Cost effective synthesis of a copper-1H-imidazole@activated carbon metal organic framework as an electrode material for supercapacitor applications

2018 ◽  
Vol 42 (12) ◽  
pp. 10300-10308 ◽  
Author(s):  
E. Elanthamilan ◽  
S. Rajkumar ◽  
R. Rajavalli ◽  
J. Princy Merlin

A simple and sonochemically synthesized Cu-IC MOF exhibits good supercapacitive behaviour.

2021 ◽  
Author(s):  
Sujing Wang ◽  
Antoine Tissot ◽  
Guillaume Maurin ◽  
Tatjana Parac-Vogt ◽  
Christian Serre ◽  
...  

<div>The discovery of nanozymes for selective cleavage of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the detailed catalytic properties of a microporous zirconium carboxylate metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features an excellent catalytic activity and selectivity, a good tolerance toward reaction conditions covering a wide range of different pH values, and importantly, an exceptional recycling ability associated with easy regeneration process. Taking into account the excellent catalytic performance of MIP-201 and its other advantages such as 6-connected Zr6 cluster active sites, the green, scalable and cost-effective synthesis, and an outstanding chemical and architectural stability, our finding suggests that MIP-201 may be a promising and practical alternative to the current commercially available catalysts for peptide bond hydrolysis.</div>


2021 ◽  
Author(s):  
Sujing Wang ◽  
Antoine Tissot ◽  
Guillaume Maurin ◽  
Tatjana Parac-Vogt ◽  
Christian Serre ◽  
...  

<div>The discovery of nanozymes for selective cleavage of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the detailed catalytic properties of a microporous zirconium carboxylate metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features an excellent catalytic activity and selectivity, a good tolerance toward reaction conditions covering a wide range of different pH values, and importantly, an exceptional recycling ability associated with easy regeneration process. Taking into account the excellent catalytic performance of MIP-201 and its other advantages such as 6-connected Zr6 cluster active sites, the green, scalable and cost-effective synthesis, and an outstanding chemical and architectural stability, our finding suggests that MIP-201 may be a promising and practical alternative to the current commercially available catalysts for peptide bond hydrolysis.</div>


CrystEngComm ◽  
2019 ◽  
Vol 21 (9) ◽  
pp. 1442-1451 ◽  
Author(s):  
Sadayappan Nagamuthu ◽  
Kwang-Sun Ryu

A metal–organic framework is employed for the preparation of an interconnected network porous structure of Mn2O3/carbon for supercapacitor applications.


2021 ◽  
Author(s):  
Sujing Wang ◽  
Hong Giang T Ly ◽  
Mohammad Wahiduzzaman ◽  
Iurii Dovgaliuk ◽  
Antoine Tissot ◽  
...  

Abstract The discovery of nanozymes for selective fragmentation of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the detailed catalytic properties of a microporous zirconium carboxylate metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features an excellent catalytic activity and selectivity, a good tolerance toward reaction conditions covering a wide range of different pH values, and importantly, an exceptional recycling ability associated with easy regeneration process. Taking into account the excellent catalytic performance of MIP-201 and its other advantages such as 6-connected Zr6 cluster active sites, the green, scalable and cost-effective synthesis, and an outstanding chemical and architectural stability, our finding suggests that MIP-201 may be a promising and practical alternative to the current commercially available catalysts for peptide bond hydrolysis.


2021 ◽  
Author(s):  
Sujing Wang ◽  
Hong Giang T Ly ◽  
Mohammad Wahiduzzaman ◽  
Iurii Dovgaliuk ◽  
Antoine Tissot ◽  
...  

Abstract The discovery of nanozymes for selective fragmentation of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the detailed catalytic properties of a microporous zirconium carboxylate metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features an excellent catalytic activity and selectivity, a good tolerance toward reaction conditions covering a wide range of different pH values, and importantly, an exceptional recycling ability associated with easy regeneration process. Taking into account the excellent catalytic performance of MIP-201 and its other advantages such as 6-connected Zr6 cluster active sites, the green, scalable and cost-effective synthesis, and an outstanding chemical and architectural stability, our finding suggests that MIP-201 may be a promising and practical alternative to the current commercially available catalysts for peptide bond hydrolysis.


Author(s):  
Davood Taherinia ◽  
Seyyed Heydar Moravvej ◽  
Mohammad Moazzeni ◽  
Elham Akbarzadeh

The development of efficient and cost-effective catalysts for the oxygen evolution reaction is highly desirable for applications that are based on sustainable and clean technologies. In this study, we report...


2021 ◽  
Vol 60 (11) ◽  
pp. 4332-4341
Author(s):  
Hossein Shahriyari Far ◽  
Mahdi Hasanzadeh ◽  
Mina Najafi ◽  
Targol Rahimi Masale Nezhad ◽  
Mahboubeh Rabbani

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