2016
DOI: 10.1002/anie.201600590
|View full text |Cite
|
Sign up to set email alerts
|

Enzyme Shielding in an Enzyme‐thin and Soft Organosilica Layer

Abstract: The fragile nature of most enzymes is a major hindrance to their use in industrial processes. Herein, we describe a synthetic chemical strategy to produce hybrid organic/inorganic nanobiocatalysts; it exploits the self-assembly of silane building blocks at the surface of enzymes to grow an organosilica layer, of controlled thickness, that fully shields the enzyme. Remarkably, the enzyme triggers a rearrangement of this organosilica layer into a significantly soft structure. We demonstrate that this change in s… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

1
57
0

Year Published

2016
2016
2023
2023

Publication Types

Select...
7
1

Relationship

3
5

Authors

Journals

citations
Cited by 44 publications
(59 citation statements)
references
References 23 publications
(16 reference statements)
1
57
0
Order By: Relevance
“…Concomitantly, AP activity dropped from 90±1.2 U g −1 (U per gram of SNPs) to 11±0.2 U g −1 . This loss in activity was consistent with our previous results, where we demonstrated that a curing phase is necessary to recover enzymatic activity through reorganization of the protective organosilica layer . Accordingly, the particles were incubated at 25 °C for 24 h for the curing reaction.…”
Section: Figuresupporting
confidence: 92%
“…Concomitantly, AP activity dropped from 90±1.2 U g −1 (U per gram of SNPs) to 11±0.2 U g −1 . This loss in activity was consistent with our previous results, where we demonstrated that a curing phase is necessary to recover enzymatic activity through reorganization of the protective organosilica layer . Accordingly, the particles were incubated at 25 °C for 24 h for the curing reaction.…”
Section: Figuresupporting
confidence: 92%
“…16 Working on the development of nanomaterials endowed with virus recognition properties, 17,18 we have designed a chemical strategy that allows embedding enzymes in a biomimetic and soft organosilica layer. 19,20 In the present work, we have expanded this shielding strategy to artificial metalloenzymes and tested the resulting nanocatalysts for the reduction of cyclic imine 1 in the presence of various cellular extracts. As shown previously with soluble ArMs, embedding the biotinylated pianostool iridium complex [Cp*Ir(biot-p-L)Cl] within various streptavidin mutants (Sav hereafter) allows to access either (R)-and (S)-salsolidine 2 (Fig.…”
mentioning
confidence: 99%
“…The time-point assay showed only a slight erosion of enantioselectivity over the course of 7 days (decrease of 11%), which could be explained by disruption of the protective layer and leakage of the catalyst caused by friction in solution. 20 However, the ICP-MS measurements of the reaction medium after the reaction revealed only traces of iridium. We thus argue that the decrease in activity is predominantly caused by loss of nanoparticles during centrifugation and washing cycles.…”
mentioning
confidence: 99%
“…We have demonstrated that enzymes, when immobilized at the surface of silica and shielded in a soft organosilica shell, retain their enzymatic activity with a drastic improvement of their stability against external stress conditions. [49] In the same context, we also demonstrated that enzyme-polymer conjugates can be attached in a stable yet reversible fashion on polymeric filtration membranes exploiting surface supramolecular interactions. [50] The commercial implementation of the enzyme protection technology developed is now carried out by INOFEA AG, a biotech company that spun-off from the activities of our laboratory.…”
Section: In Silica Protein Engineering: From Molecular Recognition Tomentioning
confidence: 65%