Environmental Science & Technology Letters,
Journal Year:
2022,
Volume and Issue:
9(7), P. 650 - 657
Published: June 17, 2022
The
extensive
production
and
use
of
polyethylene
terephthalate
(PET)
have
generated
an
enormous
amount
plastic
waste,
which
potentially
threatens
the
environment
humans.
Enzyme
biocatalysis
is
a
promising
green
chemistry
alternative,
relative
to
conventional
fossil-derived
process,
achieve
waste
treatment
recycling.
In
this
work,
we
created
biocatalyst,
BIND-PETase,
by
genetically
engineering
curli
Escherichia
coli
cell
with
functional
PETase
enzyme
for
biocatalytic
degradation
PET
plastics.
BIND-PETase
could
degrade
generate
products
at
concentration
level
greater
than
3000
μM
under
various
reaction
conditions.
effects
key
parameters,
including
pH,
temperature,
substrate
mass
load,
surfactant
addition
were
characterized.
was
reusable
remained
stable
no
significant
activity
loss
when
stored
both
4
°C
room
temperature
30
days
(Student's
t
test,
p
>
0.05).
Notably,
enable
microplastics
in
wastewater
effluent
matrix.
Moreover,
depolymerize
highly
crystalline
postconsumer
materials
ambient
conditions
efficiency
9.1%
7
days.
This
study
provides
new
horizon
developing
environmentally
friendly
approaches
solve
recycling
challenge.
Fullerenes Nanotubes and Carbon Nanostructures,
Journal Year:
2020,
Volume and Issue:
28(12), P. 1048 - 1058
Published: July 21, 2020
The
surface
properties
of
carbon
materials
are
very
important
since
many
complex
physical
and
chemical
reactions
take
place
on
their
surfaces.
X-ray
photoelectron
spectroscopy
(XPS)
test
is
one
the
most
significant
characterization
methods
to
analyze
species
banding
energies
for
several
typical
kinds
(graphite,
black,
graphene,
nanotubes,
carbides,
polymers)
were
summarized
with
XPS
spectra.
It
can
be
found
that
different
preparation
methods,
analytical
or
storage
times
possess
quite
energies.
Meanwhile,
classical
figures
analysis
results
every
material
illustrated,
which
provides
researchers
an
intuitive
understanding
related
method.
Therefore,
much
more
accurate
spectra
obtained.
ACS Sustainable Chemistry & Engineering,
Journal Year:
2020,
Volume and Issue:
8(24), P. 8894 - 8908
Published: May 22, 2020
Polyethylene
terephthalate
(PET)
hydrolase
is
a
challenging
target
as
PET
commonly
used
plastic
that
extremely
resistant
to
enzymatic
attack.
Since
the
discovery
of
from
Thermobifida
fusca
in
2005,
novel
hydrolases
and
their
availability
toward
waste
have
been
investigated.
At
present,
at
least
four
thermophilic
cutinases
are
known
could
be
for
management
amorphous
waste,
such
packaging
materials.
Heat-labile
PETase
Ideonella
sakaiensis
its
homologues
mesophilic
bacteria
exist
environment.
However,
can
efficiently
hydrolyzed
with
hydrolases.
This
Review
focuses
on
current
state
potential
application.
Contrary
an
PET,
hydrolysis
crystalline
(particularly
bottles)
remains
fully
elucidated.
It
cannot
assured
whether
biorecycling
general
would
put
into
practice
near
future,
but
plan
getting
closer
goal.
versatile
polyesterases
they
hydrolyze
not
only
also
other
polyesters.
Additionally,
thermostability
advantageous
application
terms
reaction
speed
durability.
Microbial Cell Factories,
Journal Year:
2020,
Volume and Issue:
19(1)
Published: April 28, 2020
For
decades,
plastic
has
been
a
valuable
global
product
due
to
its
convenience
and
low
price.
example,
polyethylene
terephthalate
(PET)
was
one
of
the
most
popular
materials
for
disposable
bottles
beneficial
properties,
namely
impact
resistance,
high
clarity,
light
weight.
Increasing
demand
resulted
in
indiscriminate
disposal
by
consumers,
causing
severe
accumulation
wastes.
Because
this,
scientists
have
made
great
efforts
find
way
biologically
treat
As
result,
novel
degradation
enzyme,
PETase,
which
can
hydrolyze
PET,
discovered
Ideonella
sakaiensis
201-F6
2016.
A
green
algae,
Chlamydomonas
reinhardtii,
produces
developed
this
study.
Two
representative
strains
(C.
reinhardtii
CC-124
CC-503)
were
examined,
we
found
that
could
express
PETase
well.
To
verify
catalytic
activity
produced
C.
cell
lysate
transformant
PET
samples
co-incubated
at
30
°C
up
4
weeks.
After
incubation,
terephthalic
acid
(TPA),
i.e.
fully-degraded
form
detected
performance
liquid
chromatography
analysis.
Additionally,
morphological
changes,
such
as
holes
dents
on
surface
film,
observed
using
scanning
electron
microscopy.
hydrolyzing
successfully
expressed
demonstrated.
best
our
knowledge,
is
first
case
expression
algae.
Frontiers in Microbiology,
Journal Year:
2020,
Volume and Issue:
11
Published: Nov. 11, 2020
Since
gaining
popularity
over
50
years
ago,
plastic
has
transformed
our
world,
with
many
aspects
of
modern
life
relying
on
materials.
However,
the
qualities
which
have
made
an
attractive
resource,
such
as
ease
mass
production
and
advantageous
strength-to-weight
ratio,
are
equally
responsible
for
damage
that
is
typically
caused
once
it
becomes
waste.
In
recent
years,
biological
degradation
emerged
one
way
to
address
these
unforeseen
consequences.
This
strategy
involves
using
microorganisms,
primarily
bacteria
fungi,
enzymes
capable
catalyzing
degradative
reactions,
break
apart
into
its
original
components.
The
focus
this
review
will
be
microbial
hydrolase
found
act
polyethylene
terephthalate
or
PET
plastic,
widely
packaging
synthetic
fibers
among
other
forms.
best
characterized
examples
discussed
along
use
metagenomic
protein
engineering
technologies
in
obtaining
application.
addition,
obstacles
currently
limiting
development
efficient
bioprocesses
presented.
By
continuing
study
possible
mechanisms
key
enzyme
structural
elements
behind
hydrolysis
assessing
ability
under
practical
conditions,
research
can
progress
towards
large-scale
waste
management
operations.
Finally,
contribution
hydrolases
creating
a
circular
economy
explored
Angewandte Chemie International Edition,
Journal Year:
2023,
Volume and Issue:
62(14)
Published: Feb. 8, 2023
PETase
displays
great
potential
in
PET
depolymerization.
Directed
evolution
has
been
limited
to
engineer
due
the
lack
of
high-throughput
screening
assay.
In
this
study,
a
novel
fluorescence-based
assay
employing
newly
designed
substrate,
bis
(2-hydroxyethyl)
2-hydroxyterephthalate
(termed
BHET-OH),
was
developed
for
hydrolases.
The
best
variant
DepoPETase
produced
1407-fold
more
products
towards
amorphous
film
at
50
°C
and
showed
23.3
higher
Tm
value
than
WT.
enabled
complete
depolymerization
seven
untreated
wastes
19.1
g
waste
(0.4
%
Wenzyme
/WPET
)
liter-scale
reactor,
suggesting
that
it
is
candidate
industrial
processes.
molecular
dynamic
simulations
revealed
distal
substitutions
stabilized
loops
around
active
sites
transmitted
stabilization
effect
through
enhancing
inter-loop
interactions
network.