• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

克服酶促二氧化碳还原局限性的策略。

Strategies for overcoming the limitations of enzymatic carbon dioxide reduction.

机构信息

School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Liangxiang Higher Education Park, Fangshan District, Beijing 102488, PR China.

School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Liangxiang Higher Education Park, Fangshan District, Beijing 102488, PR China.

出版信息

Biotechnol Adv. 2022 Nov;60:108024. doi: 10.1016/j.biotechadv.2022.108024. Epub 2022 Jul 28.

DOI:10.1016/j.biotechadv.2022.108024
PMID:35907470
Abstract

The overexploitation of fossil fuels has led to a significant increase in atmospheric carbon dioxide (CO) concentrations, thereby causing problems, such as the greenhouse effect. Rapid global climate change has caused researchers to focus on utilizing CO in a green and efficient manner. One of the ways to achieve this is by converting CO into valuable chemicals via chemical, photochemical, electrochemical, or enzymatic methods. Among these, the enzymatic method is advantageous because of its high specificity and selectivity as well as the mild reaction conditions required. The reduction of CO to formate, formaldehyde, and methanol using formate dehydrogenase (FDH), formaldehyde dehydrogenase (FDH), and alcohol dehydrogenase (ADH) are attractive routes, respectively. In this review, strategies for overcoming the common limitations of enzymatic CO reduction are discussed. First, we present a brief background on the importance of minimizing of CO emissions and introduce the three bottlenecks limiting enzymatic CO reduction. Thereafter, we explore the different strategies for enzyme immobilization on various support materials. To solve the problem of cofactor consumption, different state-of-the-art cofactor regeneration strategies as well as research on the development of cofactor substitutes and cofactor-free systems are extensively discussed. Moreover, aiming at improving CO solubility, biological, physical, and engineering measures are reviewed. Finally, conclusions and future perspectives are presented.

摘要

化石燃料的过度开采导致大气中二氧化碳(CO)浓度显著增加,从而引发了温室效应等问题。快速的全球气候变化促使研究人员专注于以绿色、高效的方式利用 CO。实现这一目标的方法之一是通过化学、光化学、电化学或酶法将 CO 转化为有价值的化学品。在这些方法中,由于酶法具有高特异性和选择性以及所需的温和反应条件,因此具有优势。使用甲酸脱氢酶(FDH)、甲醛脱氢酶(FDH)和醇脱氢酶(ADH)将 CO 还原为甲酸盐、甲醛和甲醇是很有吸引力的途径。在这篇综述中,讨论了克服酶促 CO 还原常见限制的策略。首先,我们简要介绍了减少 CO 排放的重要性,并介绍了限制酶促 CO 还原的三个瓶颈。然后,我们探讨了在各种支撑材料上进行酶固定化的不同策略。为了解决辅因子消耗的问题,广泛讨论了不同的最新辅因子再生策略以及开发辅因子替代品和无辅因子系统的研究。此外,为了提高 CO 的溶解度,还回顾了生物、物理和工程措施。最后,提出了结论和未来展望。

相似文献

1
Strategies for overcoming the limitations of enzymatic carbon dioxide reduction.克服酶促二氧化碳还原局限性的策略。
Biotechnol Adv. 2022 Nov;60:108024. doi: 10.1016/j.biotechadv.2022.108024. Epub 2022 Jul 28.
2
CO to Methanol: A Highly Efficient Enzyme Cascade.CO 到甲醇:高效酶级联反应。
Methods Mol Biol. 2022;2487:317-344. doi: 10.1007/978-1-0716-2269-8_19.
3
Efficient and Selective Electrochemically Driven Enzyme-Catalyzed Reduction of Carbon Dioxide to Formate using Formate Dehydrogenase and an Artificial Cofactor.使用甲酸脱氢酶和人工辅因子电化学驱动高效和选择性酶催化还原二氧化碳为甲酸盐。
Acc Chem Res. 2019 Mar 19;52(3):676-685. doi: 10.1021/acs.accounts.8b00551. Epub 2019 Feb 11.
4
Cascade catalysis in membranes with enzyme immobilization for multi-enzymatic conversion of CO2 to methanol.用于将二氧化碳多酶转化为甲醇的酶固定化膜中的级联催化。
N Biotechnol. 2015 May 25;32(3):319-27. doi: 10.1016/j.nbt.2015.02.006. Epub 2015 Feb 16.
5
Direct Biocatalytic Processes for CO Capture as a Green Tool to Produce Value-Added Chemicals.直接生物催化 CO 捕集过程作为生产高附加值化学品的绿色工具。
Molecules. 2023 Jul 19;28(14):5520. doi: 10.3390/molecules28145520.
6
The challenges of using NAD-dependent formate dehydrogenases for CO conversion.使用 NAD 依赖性甲酸盐脱氢酶进行 CO 转化所面临的挑战。
Crit Rev Biotechnol. 2022 Sep;42(6):953-972. doi: 10.1080/07388551.2021.1981820. Epub 2021 Oct 10.
7
Improving the Enzymatic Cascade of Reactions for the Reduction of CO to CHOH in Water: From Enzymes Immobilization Strategies to Cofactor Regeneration and Cofactor Suppression.提高 CO 到 CHOH 在水中的还原反应的酶级联反应:从酶固定化策略到辅因子再生和辅因子抑制。
Molecules. 2022 Aug 2;27(15):4913. doi: 10.3390/molecules27154913.
8
Construction of Functionally Compartmental Inorganic Photocatalyst-Enzyme System via Imitating Chloroplast for Efficient Photoreduction of CO to Formic Acid.通过模拟叶绿体构建具有功能分区的无机光催化剂-酶体系用于高效光还原 CO 为甲酸。
ACS Appl Mater Interfaces. 2020 Aug 5;12(31):34795-34805. doi: 10.1021/acsami.0c06684. Epub 2020 Jul 27.
9
Immobilization of formate dehydrogenase in metal organic frameworks for enhanced conversion of carbon dioxide to formate.将甲酸脱氢酶固定在金属有机框架中以增强二氧化碳向甲酸盐的转化。
Chemosphere. 2021 Mar;267:128921. doi: 10.1016/j.chemosphere.2020.128921. Epub 2020 Nov 10.
10
Bio-inspired CO reduction reaction catalysis using soft-oxometalates.利用软氧金属酸盐进行仿生 CO 还原反应催化。
J Inorg Biochem. 2022 Sep;234:111903. doi: 10.1016/j.jinorgbio.2022.111903. Epub 2022 Jun 16.

引用本文的文献

1
Bio-Inspired Microreactors Continuously Synthesize Glucose Precursor from CO with an Energy Conversion Efficiency 3.3 Times of Rice.生物启发型微反应器以 CO 为原料连续合成葡萄糖前体,能量转换效率是水稻的 3.3 倍。
Adv Sci (Weinh). 2024 Feb;11(6):e2305629. doi: 10.1002/advs.202305629. Epub 2023 Dec 3.
2
Engineering of formate dehydrogenase for improving conversion potential of carbon dioxide to formate.用于提高二氧化碳向甲酸盐转化潜力的甲酸脱氢酶工程。
World J Microbiol Biotechnol. 2023 Oct 21;39(12):352. doi: 10.1007/s11274-023-03739-5.
3
Direct Biocatalytic Processes for CO Capture as a Green Tool to Produce Value-Added Chemicals.
直接生物催化 CO 捕集过程作为生产高附加值化学品的绿色工具。
Molecules. 2023 Jul 19;28(14):5520. doi: 10.3390/molecules28145520.
4
Biocatalytic Membranes for Carbon Capture and Utilization.用于碳捕获与利用的生物催化膜
Membranes (Basel). 2023 Mar 23;13(4):367. doi: 10.3390/membranes13040367.