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Sökning: onr:"swepub:oai:lup.lub.lu.se:22bff80f-1d11-4681-9b19-86066d715b16" > Enzymatic Activity ...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003866naa a2200457 4500
001oai:lup.lub.lu.se:22bff80f-1d11-4681-9b19-86066d715b16
003SwePub
008160401s2010 | |||||||||||000 ||eng|
0247 a https://lup.lub.lu.se/record/16753862 URI
0247 a https://doi.org/10.1021/la10186042 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Brennan, Jennifer L.4 aut
2451 0a Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies
264 1b American Chemical Society (ACS),c 2010
520 a Variants of lipase were attached to gold nanoparticles (NPs) and their enzymatic activity was studied. The two bioengineered lipase variants have been prepared with biotin groups attached to different residues on the protein outer surface. The biotinylation was evidenced by denaturing polyacrylamide gel electrophoresis and quantified by the ([2-(4'-hydroxyazobenzene)]benzoic acid spectrophotometric test. NPs of 14 +/- 1 nm diameter coated with thiolated-polyethylene glycol ligands containing controlled proportions of biotin moieties have been prepared and characterized by transmission electron microscopy, UV-vis spectroscopy, small angle neutron scattering, and elemental analysis. These biotin-functionalized NPs were conjugated to lipase using streptavidin as a linker molecule. Enzyme activity assays on the lipase-nanoparticle conjugates show that the lipase loading and activity of the NPs can be controlled by varying the percentage of biotin groups in the particle protecting coat. The lipase-NP conjugates prepared using one variant display higher activity than those prepared using the other variant, demonstrating orientation-dependent enzyme activity. Cryogenic transmission electron microscopy was used to visualize the enzymatic activity of lipase-NP on well-defined lipid substrates. It was found that lipase-coated NPs are able to digest the substrates in a different manner in comparison to the free lipase.
650 7a NATURVETENSKAPx Kemix Fysikalisk kemi0 (SwePub)104022 hsv//swe
650 7a NATURAL SCIENCESx Chemical Sciencesx Physical Chemistry0 (SwePub)104022 hsv//eng
7001 a Kanaras, Antonios G.4 aut
7001 a Nativo, Paola4 aut
7001 a Tshikhudo, T. Robert4 aut
7001 a Rees, Claire4 aut
7001 a Fernandez, Laura Cabo4 aut
7001 a Dirvianskyte, Nijole4 aut
7001 a Razumas, Valdemaras4 aut
7001 a Skjot, Michael4 aut
7001 a Svendsen, Allan4 aut
7001 a Jorgensen, Christian I.4 aut
7001 a Schweins, Ralf4 aut
7001 a Zackrisson Oskolkova, Malinu Lund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)fkem-miz
7001 a Nylander, Tommyu Lund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)fk1-tny
7001 a Brust, Mathias4 aut
7001 a Barauskas, Justas4 aut
7102 a Fysikalisk kemib Enheten för fysikalisk och teoretisk kemi4 org
7730 t Langmuird : American Chemical Society (ACS)g 26:16, s. 13590-13599q 26:16<13590-13599x 0743-7463x 1520-5827
8564 u http://dx.doi.org/10.1021/la1018604y FULLTEXT
8564 8u https://lup.lub.lu.se/record/1675386
8564 8u https://doi.org/10.1021/la1018604

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