Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies

Research output: Contribution to journalArticle

Standard

Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies. / Brennan, Jennifer L.; Kanaras, Antonios G.; Nativo, Paola; Tshikhudo, T. Robert; Rees, Claire; Fernandez, Laura Cabo; Dirvianskyte, Nijole; Razumas, Valdemaras; Skjot, Michael; Svendsen, Allan; Jorgensen, Christian I.; Schweins, Ralf; Zackrisson Oskolkova, Malin; Nylander, Tommy; Brust, Mathias; Barauskas, Justas.

In: Langmuir, Vol. 26, No. 16, 2010, p. 13590-13599.

Research output: Contribution to journalArticle

Harvard

Brennan, JL, Kanaras, AG, Nativo, P, Tshikhudo, TR, Rees, C, Fernandez, LC, Dirvianskyte, N, Razumas, V, Skjot, M, Svendsen, A, Jorgensen, CI, Schweins, R, Zackrisson Oskolkova, M, Nylander, T, Brust, M & Barauskas, J 2010, 'Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies', Langmuir, vol. 26, no. 16, pp. 13590-13599. https://doi.org/10.1021/la1018604

APA

Brennan, J. L., Kanaras, A. G., Nativo, P., Tshikhudo, T. R., Rees, C., Fernandez, L. C., ... Barauskas, J. (2010). Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies. Langmuir, 26(16), 13590-13599. https://doi.org/10.1021/la1018604

CBE

Brennan JL, Kanaras AG, Nativo P, Tshikhudo TR, Rees C, Fernandez LC, Dirvianskyte N, Razumas V, Skjot M, Svendsen A, Jorgensen CI, Schweins R, Zackrisson Oskolkova M, Nylander T, Brust M, Barauskas J. 2010. Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies. Langmuir. 26(16):13590-13599. https://doi.org/10.1021/la1018604

MLA

Vancouver

Brennan JL, Kanaras AG, Nativo P, Tshikhudo TR, Rees C, Fernandez LC et al. Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies. Langmuir. 2010;26(16):13590-13599. https://doi.org/10.1021/la1018604

Author

Brennan, Jennifer L. ; Kanaras, Antonios G. ; Nativo, Paola ; Tshikhudo, T. Robert ; Rees, Claire ; Fernandez, Laura Cabo ; Dirvianskyte, Nijole ; Razumas, Valdemaras ; Skjot, Michael ; Svendsen, Allan ; Jorgensen, Christian I. ; Schweins, Ralf ; Zackrisson Oskolkova, Malin ; Nylander, Tommy ; Brust, Mathias ; Barauskas, Justas. / Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies. In: Langmuir. 2010 ; Vol. 26, No. 16. pp. 13590-13599.

RIS

TY - JOUR

T1 - Enzymatic Activity of Lipase-Nanoparticle Conjugates and the Digestion of Lipid Liquid Crystalline Assemblies

AU - Brennan, Jennifer L.

AU - Kanaras, Antonios G.

AU - Nativo, Paola

AU - Tshikhudo, T. Robert

AU - Rees, Claire

AU - Fernandez, Laura Cabo

AU - Dirvianskyte, Nijole

AU - Razumas, Valdemaras

AU - Skjot, Michael

AU - Svendsen, Allan

AU - Jorgensen, Christian I.

AU - Schweins, Ralf

AU - Zackrisson Oskolkova, Malin

AU - Nylander, Tommy

AU - Brust, Mathias

AU - Barauskas, Justas

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

U2 - 10.1021/la1018604

DO - 10.1021/la1018604

M3 - Article

VL - 26

SP - 13590

EP - 13599

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 16

ER -