Rationally Designed, “Stable-on-the-Table” NanoBiocatalysts Bound to Zr(IV) Phosphate Nanosheets

July 28, 2017

Title

Rationally Designed, “Stable-on-the-Table” NanoBiocatalysts Bound to Zr(IV) Phosphate Nanosheets

Author

I. K. Deshapriya, C.V. Kumar

Year

2016

Journal

Methods in Enzymology

Abstract

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.

Instrument

J-710

Keywords

Circular dichroism, Ligand binding, Secondary structure, Nanostructures, Materials, Biochemistry