Research Square (Research Square),
Journal Year:
2023,
Volume and Issue:
unknown
Published: Oct. 28, 2023
Abstract
Removing
anionic
pollutants
from
water
sources
remains
a
major
challenge
in
supramolecular
chemistry.
Today,
cellulose,
activated
carbon,
zeolite,
and
similar
materials,
which
are
widely
preferred,
have
weak
effect
against
pollutants.
Therefore,
further
modifications
needed
for
the
use
of
such
substances.
On
contrary,
this
study,
highly
functional
economical
polymeric
particles
(called
GD
particles)
were
synthesized
with
high
yield
did
not
require
modifications.
glutaraldehyde
diethylenetriamine
as
monomers
first
time.
The
structural
properties
characterized
by
FT-IR,
TGA,
SEM
analyses.
Then,
used
adsorption
Bromophenol
blue
phenol.
isotherm,
thermodynamic,
kinetic
models
to
explain
mechanism
between
blue,
phenol,
particles.
Thus,
it
was
determined
that
process
chemisorption,
phenol
particles,
physical
took
place.
It
polymer
had
capacities,
136.40
mg/g
bromophenol
98.26
than
natural
adsorbents.
As
result,
produced
economical,
simple,
feasible,
adsorbents
Science Advances,
Journal Year:
2025,
Volume and Issue:
11(11)
Published: March 12, 2025
Directed
evolution,
enzyme
design,
and
effective
immobilization
have
been
used
to
improve
the
catalytic
activity.
Dynamic
polymers
offer
a
promising
platform
activity
in
aqueous
solutions.
Here,
amphiphilic
dynamers
lipase
self-assemble
into
nanoparticles
of
150-
600-nanometer
diameter,
showing
remarkable
threefold
enhancement
In
addition,
they
also
demonstrated
ability
promote
reversible
refolding
partially
or
completely
denatured
lipase.
The
efficiency
is
completed
with
its
more
convenient
handling
dynameric
facilitating
efficient
recovery
reuse
cost-effective
uses.
Molecular
simulation
studies
revealed
an
in-depth
understanding
how
dynamer
action
mechanism
affects
conformational
changes
served
as
hydrophobic
support,
lid
opening
substrate
access
triad,
resulting
substantial
activation
improved
stability
recyclability
Processes,
Journal Year:
2024,
Volume and Issue:
12(4), P. 634 - 634
Published: March 22, 2024
The
use
of
edible
oils
and
fats
in
dairy
products
is
becoming
increasingly
important
the
food
industry
because
their
complementary
functional
properties.
Most
these
are
produced
using
food-grade
enzymes
as
processing
aids
processes
involving
considered
mild
environmentally
friendly
for
regulatory
purposes.
poor
stability
recovery
native
state
limit
performance,
to
enhance
activity,
stability,
reusability,
often
immobilised—a
process
that
involves
attaching
them
a
solid
support.
Additionally,
immobilisation
enables
selectively
target
specific
substrates
or
products,
making
highly
efficient.
These
features
have
led
increased
immobilised
lipid
been
used
produce
broad
range
such
whey
protein
concentrates
isolates,
peptide–lipid
conjugates,
concentrates,
structured
lipids,
human
milk
fat
substitutes.
Therefore,
this
article
reviews
current
progress
on
different
enzyme
preparations
processing.
It
also
summarises
opportunities
enzyme-catalysed
valorisation
waste
streams
with
ultimate
goals
sustainable
production
reductions
waste.
ACS Sustainable Chemistry & Engineering,
Journal Year:
2024,
Volume and Issue:
12(17), P. 6564 - 6572
Published: April 18, 2024
In
the
present
article,
glutaraldehyde
was
used
to
covalently
coimmobilize
lipase
Eversa
Transform
2.0
and
β-galactosidase
from
Aspergillus
oryzae.
Both
enzymes
were
adsorbed
on
amino
supports
modified
with
glutaraldehyde.
However,
first
enzyme
remained
almost
fully
active
under
stress
conditions,
while
lost
a
large
percentage
of
its
activity.
To
prevent
necessity
discarding
both
enzymes,
immobilized
following
this
immobilization
strategy.
The
biocatalyst
reduced
eliminate
chemical
reactivity,
then
coimmobilized
via
ion
exchange.
incubation
at
high
concentrations
salt
desorbed
support.
This
combi-biocatalyst
in
three
inactivation/rebuilding
cycles
where
inactivated
liberated
by
washing
ionic
strength
replaced
fresh
enzyme,
maintained
activity
throughout
3
cycles.
That
way,
it
possible
use
strategy
reuse
build
new
combi-biocatalysts
after
inactivation.
ChemistrySelect,
Journal Year:
2024,
Volume and Issue:
9(26)
Published: July 4, 2024
Abstract
In
this
study,
trimethylolpropane
triglycidyl
ether/diethylenetriamine
(TD)
and
glutaraldehyde/diethylenetriamine
(GD)
polymer
particles
are
synthesized
as
catalysts
for
hydrogen
production
from
NaBH
4
methanolysis
electrooxidation.
SEM,
FT‐IR
TGA
characterization
methods
applied
to
determine
the
surface
morphologies,
chemical
structures,
thermal
stability
decomposition
of
particles.
The
parameters
affecting
generation
rate
on
investigated
optimum
conditions
determined.
Under
conditions,
rates
TD
GD
obtained
34903.2
97998
mL/min.g
cat
,
respectively.
activation
energies
also
calculated
16.86
18.14
kJ/mol,
catalytic
activities
anode
in
electrooxidation
determined
by
CV,
CA,
EIS
analyses.
specific
acquired
0.54
0.64
mA/cm
2
These
results
indicate
that
promising
sodium
borohydride.
Catalysts,
Journal Year:
2024,
Volume and Issue:
14(2), P. 105 - 105
Published: Jan. 26, 2024
The
lipases
from
Thermomyces
lanuginosus
(TLL)
and
Candida
antarctica
(B)
(CALB)
were
immobilized
on
octyl-agarose
beads
at
1
mg/g
(a
loading
under
the
capacity
of
support)
by
overloading
support
with
enzymes.
These
biocatalysts
compared
in
their
stabilities
10
mM
sodium
phosphate,
HEPES,
Tris-HCl
pH
7.
Lowly
loaded
CALB
was
more
stable
than
highly
preparation,
while
TLL
this
effect
smaller.
Phosphate
very
negative
for
stability
biocatalyst
moderately
using
both
loadings.
enzymes
HEPES
presented
a
different
response
as
function
enzyme
(e.g.,
lowly
CALB,
similar
buffers,
but
it
clearly
smaller
biocatalysts).
Moreover,
specific
activity
versus
p-nitrophenol
butyrate,
triacetin
R-
or
S-methyl
mandelate
depended
buffer,
loading,
interaction
between
them.
In
some
cases,
almost
twice
expected
could
be
obtained
octyl-CALB,
depending
buffer.
A
co-interaction
effects
specificity
buffer
nature
detected.
Catalysts,
Journal Year:
2024,
Volume and Issue:
14(2), P. 115 - 115
Published: Jan. 31, 2024
The
lipase
from
Prunus
dulcis
almonds
has
been
immobilized
for
the
first
time.
For
this
purpose,
two
different
supports,
an
octadecyl
methacrylate
particulate
support,
and
aminated
agarose
(monoaminoethyl-N-aminoethyl)
have
utilized.
Both
biocatalysts
show
improved
enzyme
stability,
but
great
changes
in
specificity
were
detected.
via
ion
exchange
maintained
its
activity
intact
versus
p-nitrophenyl
butyrate,
while
on
hydrophobic
support
fully
lost
substrate,
which
was
confirmed
to
be
due
substrate
adsorption
support.
However,
biocatalyst
much
more
active
triacetin
(more
than
10-fold),
R-
or
S-
methyl
mandelate
at
pH
7.
At
9,
a
strong
effect
of
using
phosphate
bicarbonate
as
reaction
buffers
Using
bicarbonate,
interfacially
presented
no
R-isomer,
it
very
S-isomer
triacetin.
buffer
during
reaction,
all
compounds
recognized
substrates.
significantly
phosphate;
fact,
inactive
both
isomers.
This
paper
shows
time
interaction
between
effects
immobilization
protocol
used
enantiospecificity
lipases.
Biotechnology Progress,
Journal Year:
2023,
Volume and Issue:
40(1)
Published: Oct. 12, 2023
In
this
article,
we
have
analyzed
the
interactions
between
enzyme
crowding
on
a
given
support
and
its
chemical
modification
(ethylenediamine
via
carbodiimide
route
picryl
sulfonic
(TNBS)
of
primary
amino
groups)
activity
stability.
Lipase
from
Thermomyces
lanuginosus
(TLL)
lipase
B
Candida
antarctica
(CALB)
were
immobilized
octyl-agarose
beads
at
two
very
different
loadings,
one
them
exceeding
capacity
support,
well
under
capacity.
Chemical
modifications
highly
loaded
lowly
biocatalysts
gave
results
in
terms
stability,
which
could
increase
or
decrease
depending
loading.
For
example,
both
increased
their
after
while
effect
was
opposite
for
biocatalysts.
Additionally,
with
TNBS
CALB
biocatalyst
stability
activity.
