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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: 645
https://pubs.acs.org/doi/abs/10.1021/ja026855o
Entrapping Enzyme in a Functionalized Nanoporous Support. ... Local Release of Highly Loaded Antibodies from Functionalized Nanoporous Support for Cancer Immunotherapy. Chenghong Lei, Pu Liu, Baowei Chen, Yumeng Mao, Heather Engelmann, Yongsoon Shin, Jade Jaffar, Ingegerd Hellstrom, Jun Liu and Karl Erik Hellstrom.Cited by: 645
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://www.researchgate.net/publication/51548294_Enzyme_specific_activity_in_functionalized_nanoporous_supports
Enzyme specific activity in functionalized nanoporous supports ... nanostructures are paramount for enzyme entrapping ... M. miehei lipase adsorbed on hydrophobic support is even 20 times more ...
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.
https://www.pnnl.gov/science/docs/enzyme08.pdf
Enzyme speciÞc activity in functionalized ... (P L D) in functionalized nanoporous supports so that the enzym e im m obilization efÞ ciency (Ie,deÞ ned as the ratio of the speciÞ c activity of the im m obilized ... nanostructures are param ount for enzym e entrapping [7, 8].
https://iopscience.iop.org/article/10.1088/0957-4484/19/12/125102
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: 72
https://pt.scribd.com/document/258707125/Entrapping-Enzyme-in-a-Functionalized-Nanoporous-Support
Published on Web 08/28/2002. 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 …
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2879136/
Dec 25, 2009 · Both unfunctionalized and functionalized mesoporous silica have been tested for enzyme immobilization [8–16]. Our recent results have showed that the enzymes entrapped in functionalized mesoporous silica (FMS) with pore sizes as large as tens of nanometers could exhibit enhanced activity in comparison with the enzymes free in solution [17–21].Cited by: 24
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1933498/
Most man-made matrices for enzyme confinement lead to suboptimal catalytic activity. Ackerman and colleagues showed that an entrapping environment consisting of functionalized mesoporous silica actually enhances enzyme activity beyond the test-tube levels of free enzymes in solution.Cited by: 19
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