Assembly of Cellulases from Separate Catalytic Domains and a Cellulose-Binding Module for Understanding Cooperative Crystalline Cellulose Degradation
Applied Sciences,
Journal Year:
2025,
Volume and Issue:
15(4), P. 2214 - 2214
Published: Feb. 19, 2025
The
biochemical
degradation
of
abundant
cellulosic
biomass
for
industrial
use
and
energy
production
has
been
extensively
researched
in
recent
years.
Some
elaborate
cellulose
digestion
approaches
have
developed
based
on
specialized
bacteria,
which
possess
sophisticated
mechanisms
to
efficiently
degrade
recalcitrant
natural
carbohydrates.
In
this
study,
we
assembled
catalytic
domains
from
multiple
cellulolytic
enzymes
onto
a
scaffold
along
with
cellulose-binding
module
(CBM),
specifically
targeting
crystalline
cellulose.
endoglucanase
cellobiohydrolase
Acetivibrio
thermocellus
were
linked
heterotrimeric
protein
that
assembles
specific
order.
bicatalytic
complex
failed
show
the
anticipated
synergistic
effect
cooperative
cellulolysis,
presumably
because
only
serve
as
weak
anchors
each
other
binding
substrate.
On
hand,
was
remarkably
promoted
by
incorporating
CBM
into
stable
domain.
Interestingly,
reversible
association
excess
proved
more
advantageous
than
fixed
association.
This
suggests
dynamic
incorporation
units
enhances
accessibility
cellulose-degrading
modules
polysaccharide
strand
preventing
overly
strong
binding.
finding
could
interdisciplinary
applications
converting
polymeric
substrates
Language: Английский
Lignocellulose degradation in bacteria and fungi: cellulosomes and industrial relevance
Frontiers in Microbiology,
Journal Year:
2025,
Volume and Issue:
16
Published: April 25, 2025
Lignocellulose
biomass
is
one
of
the
most
abundant
resources
for
sustainable
biofuels.
However,
scaling
up
biomass-to-biofuels
conversion
process
widespread
usage
still
pending.
One
main
bottlenecks
high
cost
enzymes
used
in
key
degradation.
Current
research
efforts
are
therefore
targeted
at
creative
solutions
to
improve
feasibility
lignocellulosic-degrading
enzymes.
way
engineer
multi-enzyme
complexes
that
mimic
bacterial
cellulosomal
system,
known
increase
degradation
efficiency
50-fold
when
compared
freely-secreted
these
designer
cellulosomes
instable
and
less
efficient
than
wild
type
cellulosomes.
In
this
review,
we
aim
extensively
analyze
current
knowledge
on
through
three
aspects.
We
start
by
reviewing
comparing
sets
fungal
lignocellulose
Next,
focus
characteristics
both
systems
their
be
engineered.
Finally,
highlight
strategies
enhance
enzymatic
efficiency:
discovering
novel
lignocellulolytic
species
enzymes,
bioengineering
improved
thermostability,
structurally
optimizing
anticipate
insights
act
as
community
looking
elevate
biofuel.
Language: Английский