Journal
JOURNAL OF NANOPARTICLE RESEARCH
Volume 15, Issue 11, Pages -Publisher
SPRINGER
DOI: 10.1007/s11051-013-2038-y
Keywords
Enzyme; Catalytic activity; Immobilization; Horseradish peroxidase; Bovine serum albumin; Nanoparticle; Nanobiotechnology
Categories
Funding
- National Research Fund for Fundamental Key Project [2011CB935800, 2009CB939701]
- National Natural Science Foundation of China [21073078, 51072064]
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The using of macromolecular additives is known to be a simple and effective way to improve the activity of immobilized enzymes on solid support, yet the mechanism has not been well understood. Taking horseradish peroxidase (HRP) as an example, only 30 % of its catalytic activity was kept after being immobilized on the surface of 25-nm Au nanoparticles, mainly attributed to the conformational change of the heme-containing active site. The catalytic activity of HRP was significantly improved to 80 % when a certain amount of bovine serum albumin (BSA) was added at the initial stage of the immobilization. Systematic spectral investigation indicated that the addition of BSA inhibited the tertiary structure change around the active site, which was a prerequisite for improved activity of the immobilized HRP. Steady-state kinetic analyses revealed that the introduction of BSA could effectively improve the turnover rate of substrate to product in spite of slight reduced affinity to substrates, which also contributed to the improved catalytic activity.
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