Modeling enzyme immobilization in porous solid supports

1982 ◽  
Vol 24 (7) ◽  
pp. 1527-1546 ◽  
Author(s):  
Duong D. Do ◽  
Douglas S. Clark ◽  
James E. Bailey
CrystEngComm ◽  
2020 ◽  
Vol 22 (41) ◽  
pp. 6886-6899
Author(s):  
Erin R. Bertelsen ◽  
Nolan C. Kovach ◽  
Benjamin J. Reinhart ◽  
Brian G. Trewyn ◽  
Mark R. Antonio ◽  
...  

Functionalized ordered mesoporous carbons facilitate the templateing of microcrystalline-like domains and multinuclear speciation under high Eu3+ loading conditions.


2016 ◽  
Vol 90 ◽  
pp. 76-82 ◽  
Author(s):  
Marieta L.C. Passos ◽  
David S.M. Ribeiro ◽  
João L.M. Santos ◽  
M.Lúcia M.F.S. Saraiva

Langmuir ◽  
2017 ◽  
Vol 33 (42) ◽  
pp. 11719-11726 ◽  
Author(s):  
Nanhua Wu ◽  
Xiaoyan Ji ◽  
Wenlong Xie ◽  
Chang Liu ◽  
Xin Feng ◽  
...  

2008 ◽  
Vol 9 (1) ◽  
pp. 381-387 ◽  
Author(s):  
Mozhgan Bagheri ◽  
Héctor Rodríguez ◽  
Richard P. Swatloski ◽  
Scott K. Spear ◽  
Daniel T. Daly ◽  
...  

INEOS OPEN ◽  
2020 ◽  
Author(s):  
N. A. Samoilova ◽  

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.


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