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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
Published on: April 4, 2014
Nanoscale size impact of nanoparticle interaction and activity studies with urease
Priya Bhardwaj1,2, Bhawana Bisht1,2, Vijayender Bhalla1,2
1Institute of Microbial Technology (IMTECH), Council of Scientific and Industrial Research (CSIR) Chandigarh, 160036, India. vkbhalla@imtech.res.in.
Abstract:
Herein, we provide insights into the size-dependent interactions of silver nanoparticles (AgNPs) with urease and their implications for enzyme inhibition. AgNPs with a size of 5 nm exhibited the strongest binding affinity of 66 nM, resulting in significant enzyme attachment, interfering enzyme conformation, and a consequent loss of activity. Mid-sized AgNPs, i.e., 20 and 50 nm, exhibited binding affinities of 712 and 616 nM, causing only slight structural alterations. In contrast, 100 nm AgNPs demonstrated a high binding affinity of 171 nM accompanied by a favorable enthalpic contribution and a pronounced inhibitory effect.

