Catalysts,
Год журнала:
2020,
Номер
10(11), С. 1277 - 1277
Опубликована: Ноя. 3, 2020
Lipases
are
biocatalysts
with
a
significant
potential
to
enable
shift
from
current
pollutant
manufacturing
processes
environmentally
sustainable
approaches.
The
main
reason
of
this
prospect
is
their
catalytic
versatility
as
they
carry
out
several
industrially
relevant
reactions
hydrolysis
fats
in
water/lipid
interface
and
synthesis
solvent-free
or
non-aqueous
media
such
transesterification,
interesterification
esterification.
Because
the
outstanding
traits
Rhizopus
oryzae
lipase
(ROL),
1,3-specificity,
high
enantioselectivity
stability
organic
media,
its
application
energy,
food
pharmaceutical
industrial
sector
has
been
widely
studied.
Significant
advances
have
made
biochemical
characterisation
ROL
particularly
how
activity
affected
by
presence
prosequence.
In
addition,
native
heterologous
production
ROL,
latter
cell
factories
like
Escherichia
coli,
Saccharomyces
cerevisiae
Komagataella
phaffii
(Pichia
pastoris),
thoroughly
described.
Therefore,
review,
we
summarise
knowledge
about
R.
(i)
characteristics,
(ii)
strategies
(iii)
applications.
International Journal of Biological Macromolecules,
Год журнала:
2022,
Номер
210, С. 682 - 702
Опубликована: Май 1, 2022
Pepsin
is
a
protease
used
in
many
different
applications,
and
instances,
it
utilized
an
immobilized
form
to
prevent
contamination
of
the
reaction
product.
This
enzyme
has
two
peculiarities
that
make
its
immobilization
complex.
The
first
one
related
poor
presence
primary
amino
groups
on
surface
(just
Lys
terminal
group).
second
stability
at
alkaline
pH
values.
Both
features
this
be
considered
complicated
goal,
as
most
protocols
utilize
for
immobilization.
review
presents
some
attempts
get
pepsin
biocatalyst
their
applications.
high
density
anionic
(Asp
Glu)
anion
exchange
simpler,
but
makes
strategies
immobilize
(e.g.,
amino-glutaraldehyde
supports)
more
mixed
ion
exchange/hydrophobic
adsorption
than
real
covalent
Finally,
we
propose
possibilities
can
permit
not
only
enzyme,
also
stabilization
via
multipoint
attachment.
International Journal of Biological Macromolecules,
Год журнала:
2023,
Номер
248, С. 125853 - 125853
Опубликована: Июль 17, 2023
Lipase
B
from
Candida
antarctica
(CALB)
and
lipase
Thermomyces
lanuginosus
(TLL)
have
been
immobilized
on
octyl
agarose
at
low
loading
a
exceeding
the
maximum
support
capacity.
Then,
enzymes
treated
with
glutaraldehyde
inactivated
pH
7
in
Tris-HCl,
sodium
phosphate
HEPES,
giving
different
stabilities.
Stabilization
(depending
buffer)
of
highly
loaded
biocatalysts
was
found,
very
likely
as
consequence
detected
intermolecular
crosslinkings.
This
did
not
occur
for
lowly
biocatalysts.
Next,
were
chemically
aminated
then
glutaraldehyde.
In
case
TLL,
intramolecular
crosslinkings
(visible
by
apparent
reduction
protein
size)
increased
enzyme
stability
biocatalysts,
an
effect
that
further
due
to
Using
CALB,
less
intense,
stabilization
lower,
even
though
quite
intense
biocatalyst.
The
depended
inactivation
buffer.
interactions
between
inactivating
buffer
effects
chemical
modifications
suggest
modification
studies
must
be
performed
under
target
conditions.
bioRxiv (Cold Spring Harbor Laboratory),
Год журнала:
2025,
Номер
unknown
Опубликована: Фев. 15, 2025
Accurate
prediction
of
kinetic
parameters
is
crucial
for
understanding
known
and
tailoring
novel
enzymes
biocatalysis.
Current
models
fail
to
capture
mutation
effects
on
catalytically
essential
residues,
limiting
their
utility
in
enzyme
design.
We
grid-searched
through
ten
model
architectures
(25,671
hyperparameter
combinations)
identify
a
gradient-based
additive
framework
called
RealKcat,
trained
27,176
experimental
entries
curated
manually
(KinHub-27k)
by
screening
2,158
articles.
Clustering
catalytic
turnover
(k
cat
)
substrate
affinity
(K
M
rational
orders
magnitude,
RealKcat
achieves
>85%
test
accuracy,
demonstrating
highest
sensitivity
mutation-induced
variability
thus
far,
the
first-of-its-kind-model
demonstrate
complete
loss
activity
upon
deletion
apparatus.
Finally,
state-of-the-art
k
validation
accuracy
(96%)
alkaline
phosphatase
(PafA)
mutant
industrial
dataset
confirms
RealKcat's
generalizability
learning
per-residue
relevance.
Catalysts,
Год журнала:
2020,
Номер
10(6), С. 605 - 605
Опубликована: Май 29, 2020
Lipases
are
among
the
most
utilized
enzymes
in
biocatalysis.
In
many
instances,
main
reason
for
their
use
is
high
specificity
or
selectivity.
However,
when
full
modification
of
a
multifunctional
and
heterogeneous
substrate
pursued,
enzyme
selectivity
become
problem.
This
case
hydrolysis
oils
fats
to
produce
free
fatty
acids
alcoholysis
biodiesel,
which
can
be
considered
cascade
reactions.
these
cases,
original
heterogeneity
substrate,
presence
intermediate
products,
such
as
diglycerides
monoglycerides,
an
additional
drawback.
Using
substrates,
promote
that
some
substrates
(initial
products)
may
not
recognized
(in
worst
scenario
they
acting
inhibitors)
by
enzyme,
causing
yields
reaction
rates
drop.
To
solve
this
situation,
mixture
lipases
with
different
specificity,
differently
affected
conditions
offer
much
better
results
than
single
lipase
exhibiting
very
initial
activity
even
best
global
course.
from
sources
has
been
called
“combilipases”
becoming
increasingly
popular.
They
include
liquid
formulations
immobilized
lipases.
have
coimmobilized.
Some
discussion
offered
regarding
problems
coimmobilization
give
rise
to,
strategies
proposed.
The
combilipases
future
extended
other
processes
enzymes.
Catalysts,
Год журнала:
2020,
Номер
10(11), С. 1277 - 1277
Опубликована: Ноя. 3, 2020
Lipases
are
biocatalysts
with
a
significant
potential
to
enable
shift
from
current
pollutant
manufacturing
processes
environmentally
sustainable
approaches.
The
main
reason
of
this
prospect
is
their
catalytic
versatility
as
they
carry
out
several
industrially
relevant
reactions
hydrolysis
fats
in
water/lipid
interface
and
synthesis
solvent-free
or
non-aqueous
media
such
transesterification,
interesterification
esterification.
Because
the
outstanding
traits
Rhizopus
oryzae
lipase
(ROL),
1,3-specificity,
high
enantioselectivity
stability
organic
media,
its
application
energy,
food
pharmaceutical
industrial
sector
has
been
widely
studied.
Significant
advances
have
made
biochemical
characterisation
ROL
particularly
how
activity
affected
by
presence
prosequence.
In
addition,
native
heterologous
production
ROL,
latter
cell
factories
like
Escherichia
coli,
Saccharomyces
cerevisiae
Komagataella
phaffii
(Pichia
pastoris),
thoroughly
described.
Therefore,
review,
we
summarise
knowledge
about
R.
(i)
characteristics,
(ii)
strategies
(iii)
applications.