Enzyme loading in the support and medium composition during immobilization alter activity, specificity and stability of octyl agarose-immobilized Eversa Transform
International Journal of Biological Macromolecules,
Год журнала:
2025,
Номер
295, С. 139667 - 139667
Опубликована: Янв. 9, 2025
Язык: Английский
The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading
Catalysts,
Год журнала:
2024,
Номер
14(2), С. 105 - 105
Опубликована: Янв. 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.
Язык: Английский
The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support
Biotechnology Progress,
Год журнала:
2023,
Номер
40(1)
Опубликована: Окт. 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.
Язык: Английский
Immobilization and Stabilization of D-allulose 3-epimerase for Continuous D-allulose Synthesis in Packed-Bed Reactors
Food Bioscience,
Год журнала:
2025,
Номер
unknown, С. 105959 - 105959
Опубликована: Янв. 1, 2025
Язык: Английский
Functionalized mesoporous biosilica for immobilizing D-allulose 3-epimerase: A multienzyme cascade strategy for calorie reduction in fruit tea drinks
Food Bioscience,
Год журнала:
2024,
Номер
unknown, С. 105331 - 105331
Опубликована: Окт. 1, 2024
Tuning almond lipase features by the buffer used during immobilization: The apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized
Journal of Biotechnology,
Год журнала:
2024,
Номер
391, С. 72 - 80
Опубликована: Июнь 13, 2024
The
lipase
from
Prunus
dulcis
almonds
was
inactivated
under
different
conditions.
At
pH
5
and
9,
enzyme
stability
remained
similar
the
studied
buffers.
However,
when
inactivation
performed
at
7,
there
were
some
clear
differences
on
depending
buffer
used.
more
stable
in
Gly
than
Tris
employed
for
inactivation.
Then,
immobilized
methacrylate
beads
coated
with
octadecyl
groups
7
presence
of
Gly,
Tris,
phosphate
HEPES.
Its
activity
assayed
versus
triacetin
S-methyl
mandelate.
biocatalyst
prepared
active
mandelate,
while
other
ones
triacetin.
depends
used
immobilization.
substrate
determined
activity.
For
example,
glycine
that
promoted
lowest
or
highest
stabilities
to
quantify
activities.
Язык: Английский
Tailored magnetic silica-immobilized D-allulose 3-epimerase with enhanced stability and recyclability for efficient D-allulose production
International Journal of Biological Macromolecules,
Год журнала:
2024,
Номер
unknown, С. 137896 - 137896
Опубликована: Ноя. 1, 2024
Язык: Английский
A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives
International Journal of Molecular Sciences,
Год журнала:
2024,
Номер
25(10), С. 5084 - 5084
Опубликована: Май 7, 2024
The
use
of
lipase
immobilized
on
an
octyl-agarose
support
to
obtain
the
optically
pure
enantiomers
chiral
drugs
in
reactions
carried
out
organic
solvents
is
a
great
challenge
for
chemical
and
pharmaceutical
sciences.
Therefore,
it
extremely
important
develop
optimal
procedures
achieve
high
enantioselectivity
biocatalysts
medium.
Our
paper
describes
new
approach
biocatalysis
performed
solvent
with
CALB-octyl-agarose
including
application
polypropylene
reactor,
appropriate
buffer
immobilization
(Tris
base-pH
9,
100
mM),
drying
step,
then
storage
lipases
climatic
chamber
or
refrigerator.
An
B
from
Candida
antarctica
(CALB)
was
used
kinetic
resolution
(R,S)-flurbiprofen
by
enantioselective
esterification
methanol,
reaching
enantiomeric
excess
(eep
=
89.6
±
2.0%).
As
part
optimization,
influence
different
buffers
investigated.
effect
reactor
material
reaction
medium
activity
also
studied.
Moreover,
stability
lipases:
rugosa
(CRL)
CALB
during
various
temperature
humidity
conditions
(climatic
refrigerator)
tested.
allowed
receiving
over
9-fold
higher
conversion
values
compared
results
achieved
when
conducting
glass
as
well
approximately
30-fold
comparison
free
lipase.
good
demonstrated.
After
7
days
refrigerator
(with
protection
humidity)
60%
were
obtained
observed
form
that
had
not
been
stored.
involving
indicates
significant
role
polymer
being
achieving
catalytic
activity.
Язык: Английский