A novel photon-enzyme cascade catalysis system based on hybrid HRP-CN/Cu3(PO4)2 nanoflowers for degradation of BPA in water

2021 ◽  
pp. 131808
Author(s):  
Jiacong Wu ◽  
Xinnan Ma ◽  
Chunmei Li ◽  
Xiangtong Zhou ◽  
Juan Han ◽  
...  
Membranes ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 28
Author(s):  
Fatin Nasreen Ahmad Rizal Lim ◽  
Fauziah Marpani ◽  
Victoria Eliz Anak Dilol ◽  
Syazana Mohamad Pauzi ◽  
Nur Hidayati Othman ◽  
...  

Multi-enzyme cascade catalysis involved three types of dehydrogenase enzymes, namely, formate dehydrogenase (FDH), formaldehyde dehydrogenase (FaldDH), alcohol dehydrogenase (ADH), and an equimolar electron donor, nicotinamide adenine dinucleotide (NADH), assisting the reaction is an interesting pathway to reduce thermodynamically stable molecules of CO2 from the atmosphere. The biocatalytic sequence is interesting because it operates under mild reaction conditions (low temperature and pressure) and all the enzymes are highly selective, which allows the reaction to produce three basic chemicals (formic acid, formaldehyde, and methanol) in just one pot. There are various challenges, however, in applying the enzymatic conversion of CO2, namely, to obtain high productivity, increase reusability of the enzymes and cofactors, and to design a simple, facile, and efficient reactor setup that will sustain the multi-enzymatic cascade catalysis. This review reports on enzyme-aided reactor systems that support the reduction of CO2 to methanol. Such systems include enzyme membrane reactors, electrochemical cells, and photocatalytic reactor systems. Existing reactor setups are described, product yields and biocatalytic productivities are evaluated, and effective enzyme immobilization methods are discussed.


The Analyst ◽  
2014 ◽  
Vol 139 (5) ◽  
pp. 1030-1036 ◽  
Author(s):  
Lijuan Xiao ◽  
Yaqin Chai ◽  
Ruo Yuan ◽  
Haijun Wang ◽  
Lijuan Bai

In this work, a novel pseudo triple-enzyme cascade catalysis amplification strategy was employed to fabricate a highly sensitive electrochemiluminescence (ECL) aptasensor for thrombin (TB) detection.


ACS Catalysis ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 4871-4878 ◽  
Author(s):  
Tae-Hun Kim ◽  
Su-Hwan Kang ◽  
Jeong-Eun Han ◽  
Eun-Ji Seo ◽  
Eun-Yeong Jeon ◽  
...  

2019 ◽  
Author(s):  
De-Wei Gao ◽  
Yang Gao ◽  
Huiling Shao ◽  
Tian-Zhang Qiao ◽  
Xin Wang ◽  
...  

Enantioenriched <i>α</i>-aminoboronic acids play a unique role in medicinal chemistry and have emerged as privileged pharmacophores in proteasome inhibitors. Additionally, they represent synthetically useful chiral building blocks in organic synthesis. Recently, CuH-catalyzed asymmetric alkene hydrofunctionalization has become a powerful tool to construct stereogenic carbon centers. In contrast, applying CuH cascade catalysis to achieve reductive 1,1-difunctionalization of alkynes remains an important, but largely unaddressed, synthetic challenge. Herein, we report an efficient strategy to synthesize <i>α</i>-aminoboronates <i>via </i>CuH-catalyzed hydroboration/hydroamination cascade of readily available alkynes. Notably, this transformation selectively delivers the desired 1,1-heterodifunctionalized product in favor of alternative homodifunctionalized, 1,2-heterodifunctionalized, or reductively monofunctionalized byproducts, thereby offering rapid access to these privileged scaffolds with high chemo-, regio- and enantioselectivity.<br>


2021 ◽  
pp. 2005172
Author(s):  
Weiqing Xu ◽  
Lei Jiao ◽  
Yu Wu ◽  
Liuyong Hu ◽  
Wenling Gu ◽  
...  

Author(s):  
Ruirui Yun ◽  
Beibei Zhang ◽  
Chuang Qiu ◽  
Ziwei Ma ◽  
Feiyang Zhan ◽  
...  
Keyword(s):  
N Doping ◽  

Author(s):  
Daniel Moock ◽  
Tobias Wagener ◽  
Tianjiao Hu ◽  
Timothy Gallagher ◽  
Frank Glorius
Keyword(s):  

2021 ◽  
Vol 11 (11) ◽  
pp. 4877
Author(s):  
Ravneet Mandair ◽  
Pinar Karagoz ◽  
Roslyn M. Bill

A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant Thermococcus kodakarensis has an altered cofactor preference for NAD+, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from Sulfolobus solfataricus and NAD+/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.


Sign in / Sign up

Export Citation Format

Share Document