Nanoporous silica glass for the immobilization of interactive enzyme systems.

Andreas Buthe, Songtao Wu, Ping Wang

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Recent pursuit on utilization of nanoscale materials has manifested a variety of configurations of highly efficient enzymic biocatalyst systems for biotechnological applications. Nanoscale structures are particularly powerful in effecting multienzyme biocatalysis. Inherent properties of nanomaterials--primarily, the high surface area to volume ratio and atomic scale 3D configurations--enable higher enzyme loadings, microenvironment control surrounding enzyme molecules, regulation on mass transfer, and protein structural stabilization of the biocatalyst as compared to traditional immobilization systems. This chapter introduces one versatile nanoscale immobilization method via details demonstrated using the case of nanoporous silica glass (30 nm diameter) for the concomitant incorporation of lactate dehydrogenase (LDH), glucose dehydrogenase (GDH), and the cofactor (NADH).

Original languageEnglish (US)
Pages (from-to)37-48
Number of pages12
JournalMethods in molecular biology (Clifton, N.J.)
Volume679
DOIs
StatePublished - 2011

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