Journal of Agricultural and Food Chemistry,
Journal Year:
2024,
Volume and Issue:
72(34), P. 19071 - 19080
Published: Aug. 14, 2024
Zealexin
A1
is
a
nonvolatile
sesquiterpene
phytoalexin,
which
not
only
exhibits
extensive
antifungal
and
insecticidal
activities
but
also
has
the
ability
to
enhance
drought
resistance
of
plants,
thus
potential
applications
in
agricultural
food
fields.
In
this
study,
biosynthetic
pathway
zealexin
was
constructed
Green Chemistry,
Journal Year:
2023,
Volume and Issue:
25(5), P. 1704 - 1728
Published: Jan. 1, 2023
Publication
of
the
E
Factor
drew
attention
to
problem
waste
in
chemicals
manufacture.
Thirty
yeas
later
it
is
abundantly
clear
that
underlying
cause
global
environmental
problems,
from
climate
change
plastic
pollution.
Reviews in Environmental Science and Bio/Technology,
Journal Year:
2024,
Volume and Issue:
23(2), P. 351 - 383
Published: May 14, 2024
Abstract
Polyethylene
terephthalate
(PET)
is
one
of
the
most
marketed
aromatic
polyesters
in
world
with
an
annual
demand
2022
approximately
29
million
metric
tons,
expected
to
increase
by
40%
2030.
The
escalating
volume
PET
waste
and
current
inadequacy
recycling
methods
have
led
accumulation
terrestrial
ecosystem,
thereby
posing
significant
global
health
risks.
pressing
energy
environmental
issues
associated
underscore
urgent
need
for
“upcycling”
technologies.
These
technologies
aim
transform
reclaimed
into
higher-value
products,
addressing
both
concerns
sustainability.
Enzyme-mediated
biocatalytic
depolymerization
has
emerged
as
a
potentially
bio-sustainable
method
treating
plastics.
Numerous
plastic-degrading
enzymes
been
identified
from
microbial
origins,
advancements
protein
engineering
employed
modify
enhance
these
enzymes.
Microbial
metabolic
allows
development
modified
chassis
capable
degrading
substrates
converting
their
derived
monomers
industrial
relevant
products.
In
this
review,
we
describe
several
approaches
aiming
at
enhancing
performances
PET-degrading
present
strategies
adopted
bio-upcycle
high-value
molecules.
ACS Catalysis,
Journal Year:
2024,
Volume and Issue:
14(7), P. 5469 - 5480
Published: March 28, 2024
Enzymes
have
selectivity,
require
mild
catalytic
conditions,
and
are
important
cornerstones
in
many
industrial
processes.
Protein
self-cyclization
has
opened
up
the
possibility
of
preserving
fragile
enzymes
during
long-term
high-temperature
catalysis.
However,
mechanism
for
improvement
thermal
tolerance
not
been
elucidated,
severely
limiting
their
applications.
Herein,
we
provide
a
strategy
rational
design
fusion
proteins
based
on
structural
analysis
to
obtain
cyclized
with
improved
properties.
First,
constructed
that
preferentially
translated
SpyCatcher
(CBT)
or
SpyTag
(TBC),
both
which
could
form
stable
single
significantly
tolerance.
Especially,
half-life
TBC
obtained
by
modifying
N-terminal
at
40
°C
was
10.83
times
wild
enzymes.
Structural
revealed
terminus
protein,
SpyCatcher,
folded
into
conformation
adversely
affected
stability.
In
addition,
structure
pocket
orientation
residues
CBT
were
different
from
those
wild-type
enzymes,
led
decrease
activity.
These
conclusions
confirmed
when
another
enzyme,
sucrose
phosphorylase,
cyclized.
Finally,
glucosidase
also
superior
strain
preparation
ginsenoside
F1
high
titers
as
whole-cell
catalyst
extended
use.
conclusion,
demonstrated
first
time
conjugated
long
oligopeptide
activity
stability
It
necessary
translate
units
less
steric
hindrance
reduce
impact
protein
structure.
The
provides
simple
effective
modification
poor
tolerance,
providing
considerable
prospects
biosynthesis
vivo
vitro.
ChemBioEng Reviews,
Journal Year:
2024,
Volume and Issue:
11(3), P. 613 - 635
Published: April 29, 2024
Abstract
Lignocellulosic
biomass,
such
as
plant
residues
and
agricultural
waste,
holds
immense
potential
a
renewable
resource
for
the
production
of
biofuels,
chemicals,
animal
feed.
However,
efficient
degradation
lignocellulose
into
fermentable
sugars
remains
significant
challenge.
Recent
research
has
highlighted
critical
role
microbial
diversity
in
lignocellulosic
biomass
degradation,
offering
new
insights
from
biotechnological
perspective.
The
comprehension
utilization
are
crucial
developing
strategies
degradation.
By
uncovering
intricate
relationships
between
communities
their
enzymatic
machinery,
researchers
can
optimize
processes,
enhance
biofuel
production,
contribute
to
more
sustainable
bio‐based
economy.
Microorganisms,
including
bacteria,
fungi,
archaea,
possess
diverse
capabilities,
allowing
them
secrete
plethora
lignocellulolytic
enzymes.
Microbial
organisms
inhabiting
extreme
environments,
rumen,
hot
cold
springs,
deep
sea
trenches,
acidic
alkaline
pH
exhibit
generating
enzymes,
hemicellulolytic
which
superior
biochemical
properties
essential
industrial
bioconversion
applications.
This
review
explores
ability
enzymes
sources
efficiently
break
down
applications
biotechnology.
Critical Reviews in Biotechnology,
Journal Year:
2024,
Volume and Issue:
unknown, P. 1 - 16
Published: Sept. 12, 2024
Geraniol,
an
acyclic
monoterpene
alcohol,
has
significant
potential
applications
in
various
fields,
including:
food,
cosmetics,
biofuels,
and
pharmaceuticals.
However,
the
current
sources
of
geraniol
mainly
include
plant
tissue
extraction
or
chemical
synthesis,
which
are
unsustainable
suffer
severely
from
high
energy
consumption
severe
environmental
problems.
The
process
microbial
production
recently
undergone
vigorous
development.
Particularly,
sustainable
construction
recombinant
Biochimie,
Journal Year:
2024,
Volume and Issue:
225, P. 49 - 67
Published: May 9, 2024
The
global
β-glucosidase
market
is
currently
estimated
at
∼400
million
USD,
and
it
expected
to
double
in
the
next
six
years;
a
trend
that
mainly
ascribed
demand
for
enzyme
biofuel
processing.
Microbial
β-glucosidase,
particularly,
has
thus
garnered
significant
attention
due
its
ease
of
production,
catalytic
efficiency,
versatility,
which
have
all
facilitated
biotechnological
potential
across
different
industries.
Hence,
there
are
continued
efforts
screen,
produce,
purify,
characterize
evaluate
industrial
applicability
from
actinomycetes,
bacteria,
fungi,
yeasts.
With
this
rising
various
cost-effective
efficient
approaches
being
explored
discover,
redesign,
enhance
their
production
functional
properties.
Thus,
present
review
provides
an
up-to-date
overview
advancements
utilization
microbial
β-glucosidases
as
"Emerging
Green
Tools"
21st-century
In
regard,
focus
was
placed
on
use
recombinant
technology,
protein
engineering,
immobilization
techniques
targeted
improving
enzyme.
Furthermore,
insights
were
given
into
recent
progress
made
conventional
applications,
well
current
commercial
status-with
patents.
Bioengineering,
Journal Year:
2025,
Volume and Issue:
12(1), P. 68 - 68
Published: Jan. 14, 2025
Enzymatic
depolymerisation
is
increasingly
recognised
as
a
reliable
and
environmentally
friendly
method.
The
development
of
this
technology
hinges
on
the
availability
high-quality
enzymes
associated
bioreaction
systems
for
upscaling
biodegradation.
Microbial
heterologous
expression
have
been
studied
meeting
demand.
Among
these
systems,
Pichia
pastoris
system
has
emerged
widely
used
platform
producing
secreted
proteins.
This
article
provides
an
overview
studies
involving
recombinant
polymer-degrading
using
P.
system.
Research
interested
with
depolymerising
ability,
including
cutinase,
lipase,
laccase,
are
highlighted
in
review.
key
factors
influencing
discussed,
shedding
light
challenges
opportunities
biocatalysts
through