Journal
SOFT MATTER
Volume 10, Issue 34, Pages 6425-6432Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4sm01127a
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Funding
- State Key Laboratory of Microbial Technology of China
- National Natural Science Foundation of China [20973103, 21173133]
- National Basic Research Program of China [2011CB707400]
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The interfacial property of reverse micelles is an important factor affecting the catalytic activity of enzymes hosted in the micelles. In this article, the effect of gold nanoparticles (GNPs) on the catalytic activity of laccase (non-surface-active enzyme) and the related mechanism are reported. It was found that laccase activity was dependent on the size of the particle and its concentration as well as on the water content and the concentration of AOT. It was shown that there existed several types of micelles in the present reverse micellar system in the presence of GNPs. The population of the various micelles depended on the concentrations of both GNPs and AOT. Fluorescence and circular dichroism spectra of laccase at different water contents and GNP concentrations indicated that the conformation of laccase and its activity were tuned by GNPs via changing the structure of the reverse micelles. Analysis showed that changes in the thickness of the water layer (L-w) and in the apparent occupied area of individual AOT molecules (A(AOT)) caused by GNPs were the main parameters affecting the activity of laccase. The present work extends and deepens the understanding of the tuning mechanism of GNPs on enzymatic performance in reverse micelles and provides guidance for rational design of the optimal microenvironment of laccase.
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