Frontiers in Bioengineering and Biotechnology,
Journal Year:
2022,
Volume and Issue:
10
Published: March 2, 2022
Enzymes
play
vital
roles
in
all
organisms.
The
enzymatic
process
is
progressively
at
its
peak,
mainly
for
producing
biochemical
products
with
a
higher
value.
immobilization
of
enzymes
can
sometimes
tremendously
improve
the
outcome
biocatalytic
processes,
making
product(s)
relatively
pure
and
economical.
Carrier-free
immobilized
increase
yield
product
stability
enzyme
biocatalysis.
Immobilized
are
easier
to
purify.
Due
these
varied
advantages,
researchers
tempted
explore
carrier-free
methods
used
enzymes.
In
this
review
article,
we
have
discussed
various
aspects
immobilization,
approaches
followed
design
an
advantages
disadvantages
common
processes
immobilization.
International Journal of Molecular Sciences,
Journal Year:
2022,
Volume and Issue:
23(17), P. 10116 - 10116
Published: Sept. 4, 2022
Thermophilic
proteins
have
various
practical
applications
in
theoretical
research
and
industry.
In
recent
years,
the
demand
for
thermophilic
on
an
industrial
scale
has
been
increasing;
therefore,
engineering
of
become
a
hot
direction
field
protein
engineering.
However,
exact
mechanism
thermostability
is
not
yet
known,
knowing
basis
necessary.
order
to
understand
proteins,
we
made
statistical
analysis
sequences,
secondary
structures,
hydrogen
bonds,
salt
bridges,
DHA
(Donor–Hydrogen–Accepter)
angles,
bond
lengths
ten
pairs
their
non-thermophilic
orthologous.
Our
findings
suggest
that
polar
amino
acids
contribute
by
forming
bonds
bridges
which
provide
resistance
against
denaturation.
Short
length
wider
angle
greater
stability
proteins.
Moreover,
increased
frequency
aromatic
contributes
thermal
more
interactions.
Additionally,
coil,
helix,
loop
structure
also
thermostability.
Angewandte Chemie International Edition,
Journal Year:
2023,
Volume and Issue:
62(20)
Published: March 14, 2023
Enzyme
immobilization
has
been
demonstrated
to
be
a
favorable
protocol
for
promoting
the
industrialization
of
bioactive
molecules,
but
still
with
formidable
challenge.
Addressing
this
challenge,
we
create
dynamic
defect
generation
strategy
enzyme
by
using
dissociation
equilibrium
metal-organic
frameworks
(MOFs)
mediated
enzymes.
Enzymes
can
act
as
"macro
ligands"
generate
competitive
coordination
against
original
ligands,
along
release
metal
clusters
MOFs
defects,
hence
gradual
transport
enzymes
from
surface
inside.
Various
efficiently
immobilized
in
afford
composites
good
enzymatic
activities,
protective
performances
and
exceptional
reusabilities.
Moreover,
multienzyme
bioreactors
capable
efficient
cascade
reactions
also
generated.
This
study
provides
new
opportunities
construct
highly
biocatalysts
incorporating
different
types
Journal of the American Chemical Society,
Journal Year:
2023,
Volume and Issue:
145(15), P. 8647 - 8655
Published: April 6, 2023
Despite
significant
efforts,
it
remains
a
challenge
to
design
artificial
enzymes
that
can
mimic
both
structures
and
functions
of
natural
enzymes.
Here,
we
report
the
post-synthetic
construction
binuclear
iron
catalysts
in
MOF-253
di-iron
monooxygenases.
The
adjacent
bipyridyl
(bpy)
linkers
freely
rotate
form
[(bpy)FeIII(μ2-OH)]2
active
site
self-adaptive
fashion.
composition
structure
sites
were
characterized
by
combination
inductively
coupled
plasma-mass
spectrometry,
thermogravimetric
analysis,
X-ray
absorption
Fourier-transform
infrared
spectroscopy.
MOF-based
monooxygenase
effectively
catalyzed
oxidative
transformations
organic
compounds,
including
C-H
oxidation
alkene
epoxidation
reactions,
using
O2
as
only
oxidant,
which
indicates
successful
recapitulation
monooxygenases
readily
accessible
MOFs.
system
exhibited
at
least
27
times
higher
catalytic
activity
than
corresponding
mononuclear
control.
DFT
calculations
showed
had
14.2
kcal/mol
lower
energy
barrier
rate-determining
activation
process,
suggesting
importance
cooperativity
centers
step.
stability
recyclability
also
demonstrated.
Journal of the American Chemical Society,
Journal Year:
2023,
Volume and Issue:
145(37), P. 20365 - 20374
Published: Sept. 6, 2023
This
study
reports
the
successful
development
of
a
sustainable
synthesis
protocol
for
phase-pure
metal
azolate
framework
(MAF-6)
and
its
application
in
enzyme
immobilization.
An
esterase@MAF-6
biocomposite
was
synthesized,
catalytic
performance
compared
with
that
esterase@ZIF-8
esterase@ZIF-90
transesterification
reactions.
Esterase@MAF-6,
large
pore
aperture,
showed
superior
enzymatic
to
catalyzing
reactions
using
both
n-propanol
benzyl
alcohol
as
reactants.
The
hydrophobic
nature
MAF-6
platform
shown
activate
immobilized
esterase
into
open-lid
conformation,
which
exhibited
1.5-
4-times
activity
free
reaction
alcohol,
respectively.
present
work
offers
insights
potential
promising
matrix
immobilization
highlights
need
explore
MOF
matrices
expanded
apertures
broaden
their
practical
applications
biocatalysis.
Journal of Agricultural and Food Chemistry,
Journal Year:
2025,
Volume and Issue:
unknown
Published: March 25, 2025
Aflatoxin
B1
(AFB1)
is
considered
a
critical
analyte
in
food
safety
testing
due
to
its
widespread
contamination
and
high
toxicity.
In
this
study,
ratiometric
fluorescent
immunosensor
with
synergistic
catalysis
by
natural
enzymes
nanozymes
(N-N-RF-immunosensor)
was
constructed
for
the
rapid
detection
of
AFB1.
Copper
oxide
zeolitic
imidazolate
framework
composite
nanomaterials
(CuO/ZIF-8
NCM)
peroxidase
oxidase
activities
were
prepared.
A
fluorescence
signal
generated
through
cocatalytic
effect
CuO/ZIF-8
NCM
alkaline
phosphatase,
response
competition
interaction
between
anti-idiotypic
nanobody-alkaline
phosphatase
fusion
protein
(Nb2-5-AP)
The
assay
could
detect
aflatoxins
within
140
min,
exhibiting
half
maximal
inhibitory
concentration
(IC50)
0.032
ng/mL,
limit
(LOD)
2.4
pg/mL,
linear
range
0.0024-1.043
ng/mL.
Compared
traditional
enzyme-linked
immunosorbent
(ELISA),
sensitivity
enhanced
25-fold,
while
parameter
shortened
1/3.
Furthermore,
successfully
applied
actual
samples,
recoveries
ranging
from
81
127%.
N-N-RF-immunosensor
shows
great
potential
sensitive
aflatoxins.
