Nanozymes
constitute
a
category
of
nanomaterials
exhibiting
the
potential
to
replace
natural
enzymes.
Although
many
types
nanozymes
have
been
widely
reported
in
different
fields,
fabricating
with
ultrasmall
dimensions
and
expanding
their
applications
is
still
great
challenge.
In
this
study,
we
present
cost-effective,
one-step
methodology
for
producing
Cu2O@His.
Comparative
laccases,
Cu2O@His
demonstrates
remarkable
catalytic
capabilities
phenolic
catalysis,
alongside
robust
stability
economic
viability.
Therefore,
some
as
an
alternative
laccase
were
explored.
has
utilized
not
only
detection
epinephrine
but
also
degradation
tetracycline
antibiotics
(TCs).
addition,
four
kinds
TCs
successfully
distinguished
by
principal
component
analysis
(PCA).
Finally,
found
that
S2-
could
effectively
block
laccase-like
activity
Cu2O@His,
based
on
this,
constructed
method
sensitive
S2-.
This
work
provides
new
ideas
methods
development
study
activity.
Polymers,
Journal Year:
2024,
Volume and Issue:
16(7), P. 1010 - 1010
Published: April 8, 2024
The
enzyme
catalysis
conversion
of
lignocellulosic
biomass
into
valuable
chemicals
and
fuels
showed
a
bright
outlook
for
replacing
fossil
resources.
However,
the
high
cost
easy
deactivation
free
enzymes
restrict
process.
Immobilization
in
metal–organic
frameworks
(MOFs)
is
one
most
promising
strategies
due
to
MOF
materials’
tunable
building
units,
multiple
pore
structures,
excellent
biocompatibility.
Also,
MOFs
are
ideal
support
materials
could
enhance
stability
reusability
enzymes.
In
this
paper,
recent
progress
on
cellulose,
hemicellulose,
lignin
by
MOF-immobilized
extensively
reviewed.
This
paper
focuses
immobilized
performances
enzymatic
mechanism.
Finally,
challenges
discussed.
Remediation Journal,
Journal Year:
2025,
Volume and Issue:
35(2)
Published: Jan. 1, 2025
ABSTRACT
Hydrocarbon
contamination,
primarily
from
oil
spills
and
their
derivatives,
poses
significant
environmental
challenges
has
profound
impacts
on
public
health
ecosystems.
Innovative
bioremediation
strategies,
especially
those
utilizing
laccase
enzymes,
have
emerged
as
robust
sustainable
solutions
to
degrade
these
persistent
pollutants.
This
study
focused
optimizing
production
Enterobacter
sp.
GR18
,
isolated
the
Grawan
mineral
spring
near
Sardasht,
West
Azerbaijan
Province,
Iran.
The
bacterium
was
identified
through
comprehensive
biochemical
tests
16S
rRNA
sequencing.
Advanced
methodologies
were
used
optimize
conditions.
purified
enzyme
characterized
using
SDS‐PAGE.
effects
of
various
carbon
nitrogen
sources,
metal
ions,
inducers
enzymatic
activity
thoroughly
investigated.
Structural
changes
in
crude
samples
treated
with
analyzed
nuclear
magnetic
resonance
(NMR)
spectroscopy.
showed
exceptional
among
33
strains.
Glucose
yeast
extract
most
effective
respectively.
Copper
iron
ions
significantly
enhanced
activity.
NMR
spectroscopy
indicated
substantial
breakdown
complex
hydrocarbons
posttreatment,
demonstrating
enzyme's
effectiveness
hydrocarbon
degradation.
reveals
potential
for
high
efficient
degradation
under
extreme
These
findings
can
catalyze
development
technologies
address
contamination.
Materials,
Journal Year:
2023,
Volume and Issue:
16(19), P. 6572 - 6572
Published: Oct. 6, 2023
Oxidoreductases
are
a
wide
class
of
enzymes
that
can
catalyze
biological
oxidation
and
reduction
reactions.
Nowadays,
oxidoreductases
play
vital
part
in
most
bioenergetic
metabolic
pathways,
which
have
important
applications
biodegradation,
bioremediation,
environmental
applications,
as
well
biosensors.
However,
free
not
stable
hard
to
be
recycled.
In
addition,
cofactors
needed
reactions,
so
expensive
unstable
it
hinders
their
industrial
applications.
Enzyme
immobilization
is
feasible
strategy
overcome
these
problems.
Recently,
metal–organic
frameworks
(MOFs)
shown
great
potential
support
materials
for
immobilizing
due
unique
properties,
such
high
surface-area-to-volume
ratio,
chemical
stability,
functional
designability,
tunable
pore
size.
This
review
discussed
the
application
MOFs
composites
immobilized
carriers
oxidoreductase,
catalysts
redox
reactions
perspective
function
materials.
The
paper
also
focuses
on
MOF
carrier-based
oxidoreductase
designing
an
enzyme
cascade
reaction
system.
PLoS ONE,
Journal Year:
2024,
Volume and Issue:
19(7), P. e0304242 - e0304242
Published: July 18, 2024
In
this
work,
we
present
a
comprehensive
investigation
of
the
entrapment
laccase,
biotechnologically
relevant
enzyme,
into
levan-based
nanoparticles
(LNPs).
The
laccase
was
achieved
concomitantly
with
synthesis
LNP,
catalyzed
by
truncated
version
levansucrase
from
Leuconostoc
mesenteroides
.
study
aimed
to
obtain
biocompatible
nanomaterial,
able
entrap
functional
and
characterize
its
physicochemical,
kinetic
thermal
stability
properties.
experimental
findings
demonstrated
that
colloidal
stable
solution
spherically
shaped
an
average
diameter
68
nm,
obtained.
An
uniform
particle
size
distribution
observed,
according
polydispersity
index
determined
DLS.
When
LNPs
performed
in
presence
biocatalytically
active
1.25-fold
larger
(85
nm)
were
obtained,
maximum
load
243
μg
per
g
nanoparticle
achieved.
catalytic
efficiency
972
103
(μM·min)
-1
,
respectively,
for
free
entrapped
laccase.
A
decrease
k
cat
values
(from
7050
min
1823
-
1)
increase
apparent
Km
7.25
μM
17.73
μM)
observed
compared
enzyme.
exhibited
improved
stability,
retaining
40%
activity
after
1
h-incubation
at
70°C,
complete
inactivation
under
same
conditions,
thereby
highlighting
potential
preserving
enzyme
elevated
temperatures.
outcomes
significantly
contribute
field
nanobiotechnology
expanding
applications
presenting
innovative
strategy
enhancing
through
utilization
fructan-based
entrapments.
Chemistry - A European Journal,
Journal Year:
2024,
Volume and Issue:
unknown
Published: Oct. 18, 2024
Abstract
Laccase,
a
multi‐copper
oxidase,
is
limited
by
its
optimal
temperature
range
and
isolation
costs.
To
overcome
these
challenges,
we
synthesized
copper‐doped
zeolitic
imidazolate
framework‐67
(Cu‐doped
ZIF‐67)
with
16
mol
%
Cu
as
an
artificial
laccase
catalyst.
The
introduced
site
acts
the
phenol
oxidation
site,
Co‐based
ZIF‐67
four‐electron
oxygen
reduction
site.
Laccase
also
employs
this
division
of
sites.
Cu‐doped
demonstrated
significant
catalytic
activity,
superior
to
natural
laccase,
especially
at
elevated
temperatures,
maintained
stability
across
multiple
reaction
cycles.
These
findings
suggest
that
robust,
reusable
alternative
for
industrial
applications
requiring
high
thermal
efficient
catalysis.
Nanozymes
constitute
a
category
of
nanomaterials
exhibiting
the
potential
to
replace
natural
enzymes.
Although
many
types
nanozymes
have
been
widely
reported
in
different
fields,
fabricating
with
ultrasmall
dimensions
and
expanding
their
applications
is
still
great
challenge.
In
this
study,
we
present
cost-effective,
one-step
methodology
for
producing
Cu2O@His.
Comparative
laccases,
Cu2O@His
demonstrates
remarkable
catalytic
capabilities
phenolic
catalysis,
alongside
robust
stability
economic
viability.
Therefore,
some
as
an
alternative
laccase
were
explored.
has
utilized
not
only
detection
epinephrine
but
also
degradation
tetracycline
antibiotics.
addition,
four
kinds
TCs
successfully
distinguished
by
principal
component
analysis.
This
work
provides
new
ideas
methods
development
study
laccase-like
activity.
