Rationally Designed, "Stable-on-the-Table" NanoBiocatalysts Bound to Zr(IV) Phosphate Nanosheets.
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.
Department of Chemistry, University of Connecticut, Storrs, Connecticut, USA.
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Deshapriya
Department of Chemistry, University of Connecticut, Storrs, Connecticut, USA; Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA; Institute of Material Science, University of Connecticut, Storrs, Connecticut, USA; Department of Inorganic and Physical Chemistry, Indian Institute of Science, Bengaluru, Karnataka, India. Electronic address: challa.kumar@uconn.edu.
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Kumar
D055162:Biocatalysis; D015374:Biosensing Techniques; D002918:Chymotrypsin / Q000737:chemistry; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D007526:Isoelectric Point; D009113:Muramidase / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry*; D011485:Protein Binding; D011489:Protein Denaturation; D013816:Thermodynamics; D015040:Zirconium / Q000737:chemistry*
D004800:Enzymes, Immobilized; C027006:zirconium phosphate; D015040:Zirconium; D009113:Muramidase; D002918:Chymotrypsin
Exfoliation; Hemoglobin; Lysozyme; Myoglobin; Nanosheets; XRD; Zr(IV) phosphate