Lipases
have
been
immobilized
in
various
supports
to
catalyze
hydrolysis,
esterification,
and
transesterification
reactions
efficiently.
Among
a
broad
range
of
materials,
mesoporous
silica
has
attracted
attention
thanks
its
distinct
characteristics
advantages,
being
widely
used
for
biocatalysis
applications.
In
this
work,
the
lipase
from
Thermomyces
lanuginosus
(TLL)
was
six
different
carriers:
two
zeolites
HZSM-5
(SAR
25
280),
Si-MCM-41,
silica-aluminas
Siral
10,
20,
40.
TLL
efficiently
20
(99.9%)
40
using
26
mg
g-1
enzyme
loading.
Due
more
hydrophobic
nature,
selected
as
most
suitable
support
immobilization
5
mmol
L-1
sodium
phosphate
buffer
solution,
pH
7,
rotational
stirring
optimum
condition.
The
effect
protein
concentration
on
investigated,
results
adjusted
well
(R2
>
0.99)
Langmuir
isotherm
model.
presented
maximum
adsorption
capacity
equal
169
mgprotein
gsupport-1.
heterogeneous
biocatalyst
(TLL-S40)
applied
biodiesel
synthesis,
olive
oil
p-nitrophenyl-laurate
ethyl
oleate
synthesis.
esterification
reaction
successfully
catalyzed
by
TLL-S40,
leading
conversion
2.6-fold
higher
than
free
at
30°C.
reused
three
operational
cycles
with
retention
34%
initial
conversion.
show
that
40,
silica-alumina
material,
can
potentially
be
employed
reactions.
Biotechnology for Biofuels and Bioproducts,
Journal Year:
2024,
Volume and Issue:
17(1)
Published: Feb. 24, 2024
Abstract
Background
Biodiesel,
an
emerging
sustainable
and
renewable
clean
energy,
has
garnered
considerable
attention
as
alternative
to
fossil
fuels.
Although
lipases
are
promising
catalysts
for
biodiesel
production,
their
efficiency
in
industrial-scale
application
still
requires
improvement.
Results
In
this
study,
a
novel
strategy
multi-site
mutagenesis
the
binding
pocket
was
developed
via
FuncLib
(for
mutant
enzyme
design)
Rosetta
Cartesian_ddg
free
energy
calculation)
improve
reaction
rate
yield
of
lipase-catalyzed
production.
Thermomyces
lanuginosus
lipase
(TLL)
with
high
activity
thermostability
obtained
using
Pichia
pastoris
expression
system.
The
specific
activities
mutants
M11
M21
(each
5
4
mutations)
were
1.50-
3.10-fold
higher,
respectively,
than
those
wild-type
(wt–TLL).
Their
corresponding
melting
temperature
profiles
increased
by
10.53
6.01
°C,
$$T_{50}^{15}$$
T5015
(the
at
which
is
reduced
50%
after
15
min
incubation)
from
60.88
68.46
°C
66.30
optimum
temperatures
shifted
45
50
°C.
After
incubation
60%
methanol
1
h,
retained
more
activity,
45%
higher
that
wt–TLL.
Molecular
dynamics
simulations
indicated
increase
could
be
explained
atomic
fluctuation,
improved
catalytic
properties
attributed
newly
formed
hydrophobic
interaction.
Yields
production
catalyzed
48
h
elevated
(50
°C)
94.03%
98.56%,
markedly
wt–TLL
(88.56%)
its
optimal
(45
transesterification
soybean
oil.
Conclusions
An
integrating
first
adopted
realize
co-evolution
lipase.
Two
excellent
exhibited
great
potential
practical
applications
Catalysts,
Journal Year:
2024,
Volume and Issue:
14(6), P. 336 - 336
Published: May 22, 2024
Biodiesel
is
a
mixture
of
fatty
acid
alkyl
esters
(FAAEs)
mainly
produced
via
transesterification
reactions
among
triglycerides
and
short-chain
alcohols
catalyzed
by
chemical
catalysts
(e.g.,
KOH,
NaOH).
Lipase-assisted
enzymatic
has
been
proposed
to
overcome
the
drawbacks
synthesis,
such
as
high
energy
consumption,
expensive
separation
catalyst
from
reaction
production
large
amounts
wastewater
during
product
purification.
However,
one
main
this
process
enzyme
cost.
In
recent
years,
nano-immobilized
lipases
have
received
extensive
attention
in
design
robust
industrial
biocatalysts
for
biodiesel
production.
To
improve
lipase
catalytic
efficiency,
magnetic
nanoparticles
(MNPs)
attracted
growing
interest
versatile
carriers,
owing
their
unique
properties,
surface-to-volume
ratio
loading
capacity,
low
cost
inertness
against
microbial
degradation,
biocompatibility
eco-friendliness,
standard
synthetic
methods
large-scale
and,
most
importantly,
which
provide
possibility
immobilized
be
easily
separated
at
end
applying
an
external
field.
For
preparation
effective
nano-supports,
various
surface
functionalization
approaches
developed
immobilize
broad
range
industrially
important
lipases.
Immobilization
generally
improves
chemical-thermal
stability
wide
pH
temperature
may
also
modify
its
performance.
Additionally,
different
can
co-immobilized
onto
same
nano-carrier,
highly
strategy
enhance
yield,
specifically
those
feedstocks
containing
heterogeneous
free
acids
(FFAs).
This
review
will
present
update
on
use
iron
oxide
nanostructures
immobilization
catalyze
The
following
aspects
covered:
(1)
common
organic
modifiers
nanoparticle
support
(2)
studies
modified
MNPs-lipase
Aspects
concerning
procedures
nano-supports
highlighted.
features
that
characterize
these
nano-biocatalysts,
activity,
reusability,
resistance
heat
pH,
discussed.
Perspectives
key
considerations
optimizing
terms
sustainability
are
provided
future
studies.
Frontiers in Catalysis,
Journal Year:
2024,
Volume and Issue:
4
Published: Feb. 16, 2024
Biodiesel
is
synthesized
by
the
transesterification
of
triglycerides
oils
with
short-chain
alcohols,
such
as
methanol
and
ethanol.
According
to
Renewable
Energy
Directive
guidelines
(RED
II
2018/2001/EU)
contribution
advanced
biofuels,
which
do
not
include
edible
oils,
towards
overall
EU
target,
at
1%
in
2025
least
3.5%
2030.
Bioprocesses
that
valorize
non-edible
for
production
second-generation
biodiesel
could
play
a
critical
role
achieving
this
goal.
Immobilized
lipases,
well
other
enzyme
classes,
cutinases
acyltransferases,
are
utilized
biocatalysts
process.
For
sustainability
process,
renewable
materials
can
be
used
immobilization
matrices,
or
even
enzymes
anchored
on
cells
whole-cell
biocatalysts.
Membrane
reactors
also
employed
facilitate
enzymatic
conducting
continuous
reaction
simultaneously
separate
products
single
operation.
The
advances
aforementioned
fast-pacing
fields
presented
work.
International Journal of Molecular Sciences,
Journal Year:
2024,
Volume and Issue:
25(5), P. 2746 - 2746
Published: Feb. 27, 2024
Multi-enzymatic
strategies
have
shown
improvement
in
bioconversion
during
cofactor
regeneration.
In
this
study,
purified
l-arabinitol
4-dehydrogenase
(LAD)
and
nicotinamide
adenine
dinucleotide
oxidase
(Nox)
were
immobilized
via
individual,
mixed,
sequential
co-immobilization
approaches
on
magnetic
nanoparticles,
evaluated
to
enhance
the
conversion
of
l-xylulose.
Initially,
immobilization
LAD
or
Nox
nanoparticles
resulted
a
maximum
yield
relative
activity
91.4%
98.8%,
respectively.
The
enzymes
showed
better
pH
temperature
profiles
than
corresponding
free
enzymes.
Furthermore,
these
mixed
methods
high
loadings
114
122
mg/g
support,
Sequential
proved
more
beneficial
for
higher
because
retaining
residual
activity.
Sequentially
co-immobilized
with
broader
pH,
temperature,
storage
stability
controls,
along
reusability.
To
best
our
knowledge,
is
first
report
l-xylulose
production.
This
finding
suggests
that
selecting
strategy
using
individual
enhancing
applications.
