Revista Mexicana de Biodiversidad,
Journal Year:
2023,
Volume and Issue:
94, P. e955223 - e955223
Published: Dec. 6, 2023
The
alteration
of
forests
due
to
anthropogenic
activities
and
natural
phenomena
has
led
the
development
adaptive
features
so
that
organisms
can
tolerate
it
or
use
their
benefit.
In
this
study,
saprotrophic
fungi
from
a
disturbed
Juniperus
deppeana
forest
were
isolated
identified
for
in
vitro
propagation.
Thirty-one
specimens
collected
propagated
on
malt
extract
agar
(EMA),
potato
dextrose
(PDA),
Kraft
lignin
(A-L)
mineral
medium
(MM).
Taxonomic
identification
was
performed
basis
macro-
micromorphological
characters
basidiomata,
complemented
by
phylogenetic
analysis
ITS
sequences.
Only
7
strains
grew
under
conditions;
they
best
EMA
PDA
media.
Room
temperature
(~22
°C)
preservation
at
4
°C
conditions
maintain
viability
strains.
After
6
months,
preserved
glycerol
(15%)
4°
-20
not
viable.
belong
genera
Agrocybe,
Byssomerulius,
Coniophora
Gymnopus.
Given
environmental
where
isolated,
represent
new
research
prospects
obtaining
biomolecules
biotechnological
interest.
Applied Sciences,
Journal Year:
2023,
Volume and Issue:
13(7), P. 4394 - 4394
Published: March 30, 2023
The
rapid
growth
of
the
human
population
in
recent
decades
has
resulted
intensive
development
various
industries,
urban
agglomerations
and
increased
production
medicines
for
animals
humans,
plant
protection
products
fertilizers
on
an
unprecedented
scale.
Intensive
agriculture,
expanding
areas
newly
established
industrial
plants
release
huge
amounts
pollutants
into
environment,
which,
nature,
are
very
slowly
degraded
or
not
decomposed,
which
leads
to
their
accumulation
water
terrestrial
ecosystems.
Researchers
scouring
extremely
contaminated
environments
identify
organisms
that
have
ability
degrade
resistant
xenobiotics,
such
as
PAHs,
some
pharmaceuticals,
plasticizers
dyes.
These
a
potential
source
enzymes
could
be
used
bioremediation
municipal
wastewater.
Great
hopes
pinned
oxidoreductases,
including
laccase,
called
by
green
biocatalyst
because
end
product
oxidation
wide
range
substrates
this
enzyme
is
other
compounds,
most
often
dimers,
trimers
polymers.
Laccase
immobilization
techniques
use
systems
together
with
adsorption
separation
found
application
enzymatic
Biomolecules,
Journal Year:
2025,
Volume and Issue:
15(4), P. 531 - 531
Published: April 4, 2025
Due
to
their
catalytic
performance,
laccases
constitute
one
of
the
most
promising
groups
enzymes
for
potential
applications
in
modern
biotechnology.
In
this
study,
we
aimed
chemically
modify
Ensifer
meliloti
(Sinorhizobium
meliloti)
and
Cerrena
unicolor
laccase
comparatively
characterize
structures
both
enzymes.
The
characteristic
feature
was
spatial
localization
lysine
residues,
predominantly
positioned
distal
active
site
region
compared
solvent-accessible
surface
area
(SASA)
analysis
showed
that
bacterial
characterized
by
a
larger
hydrophobic
SASA
than
fungal
enzyme.
pKa
prediction
identified
only
Lys
E.
structure
susceptible
modification.
Modifications
were
achieved
using
mono-
bifunctional
crosslinking
agents,
glycosylations
also
performed.
degree
protein
modification
ranged
from
0%
glucose-
galactose-modified
citraconic
anhydride-modified
(CA)
C.
62.94%
palmitic
acid
N-hydroxysuccinimide
ester-modified
stability
covalently
modified
over
wide
pH
temperature
ranges
presence
inhibitors
investigated.
Protein
modifications
with
polymeric
sucrose
(PS)
ethylene
glycol
bis-(succinimidyl
succinate)
(EGNHS)
significantly
increased
activity
15
19%,
respectively.
Although
optima
remained
relatively
unchanged
modifications,
certain
variants,
especially
CA-modified
EGNHS-modified
enzyme,
exhibited
improved
at
near-neutral
(6-7).
Modification
enzyme
glutaraldehyde-carbodiimide
(GA-CDI-ver)
CA
effective
improving
its
thermal
stability.
Chemical
GA,
CDI,
GA-CDI,
PS
allowed
L
3.8
retain
full
5
mM
NaI,
whereas
CA-,
PS-,
variants
retained
even
elevated
NaCl
concentrations.
results
clearly
demonstrate
outcome
chemical
is
closely
linked
enzyme-specific
structural
features
selecting
an
appropriate
strategy
critical
achieving
desired
effect.
BioResources,
Journal Year:
2025,
Volume and Issue:
20(1), P. 1713 - 1724
Published: Jan. 6, 2025
The
laccase
activity
changes
of
the
Auricularia
cornea
var.
Li
strain
were
studied
over
a
continuous
9-day
period
using
different
carbon
sources,
nitrogen
and
lignocellulose
as
liquid
fermentation
inducers.
results
showed
that
addition
alkaline
lignin
all
stimulated
to
secrete
promoted
accumulation
mycelial
biomass.
Both
deficiencies
could
stimulate
produce
more
laccase,
but
they
detrimental
Maltose
peptone
should
be
prioritized
materials
for
cultivating
high-laccase-producing
strains
through
fermentation.
Lignocellulosic
biomass
significantly
enhance
in
Li.
During
cultivation
Li.,
wheat
bran
cottonseed
hulls
produced
high
levels
recommended.
This
study
partially
revealed
production
characteristics
identified
culture
substances
beneficial
secretion
during
growth
stages
mushroom.
provide
foundation
improving
yield
quality
Industrialization,
intensive
farming,
rapid
population
growth
and
urbanization
are
the
source
of
a
large
number
pollutants
entering
environment.
The
current
concentration
xenobiotics
released
into
environment
exceeds
its
natural
ability
to
decompose
them.
Enzymatic
degradation
seems
be
an
environmentally
friendly
process.
Due
wide
spectrum
substrate
specificity,
from
inorganic
compounds
high
molecular
weight
organic
such
as
PAH
or
dyes,
well
favorable
biochemical
properties,
laccase
has
been
used
in
biological
removal
It
is
important
understand
mechanisms
evaluate
final
products
terms
their
toxicity.
oxidizes
substrates
with
simultaneous
reduction
oxygen
water,
which
purest
reaction
co-substrate.
That
why
it
called
green
biocatalyst.
trend
increase
production
enzymes
related
development
industry,
bioremediation
synthetic
chemistry.
This
leads
search
for
laccases
greater
activity
stability
under
extreme
conditions.
potential
degrade
can
promoted
by
improving
enzymatic
catalytic
characterization
using
protein
engineering
other
genetic
methods.
Advances in Environmental and Engineering Research,
Journal Year:
2023,
Volume and Issue:
04(02), P. 1 - 32
Published: May 5, 2023
A
multicopper
oxidase,
laccases
catalyze
the
four-electron
reduction
of
substrate
with
use
molecular
oxygen.
Laccases
are
abundant
in
nature
and
can
be
found
virtually
every
form
life
on
planet.
Generally
speaking,
classified
into
three
types:
blue,
white,
yellow.
Plant,
bacterial
fungal
all
have
same
trinuclear
copper
site
for
reduction.
Non-phenolic
as
well
phenolic
molecules
both
capable
being
catalyzed
by
this
enzyme.
used
a
wide
range
industries
that
make
chemicals.
been
subject
recent
research
because
their
unique
features.
Laccase,
its
sources,
manufacture,
purification,
applications
many
sectors
discussed
length
review.
