Preparation of Biocatalytic Microparticles by Interfacial Self-Assembly of Enzyme-Nanoparticle Conjugates Around a Cross-Linkable Core

S M Andler; L-S Wang; J M Goddard; V M Rotello

doi:10.1016/bs.mie.2016.02.005

Preparation of Biocatalytic Microparticles by Interfacial Self-Assembly of Enzyme-Nanoparticle Conjugates Around a Cross-Linkable Core

Methods Enzymol. 2016:571:1-17. doi: 10.1016/bs.mie.2016.02.005. Epub 2016 Mar 11.

Authors

S M Andler¹, L-S Wang², J M Goddard¹, V M Rotello³

Affiliations

¹ Department of Food Science, University of Massachusetts-Amherst, Amherst, Massachusetts, USA.
² Department of Chemistry, University of Massachusetts-Amherst, Amherst, Massachusetts, USA.
³ Department of Chemistry, University of Massachusetts-Amherst, Amherst, Massachusetts, USA. Electronic address: rotello@chem.umass.edu.

PMID: 27112392
DOI: 10.1016/bs.mie.2016.02.005

Abstract

Rational design of hierarchical interfacial assembly of reusable biocatalytic microparticles is described in this chapter. Specifically, purified enzymes and functionalized nanoparticles are electrostatically assembled at the interface of cross-linked microparticles which are formed through ring opening metathesis polymerization. The diameters of microparticle assemblies average 10μm, and they show enhanced kinetic efficiency as well as improved stability against heat, pH, and solvent denaturation when compared to stabilities of the corresponding native enzymes.

Keywords: Enzyme; Hierarchical assembly; Immobilization; Nano; Reusable.

MeSH terms

Biocatalysis
Enzyme Stability
Enzymes, Immobilized / chemistry*
Fungal Proteins / chemistry*
Fungal Proteins / isolation & purification
Hydrogen-Ion Concentration
Kinetics
Lipase / chemistry*
Lipase / isolation & purification
Nanoparticles / chemistry*
Polymerization
Protein Denaturation
Solvents / chemistry

Substances

Enzymes, Immobilized
Fungal Proteins
Solvents
Lipase
lipase B, Candida antarctica