muramidase and zirconium-phosphate

Rational approaches for the control of nano-bio interfaces for enzyme stabilization are vital for engineering advanced, functional nanobiocatalysts, biosensors, implants, or "smart" drug delivery systems. This chapter presents an overview of our recent efforts on structural, functional, and mechanistic details of enzyme nanomaterials design, and describes how progress is being made by hypothesis-driven rational approaches. Interactions of a number of enzymes having wide ranges of surface charges, sizes, and functional groups with α-Zr(IV)phosphate (α-ZrP) nanosheets are carefully controlled to achieve high enzyme binding affinities, excellent loadings, significant retention of the bound enzyme structure, and high enzymatic activities. In specific cases, catalytic activities and selectivities of the nanobiocatalysts are improved over those of the corresponding pristine enzymes. Maximal enzyme structure retention has been obtained by coating the nanosheets with appropriate proteinaceous materials to soften the enzyme-nanosheet interface. These systematic manipulations are of significant importance to understand the complex behavior of enzymes at inorganic surfaces.

Topics: Biocatalysis; Biosensing Techniques; Chymotrypsin; Enzyme Stability; Enzymes, Immobilized; Isoelectric Point; Muramidase; Nanostructures; Protein Binding; Protein Denaturation; Thermodynamics; Zirconium