Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.2.1.17 (
lysozyme
)
21,489
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
We report a simple and rapid method for the deposition of amorphous silica onto a gold surface. The method is based on the ability of
lysozyme
to mediate the formation of silica nanoparticles. A monolayer of
lysozyme
is deposited via non-specific binding to gold. The
lysozyme
then mediates the self-assembled formation of a silica monolayer. The silica formation described herein occurs on a surface plasmon resonance (SPR) gold surface and is characterized by SPR spectroscopy. The silica layer significantly increases the surface area compared to the gold substrate and is directly compatible with a detection system. The maximum surface concentration of
lysozyme
was found to be a monolayer of 2.6 ng/mm(2) which allowed the deposition of a silica layer of a further 2 ng/mm(2). For additional surface functionalization, the silica was also demonstrated to be a suitable matrix for immobilization of biomolecules. The encapsulation of
organophosphate hydrolase
(
OPH
) was demonstrated as a model system. The silica forms at ambient conditions in a reaction that allows the encapsulation of enzymes directly during silica formation.
OPH
was successfully encapsulated within the silica particles and a detection limit for the substrate, paraoxon, using the surface-encapsulated enzyme was found to be 20 microM.
...
PMID:Enzyme-encapsulated silica monolayers for rapid functionalization of a gold surface. 1699 52
The opd gene, encoding
organophosphorus hydrolase
(
OPH
) from Flavobacterium sp. capable of degrading a wide range of organophosphate pesticides, was surface- and intracellular-expressed in Synechococcus PCC7942, a prime example of photoautotrophic cyanobacteria.
OPH
was displayed on the cyanobacterial cell surface using the truncated ice nucleation protein as an anchoring motif. A minor fraction of
OPH
was displayed onto the outermost surface of cyanobacterial cells, as verified by immunostaining visualized under confocal laser scanning microscopy and
OPH
activity analysis; however, a substantial fraction of
OPH
was buried in the cell wall, as demonstrated by proteinase K and
lysozyme
treatments. The cyanobacterial outer membrane acts as a substrate (paraoxon) diffusion barrier affecting whole-cell biodegradation efficiency. After freeze-thaw treatment, permeabilized whole cells with intracellular-expressed
OPH
exhibited 14-fold higher bioconversion efficiency (Vmax/Km) than that of cells with surface-expressed
OPH
. As cyanobacteria have simple growth requirements and are inexpensive to maintain, expression of
OPH
in cyanobacteria may lead to the development of a lowcost and low-maintenance biocatalyst that is useful for detoxification of organophosphate pesticides.
...
PMID:Biodegradation of organophosphate pesticide using recombinant Cyanobacteria with surface- and intracellular-expressed organophosphorus hydrolase. 1863 96
