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https://pubs.acs.org/doi/10.1021/ja026855o
The enzyme organophosphorus hydrolase (OPH) was spontaneously entrapped in carboxylethyl- or aminopropyl-functionalized mesoporous silica with rigid, uniform open-pore geometry (30 nm). This approach yielded larger amounts of protein loading and much higher specific activity of the enzyme when compared to the unfunctionalized mesoporous silica and normal porous silica with the same pore size.Cited by: 632
https://www.researchgate.net/publication/11153462_Entrapping_Enzyme_in_a_Functionalized_Nanoporous_Support
Entrapping Enzyme in a Functionalized Nanoporous Support Article in Journal of the American Chemical Society 124(38):11242-3 · October 2002 with 43 Reads How we measure 'reads'
https://pubs.acs.org/doi/pdf/10.1021/ja026855o
Entrapping Enzyme in a Functionalized Nanoporous Support Chenghong Lei , Yongsoon Shin , Jun Liu * † , and Eric J. Ackerman * Pacific Northwest National Laboratory, Richland, Washington 99352Cited by: 632
https://pt.scribd.com/document/258707125/Entrapping-Enzyme-in-a-Functionalized-Nanoporous-Support
Entrapping Enzyme in a Functionalized Nanoporous Support Chenghong Lei, Yongsoon Shin, Jun Liu,*, and Eric J. Ackerman* Pacific Northwest National Laboratory, Richland, Washington 99352 Received May 9, 2002. There is a long history for enzyme (protein) immobilization using
https://www.researchgate.net/publication/51548294_Enzyme_specific_activity_in_functionalized_nanoporous_supports
Enzyme specific activity in functionalized nanoporous supports ... enzyme in a f unctionalized nanoporous support J ... can be enhanced about 2.0-fold by entrapping it into the HOOC-functionalized ...
https://iopscience.iop.org/article/10.1088/0957-4484/19/12/125102/pdf
LD) in functionalized nanoporous supports so that the enzyme immobilization efficiency (I e, defined as the ratio of the specific activity of the immobilized enzyme to the specific activity of the free enzyme in solution) can be much higher than 100%. A net negatively charged glucose oxidase (GOX) and a net positively chargedCited by: 73
https://iopscience.iop.org/article/10.1088/0957-4484/19/12/125102/meta
Feb 20, 2008 · Here we reveal that enzyme specific activity can be increased substantially by changing the protein loading density (P LD) in functionalized nanoporous supports so that the enzyme immobilization efficiency (I e, defined as the ratio of the specific activity of the immobilized enzyme to the specific activity of the free enzyme in solution) can be much higher than 100%.Cited by: 73
https://www.pnnl.gov/science/docs/enzyme08.pdf
Enzyme speciÞc activity in functionalized n an op orou s su p p orts C h en gh on g L ei,T h ereza A S oares,Y on gsoon S h in ,Ju n L iu an d E ric J A ck erm an P aciÞ c N orthw estN ational L aboratory,P O B ox 999,R ichland,W A 99352,U S A E -m ail: E ric.A ckerm an@ pnl.gov R eceived 19 O ctober 2007,in Þ nal form 17 January 2008
https://www.osti.gov/biblio/894458-characterization-functionalized-nanoporous-supports-protein-confinement
We report that even under the heated condition, the conformation and activity of a protein can be hoarded in a functionalized nanoporous support via non-covalent interaction, although the hoarded protein was not exhibiting the full protein activity, the protein released subsequently still maintained its native conformation and activity.
http://onlinelibrary.wiley.com/doi/10.1002/chem.201101191/full
Fabrication of Nanoporous Nanocomposites Entrapping Fe 3 O 4 Magnetic Nanoparticles and ... followed by the immobilization of oxidative enzymes. Glutaraldehyde crosslinking was employed to prevent enzymes leaching from the pores and led to over 20 wt % loading of the enzyme. ... A facile strategy to prepare porphyrin functionalized ZnS ...
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