Catalysts,
Journal Year:
2024,
Volume and Issue:
14(9), P. 649 - 649
Published: Sept. 23, 2024
Taste
and
odor
(T&O)
compounds
have
emerged
as
crucial
parameters
for
assessing
water
quality.
Therefore,
identifying
effective
methodologies
the
removal
of
these
is
imperative.
In
this
study,
an
approach
utilizing
laccase
assisted
by
a
micro-electric
field
was
developed
degradation
2-methylisoborneol
(2-MIB).
For
purpose,
optimal
conditions
laccase-catalyzed
2-MIB
were
determined,
they
pH
4.0,
25
°C,
150
rpm,
0.1
U/mL
laccase,
200
ng/L
2-MIB.
Under
specified
conditions,
efficiency
approximately
78%
after
4
h
reaction
period.
Subsequently,
introduction
electric
yielded
synergistic
effect
with
enzyme
degradation.
At
current
intensity
0.04
A
over
duration,
increased
to
90.78%.
An
analysis
using
SPME-GC/MS
provided
information
on
intermediates
resulting
from
degradation,
electrocatalytic
micro-electric-assisted
The
potential
pathways
illustrated
that
three
methods
result
in
common
products,
such
capric
aldehyde,
nonylaldehyde,
2-ethylhexanol,
their
final
products
include
3-pentanone,
acetone,
2-butanone.
This
study
provides
enzyme–electrochemical
method
efficient
rapid
strategy
catalysis
has
good
pollutants
natural
environment.
Journal of Agricultural and Food Chemistry,
Journal Year:
2024,
Volume and Issue:
72(44), P. 24158 - 24169
Published: Oct. 22, 2024
Laccase,
a
multipurpose
biocatalyst,
is
widely
distributed
across
all
kingdoms
of
life
and
plays
key
role
in
essential
biological
processes
such
as
lignin
synthesis,
degradation,
pigment
formation.
These
functions
are
critical
for
fungal
growth,
plant-pathogen
interactions,
maintenance
soil
health.
Due
to
its
broad
substrate
specificity,
multifunctional
nature,
environmentally
friendly
characteristics,
laccase
employed
catalyst
various
green
chemistry
initiatives.
With
ability
oxidize
diverse
range
phenolic
nonphenolic
compounds,
has
also
been
found
be
useful
food
additive
assessing
quality
parameters.
Ongoing
advancements
research
technology
continually
expanding
the
recognition
laccase's
potential
address
global
environmental,
health,
energy
challenges.
This
review
aims
provide
insights
into
applications
laccases
biotechnology
industry.
International Journal of Molecular Sciences,
Journal Year:
2025,
Volume and Issue:
26(2), P. 735 - 735
Published: Jan. 16, 2025
Thermus
thermophilus
HB27
laccase
(Tth-Lac)
is
a
thermostable
enzyme
that
contains
β-hairpin
(Ala292-Gln307)
covering
the
substrate
entrance.
We
analyzed
role
of
this
in
enzymatic
activity
Tth-Lac
through
three
mutants:
two
variants
without
(C1Tth-Lac
and
C2Tth-Lac)
one
with
partially
modified
(P1Tth-Lac).
Enzymatic
was
assayed
different
substrates
copper.
C1Tth-Lac
showed
higher
dependency
on
copper,
increasing
its
by
1600-fold
for
syringaldazine
(SGZ).
All
mutants
presented
than
phenolic
presence
The
position
signal
associated
CuT2
also
changed,
as
shown
EPR
spectra.
Elucidation
crystal
structure
P1Tth-Lac
mutant
(PDB:
9CPM)
partial
deletion
did
not
significantly
affect
overall
tertiary
compared
to
wild-type
2xu9)
nor
coordination
four
internally
bound
Cu
atoms.
Higher
B-factors
residues
downstream
indicate
increased
flexibility
(Q307,
G308,
P309,
S310)
were
otherwise
more
ordered
structure.
Redox
potential
experiments
platinum
electrodes
have
all
proteins
high
redox
potential,
finding
could
significant
implications
field
protein
research.
Genes,
Journal Year:
2025,
Volume and Issue:
16(4), P. 403 - 403
Published: March 30, 2025
Background/Objectives:
This
review
examines
the
role
of
pharmacogenomics
in
individual
responses
to
pharmacotherapy
various
drugs
abuse,
including
alcohol,
cocaine,
and
opioids,
identify
genetic
variants
that
contribute
variability
substance
use
disorder
treatment
outcomes.
In
addition,
it
explores
pharmacomicrobiomic
aspects
use,
highlighting
impact
gut
microbiome
on
bioavailability,
drug
metabolism,
pharmacodynamics,
pharmacokinetics.
Results:
Research
pharmacogenetics
has
identified
several
promising
may
existing
pharmacotherapies
for
addiction.
However,
interpretation
these
findings
remains
limited.
It
is
estimated
factors
account
20–95%
responses.
Therefore,
alone
cannot
fully
explain
differences
responses,
such
as
diversity
also
play
a
significant
role.
Drug
microbial
biotransformation
produced
by
exoenzymes
convert
low
molecular
weight
organic
compounds
into
analogous
oxidation,
reduction,
hydrolysis,
condensation,
isomerization,
unsaturation,
or
introduction
heteroatoms.
Despite
advances
pharmacomicrobiomics,
challenges
persist
lack
standardized
methodologies,
inter-individual
variability,
limited
understanding
mechanisms,
need
large-scale
validation
studies
develop
microbiota-based
biomarkers
clinical
use.
Conclusions:
Progress
disorders
provided
biological
insights
pharmacological
needs
associated
with
common
drug-metabolizing
enzymes.
The
its
metabolites
pivotal
stages
addiction
seeking,
reward,
biotransformation.
integrating
pharmacomicrobiomics
will
form
crucial
foundation
precision
personalized
medicine.
Processes,
Journal Year:
2025,
Volume and Issue:
13(4), P. 1034 - 1034
Published: March 31, 2025
The
extensive
use
of
pharmaceuticals
in
human
and
veterinary
medicine
has
led
to
their
persistent
environmental
release,
posing
ecological
public
health
risks.
Major
sources
include
manufacturing
effluents,
excretion,
aquaculture,
improper
disposal,
contributing
bioaccumulation
ecotoxicity.
Mycoremediation
is
the
fungal-mediated
biodegradation
pharmaceuticals,
offers
a
promising
sustainable
approach
mitigate
pharmaceutical
pollution.
Studies
have
reported
that
certain
fungal
species,
including
Trametes
versicolor
Pleurotus
ostreatus,
can
degrade
up
90%
contaminants,
such
as
diclofenac,
carbamazepine,
ibuprofen,
within
days
weeks,
depending
on
conditions.
Fungi
produce
range
extracellular
enzymes,
laccases
peroxidases,
alongside
intracellular
enzymes
like
cytochrome
P450
monooxygenases,
which
catalyze
transformation
complex
compounds.
These
play
an
essential
role
modifying,
detoxifying,
mineralizing
xenobiotics,
thereby
reducing
persistence
toxicity.
effectiveness
biotransformation
influenced
by
factors
substrate
specificity,
enzyme
stability,
Optimal
degradation
typically
occurs
at
pH
4.5–6.0
temperatures
20–30
°C.
Recent
advancements
engineering,
immobilization
techniques,
bioreactor
design
improved
catalytic
efficiency
process
feasibility.
However,
scaling
fungal-based
remediation
systems
for
large-scale
applications
remains
challenge.
Addressing
these
limitations
with
synthetic
biology,
metabolic
other
biotechnological
innovations
could
further
enhance
enzymatic
pharmaceuticals.
This
review
highlights
innovations,
applications,
challenges
mycoremediation,
emphasizing
potential
fungi
transformative
solution
waste
management.
Biomolecules,
Journal Year:
2024,
Volume and Issue:
14(3), P. 369 - 369
Published: March 19, 2024
Laccases
are
industrially
relevant
enzymes
that
have
gained
great
biotechnological
importance.
To
date,
most
of
fungal
and
mesophilic
origin;
however,
from
extremophiles
possess
an
even
greater
potential
to
withstand
industrial
conditions.
In
this
study,
we
evaluate
the
a
recombinant
spore-coat
laccase
thermoalkaliphilic
bacterium
Bacillus
sp.
FNT
(FNTL)
biodegrade
antibiotics
tetracycline,
β-lactams,
fluoroquinolone
families.
This
extremozyme
was
previously
characterized
as
being
thermostable
highly
active
in
wide
range
temperatures
(20–90
°C)
very
versatile
towards
several
structurally
different
substrates,
including
recalcitrant
environmental
pollutants
such
PAHs
synthetic
dyes.
First,
molecular
docking
analyses
were
employed
for
initial
ligand
affinity
screening
modeled
site
FNTL.
Then,
silico
findings
experimentally
tested
with
four
consumed
antibiotics,
representatives
each
family:
oxytetracycline,
amoxicillin,
ciprofloxacin.
HPLC
results
indicate
FNTL
help
natural
redox
mediator
acetosyringone,
can
efficiently
91,
90,
82%
tetracycline
(0.5
mg
mL−1)
24
h
at
40,
30,
20
°C,
respectively,
no
apparent
ecotoxicity
products
on
E.
coli
B.
subtilis.
These
complement
our
previous
studies,
highlighting
application
wastewater
bioremediation.
