Removal of lead ions from aqueous solution using new magnetic metal-organic framework

2021 ◽  
pp. 1-30
Author(s):  
Homeira Nasiri ◽  
Farshad Yazdani ◽  
Jalal Zeinali ◽  
Hamid Reza Mortaheb
2019 ◽  
Vol 66 (10) ◽  
pp. 1327-1335 ◽  
Author(s):  
Mohammad Ali Karimi ◽  
Hassan Masrouri ◽  
Hassan Karami ◽  
Saeed Andishgar ◽  
Mehrnaz Alsadat Mirbagheri ◽  
...  

2018 ◽  
Vol 483 ◽  
pp. 488-495 ◽  
Author(s):  
Guoyuan Yuan ◽  
Changsong Zhao ◽  
Hong Tu ◽  
Min Li ◽  
Jun Liu ◽  
...  

2016 ◽  
Vol 28 (2) ◽  
pp. 277-281 ◽  
Author(s):  
N.D. Shooto ◽  
N. Ayawei ◽  
D. Wankasi ◽  
L. Sikhwivhilu ◽  
E.D. Dikio

2018 ◽  
Vol 65 (10) ◽  
pp. 1229-1238 ◽  
Author(s):  
Mohammad Ali Karimi ◽  
Hassan Masrouri ◽  
Mehrnaz Alsadat Mirbagheri ◽  
Saeed Andishgar ◽  
Tayebe Pourshamsi

2021 ◽  
Author(s):  
Faezeh Taghavi ◽  
Amir Khojastehnezhad ◽  
Reza Khalifeh ◽  
Maryam Rajabzadeh ◽  
Fahimeh Rezaei ◽  
...  

The first report of the use of an acidic magnetic metal organic framework for the chemical fixation of CO2 as an environmentally friendly reaction.


Nanomaterials ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1759
Author(s):  
Neda Motamedi ◽  
Mahmood Barani ◽  
Azadeh Lohrasbi-Nejad ◽  
Mojtaba Mortazavi ◽  
Ali Riahi-Medvar ◽  
...  

The improvement in the enzyme activity of Aspergillus flavus urate oxidase (Uox) was attained by immobilizing it on the surface of a Ni-based magnetic metal–organic framework (NimMOF) nanomaterial; physicochemical properties of NimMOF and its application as an enzyme stabilizing support were evaluated, which revealed a significant improvement in its stability upon immobilization on NimMOF (Uox@NimMOF). It was affirmed that while the free Uox enzyme lost almost all of its activity at ~40–45 °C, the immobilized Uox@NimMOF retained around 60% of its original activity, even retaining significant activity at 70 °C. The activation energy (Ea) of the enzyme was calculated to be ~58.81 kJ mol−1 after stabilization, which is approximately half of the naked Uox enzyme. Furthermore, the external spectroscopy showed that the MOF nanomaterials can be coated by hydrophobic areas of the Uox enzyme, and the immobilized enzyme was active over a broad range of pH and temperatures, which bodes well for the thermal and long-term stability of the immobilized Uox on NimMOF.


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