Heterofunctional Methacrylate Beads Bearing Octadecyl and Vinyl Sulfone Groups: Tricks to Obtain an Interfacially Activated Lipase from Thermomyces lanuginosus and Covalently Attached to the Support
Catalysts,
Journal Year:
2023,
Volume and Issue:
13(1), P. 108 - 108
Published: Jan. 3, 2023
Lipase
from
Thermomyces
lanuginosus
(TLL)
has
been
immobilized
on
a
methacrylate
macroporous
resin
coated
with
octadecyl
groups
(Purolite
Lifetech®®
ECR8806F).
This
immobilization
protocol
gave
biocatalyst
significantly
higher
stability
than
that
obtained
using
octyl
agarose.
To
further
improve
the
features,
we
tried
to
covalently
immobilize
enzyme
this
support.
For
purpose,
support
was
activated
divinyl
sulfone.
The
results
showed
at
least
1/3
of
molecules
were
not
immobilized.
solve
problem,
produced
an
aminated
and
then
it
permitted
full
covalent
previously
TLL.
use
different
blocking
agents
as
reaction
endpoint
(using
ethylenediamine,
Asp,
Gly,
Cys)
greatly
altered
functional
features
(activity,
specificity,
or
stability).
example,
ethylenediamine
increased
ratio
activity
versus
R-
S-methyl
mandelate
by
three-fold
factor.
Cys
most
stable
biocatalyst,
maintaining
close
90%
under
conditions
where
just
adsorbed
maintained
less
55%.
That
way,
strategy
modify
obtaining
interfacially
layer
and,
later,
vinyl
sulfone
groups.
Language: Английский
Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization
Molecules,
Journal Year:
2024,
Volume and Issue:
29(3), P. 628 - 628
Published: Jan. 29, 2024
This
work
presents
a
framework
for
evaluating
hybrid
nanoflowers
using
Burkholderia
cepacia
lipase.
It
was
expanded
on
previous
findings
by
testing
lipase
(hNF-lipase)
formation
over
wide
range
of
pH
values
(5–9)
and
buffer
concentrations
(10–100
mM).
The
free
enzyme
activity
compared
with
that
hNF-lipase.
analysis,
performed
molecular
docking,
described
the
effect
interaction
copper
ions.
morphological
characterization
hNF-lipase
scanning
electron
microscopy.
Fourier
Transform
Infrared
Spectroscopy
physical–chemical
characterization.
results
show
all
presented
higher
than
enzyme.
Activity
is
at
7.4
has
highest
concentration
100
mM.
Molecular
docking
analysis
been
used
to
understand
protonation
identify
main
binding
sites
nanostructures
shape
flowers
in
their
micrographs
from
6
8.
spectra
present
peaks
typical
amide
regions
I
II,
current
lipase,
areas
P–O
vibrations,
confirming
presence
phosphate
group.
Therefore,
an
efficient
biocatalyst
increased
catalytic
activity,
good
nanostructure
formation,
improved
stability.
Language: Английский
Enzyme Immobilization
Molecules,
Journal Year:
2023,
Volume and Issue:
28(3), P. 1373 - 1373
Published: Feb. 1, 2023
The
development
of
enzyme
immobilization
started
in
the
middle
previous
century
as
a
potential
answer
to
problem
recovery
and
reuse
[...]
Language: Английский
The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
International Journal of Biological Macromolecules,
Journal Year:
2022,
Volume and Issue:
222, P. 2452 - 2466
Published: Oct. 8, 2022
Mineralization
of
immobilized
enzymes
has
showed
to
couple
the
advantages
both
processes.
Here,
influence
immobilization
protocol
on
effects
mineralization
been
investigated.
The
lipases
from
Thermomyces
lanuginosus
and
Candida
rugosa
were
octyl-,
vinyl
sulfone
(VS)
octyl
(blocked
with
different
nucleophiles)
glutaraldehyde-
(at
pH
values)
agarose
beads.
stability,
activity
specificity
biocatalysts
very
different,
differently
blocked
VS-biocatalysts
glutaraldehyde
prepared
at
pH.
All
submitted
using
metals.
activity,
stability
strongly
depended
enzyme
protocol.
For
same
enzyme,
a
could
be
negative,
positive
or
present
no
effect
depending
procedure
substrate.
In
best
cases,
increased
by
two-fold
factor,
while
was
significantly
improved
in
many
instances.
These
results
highlight
great
potential
improve
their
properties,
as
well
interactions
that
can
exhibit.
combination
methodologies
greatly
increases
possibilities
find
biocatalyst
suitable
for
specific
process.
Language: Английский
Synthesis of Novel Polymer-Assisted Organic-Inorganic Hybrid Nanoflowers and Their Application in Cascade Biocatalysis
Molecules,
Journal Year:
2023,
Volume and Issue:
28(2), P. 839 - 839
Published: Jan. 14, 2023
This
study
reports
on
the
synthesis
of
novel
bienzyme
polymer-assisted
nanoflower
complexes
(PANF),
their
morphological
and
structural
characterization,
effectiveness
as
cascade
biocatalysts.
First,
highly
porous
polyamide
6
microparticles
(PA6
MP)
are
synthesized
by
activated
anionic
polymerization
in
solution.
Second,
PA6
MP
used
carriers
for
hybrid
assemblies
comprising
glucose
oxidase
(GOx)
horseradish
peroxidase
(HRP).
Thus,
four
PANF
with
different
co-localization
compartmentalization
two
enzymes
prepared.
In
samples
NF
GH/PA
GH@PA,
both
localized
within
same
flowerlike
organic-inorganic
nanostructures
(NF),
difference
being
way
assembled
NF.
G/PAiH
G@PAiH,
only
GOx
is
located
NF,
while
HRP
preliminary
immobilized
MP.
The
morphology
structure
have
been
studied
microscopy,
spectroscopy,
synchrotron
X-ray
techniques.
catalytic
activity
was
assessed
a
two-step
reaction
oxidation.
up
to
2-3
times
more
active
than
free
GOx/HRP
dyad.
They
also
display
enhanced
kinetic
parameters,
superior
thermal
stability
40-60
°C
range,
optimum
performance
at
pH
4-6,
excellent
storage
stability.
All
consecutive
operational
cycles.
Language: Английский
Tuning Immobilized Enzyme Features by Combining Solid-Phase Physicochemical Modification and Mineralization
International Journal of Molecular Sciences,
Journal Year:
2022,
Volume and Issue:
23(21), P. 12808 - 12808
Published: Oct. 24, 2022
Lipase
B
from
Candida
antarctica
(CALB)
and
lipase
Thermomyces
lanuginosus
(TLL)
were
immobilized
on
octyl
agarose.
Then,
the
biocatalysts
chemically
modified
using
glutaraldehyde,
trinitrobenzenesulfonic
acid
or
ethylenediamine
carbodiimide,
physically
coated
with
ionic
polymers,
such
as
polyethylenimine
(PEI)
dextran
sulfate.
These
produced
alterations
of
enzyme
activities
have,
in
most
cases,
negative
effects
some
substrates
positive
other
ones
(e.g.,
amination
TLL
increases
activity
versus
p-nitro
phenyl
butyrate
(p-NPB),
reduces
R-methyl
mandate
by
half
maintains
S-isomer).
The
modification
PEI
increased
biocatalyst
8-fold
mandelate.
Enzyme
stability
was
also
modified,
usually
showing
an
improvement
glutaraldehyde
enabled
to
maintain
more
than
70%
initial
activity,
while
unmodified
maintained
less
50%).
enzymes
mineralized
phosphate
metals
(Zn2+,
Co2+,
Cu2+,
Ni2+
Mg2+),
this
affected
specificity
its
after
zinc
mineralization
triacetin,
decreased
all
assayed
substrates)
same
increase
residual
almost
0
60%).
Depending
enzyme,
a
metal
could
be
positively,
neutrally
negatively
for
specific
feature.
Finally,
we
analyzed
if
chemical
could,
somehow,
tune
mineralization.
Effectively,
have
very
different
it
previously
submitted
physicochemical
modifications.
present
stability,
depending
previous
performed
that
these
modifications
alter
features.
For
example,
treated
salts
mandelate,
maintaining
unaltered
substrates,
whereas
aminated
both
methyl
mandelate
isomers,
p-NPB
triacetin.
found
easier
CALB
strategies
used
paper.
In
way,
combination
physical
before
their
range
features
can
experienced,
enabling
enlarge
library.
Language: Английский
Mineralization of Lipase from Thermomyces lanuginosus Immobilized on Methacrylate Beads Bearing Octadecyl Groups to Improve Enzyme Features
Catalysts,
Journal Year:
2022,
Volume and Issue:
12(12), P. 1552 - 1552
Published: Dec. 1, 2022
Lipase
from
Thermomyces
lanuginosus
(TLL)
has
been
immobilized
on
Purolite
Lifetech®
ECR8806F
(viz.
methacrylate
macroporous
resin
containing
octadecyl
groups,
designated
as
C18-TLL),
and
the
enzyme
performance
compared
to
that
of
octyl-agarose,
agarose
C8-TLL.
The
hydrolytic
activity
versus
p-nitrophenol
butyrate
decreased
significantly,
a
lower
extent
S-methyl
mandelate
(more
than
twofold),
while
triacetin
R-methyl
mandelate,
was
higher
for
biocatalyst
prepared
using
C18
(up
almost
five-fold).
Regarding
stability,
C18-TLL
significantly
more
stable
Next,
biocatalysts
were
mineralized
zinc,
copper
or
cobalt
phosphates.
Mineralization
increased
this
very
S-isomer,
effects
C8-TLL
diverse
(hydrolytic
increase
decrease
dependent
metal
substrate).
zinc
salt
treatment
stability
both
biocatalysts,
but
with
impact
agarose-C8-TLL.
On
contrary,
treatments
intensively
C18-TLL.
results
show
even
enzymes
following
same
strategy,
differences
in
conformation
cause
mineralization
have
activity,
specificity.
Language: Английский
Biocatalysts engineering by varying the binary CNTs-silica composition and the physicochemical characteristics of adsorbents for the immobilization of recombinant T. lanuginosus lipase
Journal of Biotechnology,
Journal Year:
2024,
Volume and Issue:
389, P. 13 - 21
Published: April 28, 2024
Language: Английский
Fabrication of β-glucosidase–Copper Phosphate Hybrid Nanoflowers for Bioconversion of Geniposide into Gardenia Blue
International Journal of Nanoscience,
Journal Year:
2023,
Volume and Issue:
22(05)
Published: May 17, 2023
Gardenia
blue
(GB)
is
a
natural
pigment
widely
used
in
textiles
and
food
industries
as
an
eco-friendly
alternative
to
synthetic
dyes
owing
its
safety,
biocompatibility
chemical
stability.
Herein
we
demonstrated
recyclable,
reusable
efficient
catalysis
system
for
the
biosynthesis
of
GB
from
geniposide
using
[Formula:
see
text]-glucosidase
embedded
copper
phosphate
hybrid
nanoflowers.
In
this
study,
promising
text]-glucosidase-secreting
actinomycete
was
isolated
identified
Streptomyces
variabilis
BGPA1.
The
secreted
enzyme
successfully
immobilized
nanoflowers
evidenced
by
scanning
electron
microscopy
(SEM)
Fourier-transform
infrared
spectroscopy
(FTIR)
analysis.
Results
revealed
functionality
prepared
bioconversion
into
genipin
which
interacts
with
glycine
yielding
pigment.
optimum
pH
temperature
were
found
be
6.0
50
∘
C,
respectively.
Interestingly,
text]-glucosidase–copper
retained
up
94%
their
initial
activity
after
15
cycles
repeated
usage,
indicating
remarkable
recyclability
reusability
biocatalytic
system.
This
study
suggests
that
could
potential
candidate
facile
production
GB.
Language: Английский
Investigation of Complexing Properties with Polyethyleneimine of Some Commercial Lipases
Yüzüncü Yıl Üniversitesi Fen Bilimleri Enstitüsü Dergisi,
Journal Year:
2024,
Volume and Issue:
29(1), P. 189 - 199
Published: March 5, 2024
Lipases
are
enzymes
used
in
various
industrial
process
and
immobilized
to
increase
their
applicability
as
biocatalysts.
Ionic
polymers
such
polyethyleneimine
(PEI)
make
possible
the
co-precipitation
of
enzymes.
In
this
study,
complexation
aggregation
with
PEI
were
investigated
commercial
from
Novozyme
51032
(Fusarium
solani
pisi),
Palatase
20000
L
(Rhizomucor
miehei),
Lipolase
100
(Thermomyces
lanuginosus),
Lipozyme
CAL
B
(Candida
antarctica
B)
Amano
(Pseudomonas
fluorescens)
using
a
linker
agent.
The
highest
percentage
PEI-enzyme
agregate
was
obtained
for
51032,
at
PEI/enzyme
ratio
1/20-1/80
range.
This
study
documented
that
(Amano)
P.
fluorescens
enzyme
preparations
failed
occur
precipitates
resulting
aggregates.
some
lipase
may
contain
impurity
components
prevent
or
PEI.
Complexing
lipases
is
based
on
basis
electrostatic
interaction
cationic
polymer
PEI-lipase
Language: Английский