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Hydrolases on silica surfaces: Coverage-activity–molecular property relationships revealed

Paper ID Volume ID Publish Year Pages File Format Full-Text
34526 45032 2014 10 PDF Available
Title
Hydrolases on silica surfaces: Coverage-activity–molecular property relationships revealed
Abstract

•A novel surface–protein and protein–protein interaction model is confirmed.•The model correlates surface coverage and changes in conformation and orientation.•The model explains catalytic competency of fumed-silica based nanobiocatalysts.•Conformational changes of immobilized enzymes depend on intrinsic packing density.

A set of recommendations to maintain high activity of immobilized enzymes is developed based on direct observation via AFM. This helps to close knowledge gaps that often lead to poor performance of nanobiocatalysts for chemical synthesis. Molecule-level height and volume distribution analyses from high-resolution AFM images were applied to Candida antarctica Lipase B (CALB), subtilisin Carlsberg, and the Lipase from Thermomyces lanuginosus (TLL) deposited on model silica surfaces. Ensembles of flexible or “soft” enzymes appear separated when interactions with the surface are considerable at low surface coverage but form highly entangled structures of increased conformational stability at high surface coverage. By contrast, ensembles of rigid or “hard” enzymes appear to maintain stable aggregates even under strong interaction with the surface. The more rigid the enzyme the higher its tendency to remain in a densely packed state that is able to withstand surface-induced conformational transitions detrimental to catalysis. Weakening of surface-protein interactions for “soft” enzymes will prevent single-molecule immobilization, which reduces catalytic competency through structural changes. Multi-layer coverage in enzyme immobilization should generally be avoided due to mass transfer limitations.

Keywords
Conformational stability; AFM; Silica; Protein–surface interactions; Protein–protein interactions
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 5, May 2014, Pages 830–839
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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