ( 36 ): 4213 - 4222 .

LI S H , SHI J F , LIU S S , et al . Molecule-electron-proton transfer in enzyme-photo-coupled catalytic system [J ] . Chinese Journal of Catalysis , 2023 , 44 : 96 - 110 .

SÁNCHEZ-IGLESIAS A , CHUVILIN A , GRZELCZAK M . Plasmon-driven photoregeneration of cofactor molecules [J ] . Chemical Communications , 2015 , 51 ( 25 ): 5330 - 5333 .

YU S S , ZHANG S D , LI K N , et al . Furfuryl alcohol production with high selectivity by a novel visible-light driven biocatalysis process [J ] . ACS Sustainable Chemistry & Engineering , 2020 , 8 ( 42 ): 15980 - 15988 .

ZHAO H Q , QI Y N , ZHAN P , et al . Artificial photoenzymatic reduction of carbon dioxide to methanol by using electron mediator and co-factorassembled ZnIn 2 S 4 nanoflowers [J ] . ChemSusChem , 2023 , 16 ( 12 ): e202300061 .

JARVIS A G . Designer metalloenzymes for synthetic biology: enzyme hybrids for catalysis [J ] . Current Opinion in Chemical Biology , 2020 , 58 : 63 - 71 .

WANG Y Z , SUN J , ZHANG H H , et al . Tetra (4-carboxyphenyl) porphyrin for efficient cofactor regeneration under visible light and its immobilization [J ] . Catalysis Science & Technology , 2018 , 8 ( 10 ): 2578 - 2587 .

ZHU Q , ZHUANG Y , ZHAO H Q , et al . 2,5-Diformylfuran production by photocatalytic selective oxidation of 5-hydroxymethylfurfural in water using MoS 2 /CdIn 2 S 4 flower-like heterojunctions [J ] . Chinese Journal of Chemical Engineering , 2023 , 54 : 180 - 191 .

ZHUANG Y , ZHU Q , LI G Z , et al . Photocatalytic degradation of organic dyes using covalent triazine-based framework [J ] . Materials Research Bulletin , 2022 , 146 : 111619 .

WU Y Z , SHI J F , LI D L , et al . Synergy of electron transfer and electron utilization via metal-organic frameworks as an electron buffer tank for nicotinamide regeneration [J ] . ACS Catalysis , 2020 , 10 ( 5 ): 2894 - 2905 .

JI X Y , LIU C C , WANG J , et al . Integration of functionalized two-dimensional TaS 2 nanosheets and an electron mediator for more efficient biocatalyzed artificial photosynthesis [J ] . Journal of Materials Chemistry A , 2017 , 5 ( 11 ): 5511 - 5522 .

BROWN K A , WILKER M B , BOEHM M , et al . Photocatalytic regeneration of nicotinamide cofactors by quantum dot-enzyme biohybrid complexes [J ] . ACS Catalysis , 2016 , 6 ( 4 ): 2201 - 2204 .

HAFENSTINE G R , HARRIS A W , MA K , et al . Conversion of ethanol to 2-ethylhexenal at ambient conditions using tandem, biphasic catalysis [J ] . ACS Sustainable Chemistry & Engineering , 2017 , 5 ( 11 ): 10483 - 10489 .

TEOH W Y , SCOTT J A , AMAL R . Progress in heterogeneous photocatalysis: from classical radical chemistry to engineering nanomaterials and solar reactors [J ] . The Journal of Physical Chemistry Letters , 2012 , 3 ( 5 ): 629 - 639 .

LUTZ J , MOZHAEV V V , KHMELNITSKY Y L , et al . Preparative application of 2-hydroxybiphenyl 3-monooxygenase with enzymatic cofactor regeneration in organic-aqueous reaction media [J ] . Journal of Molecular Catalysis B: Enzymatic , 2002 , 19/20 : 177 - 187 .

DÉLÉCOULS-SERVAT K , BASSÉGUY R , BERGEL A . Membrane electrochemical reactor (MER): application to NADH regeneration for ADH-catalysed synthesis [J ] . Chemical Engineering Science , 2002 , 57 ( 21 ): 4633 - 4642 .

RUINATSCHA R , BUEHLER K , SCHMID A . Development of a high performance electrochemical cofactor regeneration module and its application to the continuous reduction of FAD [J ] . Journal of Molecular Catalysis B: Enzymatic , 2014 , 103 : 100 - 105 .

KIWI J . Photochemical generation of reduced β-nicotinamide-adenine dinucleotide (induced by visible light) [J ] . Journal of Photochemistry , 1981 , 16 ( 2 ): 193 - 202 .

WIENKAMP R , STECKHAN E . Selective generation of NADH by visible light [J ] . Angewandte Chemie International Edition , 1983 , 22 ( 6 ): 497 .

RODRÍGUEZ-HINESTROZA R A , LÓPEZ C , LÓPEZ-SANTÍN J , et al . HLADH-catalyzed synthesis of β-amino acids, assisted by continuous electrochemical regeneration of NAD + in a filter press microreactor [J ] . Chemical Engineering Science , 2017 , 158 : 196 - 207 .

ZHAN P , LIU X S , ZHU Q A , et al . Selective furfuryl alcohol production from furfural via bio-electrocatalysis [J ] . Catalysts , 2023 , 13 ( 1 ): 101 .

TOSSTORFF A , KRONER C , OPPERMAN D J , et al . Towards electroenzymatic processes involving old yellow enzymes and mediated cofactor regeneration [J ] . Engineering in Life Sciences , 2017 , 17 ( 1 ): 71 - 76 .

WANG X D , SABA T , YIU H H P , et al . Cofactor NAD(P)H regeneration inspired by heterogeneous pathways [J ] . Chem , 2017 , 2 ( 5 ): 621 - 654 .

CAHN J K B , WERLANG C A , BAUMSCHLAGER A , et al . A general tool for engineering the NAD/NADP cofactor preference of oxidoreductases [J ] . ACS Synthetic Biology , 2017 , 6 ( 2 ): 326 - 333 .

ZHAN P , LIU X S , ZHANG S D , et al . Electroenzymatic reduction of furfural to furfuryl alcohol by an electron mediator and enzyme orderly assembled biocathode [J ] . ACS Applied Materials & Interfaces , 2023 , 15 ( 10 ): 12855 - 12863 .

SON E J , LEE S H , KUK S K , et al . Carbon nanotube–graphitic carbon nitride hybrid films for flavoenzyme-catalyzed photoelectrochemical cells [J ] . Advanced Functional Materials , 2018 , 28 ( 24 ): 1705232 .

ZHANG J Z , CAI D , QIN Y L , et al . High value-added monomer chemicals and functional bio‐based materials derived from polymeric components of lignocellulose by organosolv fractionation [J ] . Biofuels, Bioproducts and Biorefining , 2020 , 14 ( 2 ): 371 - 401 .

JIA Q Q , TENG X N , YU S S , et al . Production of furfural from xylose and hemicelluloses using tin-loaded sulfonated diatomite as solid acid catalyst in biphasic system [J ] . Bioresource Technology Reports , 2019 , 6 : 145 - 151 .

LI N , ZONG M H . (Chemo)biocatalytic upgrading of biobased furanic platforms to chemicals, fuels, and materials: a comprehensive review [J ] . ACS Catalysis , 2022 , 12 ( 16 ): 10080 - 10114 .

BOZELL J J , PETERSEN G R . Technology development for the production of biobased products from biorefinery carbohydrates—the US Department of Energy's "Top 10" revisited [J ] . Green Chemistry , 2010 , 12 ( 4 ): 539 - 554 .

VAN PUTTEN R J , VAN DER WAAL J C , DE JONG E , et al . Hydroxymethylfurfural, a versatile platform chemical made from renewable resources [J ] . Chemical Reviews , 2013 , 113 ( 3 ): 1499 - 1597 .

CARRO J , FERNÁNDEZ-FUEYO E , FERNÁNDEZ-ALONSO C , et al . Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural [J ] . Biotechnology for Biofuels , 2018 , 11 : 86 .

KUMAR H , FRAAIJE M W . Conversion of furans by baeyer-villiger monooxygenases [J ] . Catalysts , 2017 , 7 ( 6 ): 179 .

KNAUS T , TSELIOU V , HUMPHREYS L D , et al . A biocatalytic method for the chemoselective aerobic oxidation of aldehydes to carboxylic acids [J ] . Green Chemistry , 2018 , 20 ( 17 ): 3931 - 3943 .

SATTLER J H , FUCHS M , TAUBER K , et al . Redox self-sufficient biocatalyst network for the amination of primary alcohols [J ] . Angewandte Chemie International Edition , 2012 , 51 ( 36 ): 9156 - 9159 .

VELASCO-LOZANO S , SANTIAGO-ARCOS J , MAYORAL J A , et al . Co-immobilization and colocalization of multi-enzyme systems for the cell-free biosynthesis of aminoalcohols [J ] . ChemCatChem , 2020 , 12 ( 11 ): 3030 - 3041 .

JIA H Y , ZONG M H , ZHENG G W , et al . One-pot enzyme cascade for controlled synthesis of furancarboxylic acids from 5-hydroxymethylfurfural by H 2 O 2 internal recycling [J ] . ChemSusChem , 2019 , 12 ( 21 ): 4764 - 4768 .

ZHANG X Y , ZONG M H , LI N . Whole-cell biocatalytic selective oxidation of 5-hydroxymethylfurfural to 5-hydroxymethyl-2-furancarboxylic acid [J ] . Green Chemistry , 2017 , 19 ( 19 ): 4544 - 4551 .

PENG B , MA C L , ZHANG P Q , et al . An effective hybrid strategy for converting rice straw to furoic acid by tandem catalysis via Sn-sepiolite combined with recombinant E. coli whole cells harboring horse liver alcohol dehydrogenase [J ] . Green Chemistry , 2019 , 21 ( 21 ): 5914 - 5923 .

LIAO H X , JIA H Y , DAI J R , et al . Bioinspired cooperative photobiocatalytic regeneration of oxidized nicotinamide cofactors for catalytic oxidations [J ] . ChemSusChem , 2021 , 14 ( 7 ): 1687 - 1691 .

吴淑可 , 周颐 , 王文 , 等 . 从单酶催化到多酶级联催化——从王义翘教授在酶技术领域的贡献说开去 [J ] . 合成生物学 , 2021 , 2 ( 4 ): 543 - 558 .

WU S K , ZHOU Y , WANG W , et al . From single-enzyme catalysis to multienzyme cascade: inspired from Professor Daniel I.C. Wang's pioneer work in enzyme technology [J ] . Synthetic Biology Journal , 2021 , 2 ( 4 ): 543 - 558 .

汤恒 , 韩鑫 , 邹树平 , 等 . 多酶催化体系在医药化学品合成中的应用 [J ] . 合成生物学 , 2021 , 2 ( 4 ): 559 - 576 .

TANG H , HAN X , ZOU S P , et al . Application of multi-enzyme catalytic system in the synthesis of pharmaceutical chemicals [J ] . Synthetic Biology Journal , 2021 , 2 ( 4 ): 559 - 576 .

CARBALLEIRA J D , QUEZADA M A , HOYOS P , et al . Microbial cells as catalysts for stereoselective red-ox reactions [J ] . Biotechnology Advances , 2009 , 27 ( 6 ): 686 - 714 .

WACHTMEISTER J , ROTHER D . Recent advances in whole cell biocatalysis techniques bridging from investigative to industrial scale [J ] . Current Opinion in Biotechnology , 2016 , 42 : 169 - 177 .

ZHANG D X , ONG Y L , LI Z , et al . Biological detoxification of furfural and 5-hydroxyl methyl furfural in hydrolysate of oil palm empty fruit bunch by Enterobacter sp. FDS8 [J ] . Biochemical Engineering Journal , 2013 , 72 : 77 - 82 .

RAN H , ZHANG J , GAO Q Q , et al . Analysis of biodegradation performance of furfural and 5-hydroxymethylfurfural by Amorphotheca resinae ZN 1 [J ] . Biotechnology for Biofuels , 2014 , 7 ( 1 ): 51 .

YAN Y X , BU C Y , HUANG X , et al . Efficient whole‐cell biotransformation of furfural to furfuryl alcohol by Saccharomyces cerevisiae NL22 [J ] . Journal of Chemical Technology & Biotechnology , 2019 , 94 ( 12 ): 3825 - 3831 .

PUETZ H , PUCHĽOVÁ E , VRANKOVÁ K , et al . Biocatalytic oxidation of alcohols [J ] . Catalysts , 2020 , 10 ( 9 ): 952 .

Views

下载量

CSCD

Alert me when the article has been cited

提交

Tools

Publicity Resources

No data

Related Author

LIU Xiangshi

WU Yilu

ZHAN Peng

HUANG Tianhao

CAI Di

QIN Peiyong

Related Institution

National Energy R&D Center for Biorefinery， Beijing University of Chemical Technology

Collage of Life Science and Technology， Beijing University of Chemical Technology

⁰