The structure and function of an enzyme can be altered by nanoparticles (NPs). The interaction between enzyme and NPs is governed by the key properties of NPs, such as structure, size, surface chemistry, charge and surface shape. Recent representative studies on the NP-enzyme interactions and the regulation of enzyme activity by NPs with different size, composition and surface modification are reviewed.

A significant increase in biomedical applications of nanomaterials and their potential toxicity demands versatile analytical techniques to determine protein–nanoparticle (NP) interactions. These diverse analytical techniques are reviewed. Spectroscopic methods play a significant role in studying binding affinity, binding ratio, and binding mechanisms. To elucidate NP–proteome interactions, chromatography and electrophoresis techniques are applied to separate NP-bound proteins and matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) to identify these proteins. Since NP–protein binding is a dynamic event, surface plasmon resonance (SPR) and quartz crystal microbalance (QCM) are methods of choice to study the kinetics of NP–protein binding.