4.7 Article

Conformational changes and catalytic competency of hydrolases adsorbing on fumed silica nanoparticles: II. Secondary structure

Journal

COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 81, Issue 1, Pages 1-10

Publisher

ELSEVIER
DOI: 10.1016/j.colsurfb.2010.06.005

Keywords

Conformational stability; Adsorption; Fumed silica; Protein-surface interactions; FTIR; CD

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Secondary conformational analysis via Circular Dichroism (CD) and Amide-I FTIR was applied to preparations of Candida antarctica Lipase B (CALB), subtilisin Carlsberg, and the Lipase from Thermomyces lanuginosus (TLL) on fumed silica to confirm that the hardness and packing density of the enzymes on the solid fumed silica nanoparticle surface can be used to rationalize the variable enzyme-dependent changes of catalytic competency with surface coverage. Soft enzymes should be immobilized at a surface coverage where enzyme-enzyme interactions predominate thereby preventing detrimental structural changes caused by enzyme-support interactions, while hard enzymes can be immobilized at low to intermediate surface coverage with good catalytic performance. Multi-layered coverage reduces the superficial average catalytic performance in all cases due to mass transfer limitations. (C) 2010 Elsevier By. All rights reserved.

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