Journal
RSC ADVANCES
Volume 2, Issue 11, Pages 4736-4745Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2ra20056b
Keywords
-
Categories
Funding
- Department of Science and Technology [SR/S1/PC-30/2008]
- Department of Biotechnology
- Council of Scientific and Industrial Research, India
Ask authors/readers for more resources
The presence of citrate-stabilized gold nanoparticles (cit-Au NPs) significantly enhanced the specific activity of alpha-amylase, which could also be modulated by varying the concentration of the enzyme, while keeping the NP concentration constant. Also, the lowest concentration (0.175 mu g mL(-1)) at which the Michaelis-Menten behavior of the enzyme could clearly be observed in the presence of NPs was much less than that in their absence. At higher protein concentrations the activity decreased monotonically until it reached nearly the same as that of free enzyme, while exhibiting Michaelis-Menten kinetics at all concentrations. Transmission electron microscopy (TEM) and dynamic light scattering (DLS) based particle size analyses indicated increased agglomeration of the NPs with increased protein concentration. The results have been explained based on a model which considered the presence of enzyme bound to NP and that available for enhanced catalysis, enzyme bound to NP but unavailable due to being buried inside the agglomerate and the free enzyme.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available