Dual Valorization of Lignin as a Versatile and Renewable Matrix for Enzyme Immobilization and (Flow) Bioprocess Engineering
ChemSusChem,
Journal Year:
2021,
Volume and Issue:
14(15), P. 3198 - 3207
Published: June 10, 2021
Lignin
has
emerged
as
an
attractive
alternative
in
the
search
for
more
eco-friendly
and
less
costly
materials
enzyme
immobilization.
In
this
work,
terephthalic
aldehyde-stabilization
of
lignin
is
carried
out
during
its
extraction
to
develop
a
series
functionalized
lignins
with
range
reactive
groups
(epoxy,
amine,
aldehyde,
metal
chelates).
This
expands
immobilization
pool
enzymes
(carboxylase,
dehydrogenase,
transaminase)
by
different
binding
chemistries,
affording
yields
64-100
%.
As
proof
concept,
ω-transaminase
reversibly
immobilized
on
polyethyleneimine-lignin
integrated
packed-bed
reactor.
The
stability
biocatalyst
tested
continuous-flow
deamination
reactions
maintains
same
conversion
100
cycles.
These
results
outperform
previous
tests
covalently
methacrylic
resins,
advantage
that
reversibility
allows
recycling
reuse
beyond
inactivation.
Additionally,
in-line
system
also
based
added
into
downstream
process
separate
reaction
products
catch-and-release.
demonstrate
fully
closed-loop
sustainable
flow-biocatalytic
exclusively
lignin.
Language: Английский
Microtiter Plate Immobilization Screening for Prototyping Heterogeneous Enzyme Cascades
Angewandte Chemie International Edition,
Journal Year:
2024,
Volume and Issue:
63(35)
Published: July 22, 2024
Abstract
Immobilization
is
a
key
enabling
technology
in
applied
biocatalysis
that
facilitates
the
separation,
recovery,
and
reuse
of
heterogeneous
biocatalysts.
However,
finding
consensus
immobilization
protocol
for
several
enzymes
forming
multi‐enzyme
system
extremely
difficult
relies
on
combinatorial
trial‐and‐error
approach.
Herein,
we
describe
which
17
different
carriers
functionalized
with
reactive
groups
are
tested
96‐well
microtiter
plate
to
screen
up
21
protocols
18
enzymes.
This
screening
includes
an
activity
stability
assay
select
optimal
chemistry
achieve
most
active
stable
The
information
retrieved
from
can
be
rationalized
using
Python‐based
application
CapiPy.
Finally,
through
scoring
results,
find
assemble
immobilized
four‐enzyme
transform
vinyl
acetate
into
(
S
)‐3‐hydroxybutyric
acid.
methodology
opens
path
speed
prototyping
pathways
chemical
manufacturing.
Language: Английский
Closing the loop: technological innovations in food waste valorisation for global sustainability
Discover Sustainability,
Journal Year:
2025,
Volume and Issue:
6(1)
Published: April 8, 2025
Language: Английский
Microtiter Plate Immobilization Screening for Prototyping Heterogeneous Enzyme Cascades
Angewandte Chemie,
Journal Year:
2024,
Volume and Issue:
136(35)
Published: July 22, 2024
Abstract
Immobilization
is
a
key
enabling
technology
in
applied
biocatalysis
that
facilitates
the
separation,
recovery,
and
reuse
of
heterogeneous
biocatalysts.
However,
finding
consensus
immobilization
protocol
for
several
enzymes
forming
multi‐enzyme
system
extremely
difficult
relies
on
combinatorial
trial‐and‐error
approach.
Herein,
we
describe
which
17
different
carriers
functionalized
with
reactive
groups
are
tested
96‐well
microtiter
plate
to
screen
up
21
protocols
18
enzymes.
This
screening
includes
an
activity
stability
assay
select
optimal
chemistry
achieve
most
active
stable
The
information
retrieved
from
can
be
rationalized
using
Python‐based
application
CapiPy.
Finally,
through
scoring
results,
find
assemble
immobilized
four‐enzyme
transform
vinyl
acetate
into
(
S
)‐3‐hydroxybutyric
acid.
methodology
opens
path
speed
prototyping
pathways
chemical
manufacturing.
Language: Английский
Unveiling the spatial rearrangements of exhausted immobilised multi-enzyme systems through cryo-X-ray fluorescence nanoprobe imaging
Chemical Science,
Journal Year:
2024,
Volume and Issue:
unknown
Published: Jan. 1, 2024
Enzyme
immobilisation
is
of
great
importance
for
the
fabrication
heterogeneous
biocatalysts,
as
it
allows
stabilisation
proteins
using
a
solid
support.
Moreover,
permits
their
reuse
in
continuous
and
discontinuous
reactors.
The
behaviour
enzymes
at
interface
with
materials
where
they
are
supported
not
well
understood
during
operational
conditions.
Here,
we
use
X-ray
fluorescence
(XRF)
imaging
to
study
changes
overall
structure
biocatalyst
formed
by
two
unmodified
metalloenzymes
(a
copper-dependent
laccase
zinc-dependent
dehydrogenase)
upon
incubation,
either
under
drastic
(high
temperature)
or
Those
were
co-immobilised
reversibly
(by
electrostatic
interactions
His-tag
metal
coordination)
form
cascade
reaction
that
catalyses
NAD
Language: Английский