Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи
Laccases (benzodiol: oxygen oxidoreductases, EC 1.10.3.2) belong to the so-called blue-copper oxidase family and are coppercontaining enzymes that are involved in oxidative processes by catalyzing the oxidation of various compounds with molecular oxygen, including o- and w-diphenols, aminophenols, p...
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| Date: | 2019 |
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M.M. Gryshko National Botanical Garden of the NAS of Ukraine
2019
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Plant Introduction| _version_ | 1860145068006965248 |
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| author | Zakrasov, A.V. |
| author_facet | Zakrasov, A.V. |
| author_sort | Zakrasov, A.V. |
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| description | Laccases (benzodiol: oxygen oxidoreductases, EC 1.10.3.2) belong to the so-called blue-copper oxidase family and are coppercontaining enzymes that are involved in oxidative processes by catalyzing the oxidation of various compounds with molecular oxygen, including o- and w-diphenols, aminophenols, polyphenols, polyamines, aryl diamines, phenolic substructures of lignin, and also some inorganic ions. The physiological functions of laccases are diverse: participation in the formation of pigments and the formation of fruiting bodies of fungi, detoxification of phenols, catalysis of the oxidation of non-phenolic lignin units (C4-esterified) to radicals.
Laccase activity increases due to the introduction of Cu2+, Mg2+ and Na+, but is strongly inhibited by Fe2+, Ag+, l-cysteine, dithiothreitol and NaN3. In the lower soil layers, the activity of laccase shows a significant increase when supplied with mineral N, the addition of compost leads to increased activity in the surface layer.
The prospects for the practical use of oxidases increased after the discovery of the possibility of enhancing their action using redox mediators, which are substrates of these enzymes, during the oxidation of which highly redox potential and chemically active products are formed. Biocatalytic systems created by nano-technologies (bacterial nanocellulose, carbon nanotubes, magnetic nanoflowers etc.) increase the reaction efficiency by increasing the surface area and loading capacity, and reducing the mass transfer resistance. The effectiveness of immobilization is highly dependent on the process conditions, the properties of the enzyme and the material of the carrier. In particular, a clear correlation was established between the redox potential of the substrate and the efficiency of homogeneous catalysis.
Of particular note is the effect of laccase on soil emissions of CO2 and other greenhouse gases. Participating in the polymerization of soluble phenols, they thereby contribute to humification, forming stable humic fractions that bind soil carbon.
The data presented indicate that soil laccase is an important factor in the functionality of soil, but they need to be studied in more detail in order to understand the mechanisms that regulate their activity. |
| doi_str_mv | 10.5281/zenodo.3566632 |
| first_indexed | 2025-07-17T12:53:29Z |
| format | Article |
| fulltext |
89ISSN 16056574. Інтродукція рослин, 2019, № 4: 89—96
https://doi.org/ 10.5281/zenodo.3566632
UDC 631.465
A.V. ZAKRASOV
M.M. Gryshko National Botanical Garden, National Academy of Sciences of Ukraine
Ukraine, 01014 Kyiv, Timiryazevska str., 1
azakrasov@ukr.net
RESEARCHES OF SOIL LACCASES IN THE 21ST CENTURY:
MAIN DIRECTIONS AND PROSPECTS
Laccases (benzodiol: oxygen oxidoreductases, EC 1.10.3.2) belong to the socalled bluecopper oxidase family and are copper
containing enzymes that are involved in oxidative processes by catalyzing the oxidation of various compounds with molecular
oxygen, including o and wdiphenols, aminophenols, polyphenols, polyamines, aryl diamines, phenolic substructures of lignin,
and also some inorganic ions. The physiological functions of laccases are diverse: participation in the formation of pigments
and the formation of fruiting bodies of fungi, detoxification of phenols, catalysis of the oxidation of nonphenolic lignin units
(C
4
esterified) to radicals.
Laccase activity increases due to the introduction of Cu2+, Mg2+ and Na+, but is strongly inhibited by Fe2+, Ag+, lcysteine,
dithiothreitol and NaN
3
. In the lower soil layers, the activity of laccase shows a significant increase when supplied with mineral
N, the addition of compost leads to increased activity in the surface layer.
The prospects for the practical use of oxidases increased after the discovery of the possibility of enhancing their action using
redox mediators, which are substrates of these enzymes, during the oxidation of which highly redox potential and chemically
active products are formed. Biocatalytic systems created by nanotechnologies (bacterial nanocellulose, carbon nanotubes, mag
netic nanoflowers etc.) increase the reaction efficiency by increasing the surface area and loading capacity, and reducing the
mass transfer resistance. The effectiveness of immobilization is highly dependent on the process conditions, the properties of the
enzyme and the material of the carrier. In particular, a clear correlation was established between the redox potential of the sub
strate and the efficiency of homogeneous catalysis.
Of particular note is the effect of laccase on soil emissions of CO
2
and other greenhouse gases. Participating in the polyme ri
zation of soluble phenols, they thereby contribute to humification, forming stable humic fractions that bind soil carbon.
The data presented indicate that soil laccase is an important factor in the functionality of soil, but they need to be studied
in more detail in order to understand the mechanisms that regulate their activity.
Key words: laccase, enzymatic activity, immobilization, greenhouse gas emissions..
© A.V. ZAKRASOV, 2019
Laccases (benzodiol: oxygen oxidoreductases, EC
1.10.3.2) belong to the socalled bluecopper oxi
dase family and are coppercontaining enzymes
that are involved in oxidative processes by catalyzing
the oxidation of various compounds with molecular
oxygen, including o and wdiphenols, ami no phe
nols, polyphenols, polyamines, aryl dia mi nes, phe
nolic substructures of lignin, and also some inorga
nic ions. [8, 15, 20]. Due to the coordinated inter
action of four copper ions of three different types
that make up the active center of laccases, the en
zyme is able to directly bioelectrocatalyst the mo
lecular oxygen reduction reaction by the mechanism
of direct mediatorless electron transfer from the elect
rode to the active center, followed by oxygen reduc
tion directly to water, bypassing the formation sta ge
intermediate highly reactive toxic oxygen intermedi
ates such as superoxide anion radical l (Og")", hyd ro
xyl radical (OH") and hydrogen peroxide (H
2
O
2
)
[3]. Qi Luo, who described an effective method for
the degradation of perfluorooctanoic acid through a
laccasecatalyz ed oxi dative humification reaction,
concludes that the degradation mechanism involves
the chain reaction of free radicals initiated by their
direct attacks on the CC bond of this perfluoroalkyl
acid [31]. A number of works have shown the high
potential of basidiomycetes as effective destructors of
xenobiotics, including pesticides [18, 24, 26]. Lac
cases are found in many xylotrophic and phyto pa
tho genic fungi, as well as soil saprophy tes.
90 ISSN 16056574. Plant introduction, 2019, № 4
A.V. Zakrasov
Laccase of basidiomycetes of white rot of wood
is able to catalyze the oxidation of nonphenolic
lignin units (C
4
esterified) to radicals, whereby
during this reaction laccase acts in the presence of
radical mediators that are formed during the con
jugated oxidation of thiols or unsaturated lipids
[15, 17]. Laccase presence in cultural filtrates, it
has been proven for most lignindestroying fungi,
including: Coriolus (Trametes) versicolor, C. hirsu
tus, C. zonatus, Phanerochaete chrysosporium, Pleu
ro tus eryngii, Panus tigrinus, Fomes sp., Cerrena ma
xima, Rigidoporis sp., Phellinus sp ., Lentinus tigrinus,
Clitocybula dusenii, Nematoloma forwardii, Pholiota
mutabilis, Collybia sp., Armillariella sp., Co prinus ci
nereus, Phlebia brevispora, Poria cinerescens, Bjerkan
dera adusta, Ganoderma lucidum, Irpex lacteum etc.
In Phanerochaete chrysosporium marked by a rath
er low level of laccase activity [9].
In the literature, there is evidence that copper
ions in the active center of laccases may, in the
process of biosynthesis, appear to be partially re
placed by ions of other metals. For example, two
forms of laccase are found in oyster mushrooms.
One of them, like most other laccases, is induced
by an excess of copper ions, has an absorption max
imum in the blue part of the visible spectrum and
contains four copper ions. The second contains one
copper ion, two zinc ions and one iron ion, and
does not have an absorption maximum of about
600 nm. Instead, it has a broad absorption maximum
at 400 nm. The only difference between the two en
zymes from the other laccases is the lack of activity
towards guaiacol. Leontievsky described the yellow
laccases of the species Partus tigrinus, Phlebia ra
diata, Phlebia tre mellosa and Agaricus bi sporus, iso
lated from solidphase cultures and not having ty
pical spectral and catalytic properties, unlike blue
laccases from submerged cultures. It is assumed that
yellow laccases are formed as a result of the modifi
cation of ordinary blue laccases by decomposition
products of lignin. In this case, the secondary struc
ture and microenvironment of cop per atoms in the
active center change, and yellow laccase acquires
the ability to oxidize stable lignin substructures [2].
In addition, laccase secretion has been described in
a number of bacteria of such species as Proteobacte
ria, Actinobacteria, Bacteroidetes etc [21].
Patricia Luis, using the example of brown forest
soils, describes the specific distribution of laccase
genes and the corresponding fungal species in dif
ferent soil horizons (A
0
, Ad, A
1
): forest litter showed
the highest diversity of genes. In this sa pro phytic
fungi were less common in researched horizons
and demonstrated a higher diversity in laccase
genes than mycorrhizal [23].
This class of enzymes has many functions, both
at the organism level and at the ecosystem level,
and can initiate both positive and negative feed
back loops between soil organisms and soil organ
ic matter. The physiological functions of laccases
are diverse: participation in the processes of for
mation of pigments and the formation of fruit
bodies of fungi, biodegradation of lignin and de
toxification of phenols. In connection with the
above features of this family of enzymes, they are
intensively used in various branches of biotech
nology.
It was reported that laccase with a higher redox
potential tends to have a higher oxidation rate [5,
13]. Gorbachev showed that the efficiency of ca
talysis of high and lowpotential laccases in rela
tion to substrates donor electrons of similar struc
ture linearly depends on the “driving force of the
reaction”, i.e. from the difference between the re
dox potentials of the T1 center of the enzyme and
the substrate. She experimentally proved that chel
ated ions of divalent manganese are natural sub
strates of highly redoxpotential fungal laccases
and the chelated ions of trivalent manganese for
m ed as a result of the enzymatic reaction are ca
pable of nonenzymatic oxidation of the model
compound of lignin — veratric alcohol to veratric
acid. Low redox potential wood laccase does not
catalyze this reaction [1].
Of great interest, both in fundamental and ap
plied terms, is the substrate specificity of these en
zymes, which can oxidize a wide range of organic
as well as inorganic compounds. There is evidence
that the secretion of laccase depends on the culti
vation conditions and may be caused by metallic,
phenolic or aromatic compounds. In particular,
Thiago Santana using the example of Lentinus cri
nitus laccase shows that the interaction of guaiacol
or veratril alcohol and copper (250 µM) added to
91ISSN 16056574. Інтродукція рослин, 2019, № 4
Researches of soil laccases in the 21st century: main directions and prospects
the culture medium causes synergistic effects lead
ing to an increase in the activity of laccase [32].
Ranjit Das, who studied the activity of laccase
from spore cells of Bacillus sp. GZB in the process
of degradation of bisphenol A, claims that the ac
tivity of laccase was increased due to the introduc
tion of Cu2+, Mg2+ and Na+, but was strongly in
hibited by Fe2+, Ag+, lcysteine, dithiothreitol and
NaN
3
[10]. Adeline Vigno at al. reported that the
laccase activity essentially inhibiting with enolog
ical tannins [34]. In order to avoid secondary con
tamination with heavy metals, Yun Zeng suggests
for the oxidation of polycyclic aromatic hydrocar
bons to use Cuindependent bacterial laccase CotA
from Bacillus subtilis, which also has a relatively
high redox potential (525 mV compared to 440 mV
in CueO from Escherichia coli) [38]. Martina Maz
zon testifies that in the lower soil layers, laccase
activity showed a significant increase in the supply
of mineral N, whereas the addition of compost led
to increased activity in the surface layer [25].
Laccases can quickly oxidize benzo[a]pyrene. It
is believed that the metabolites with increasing
solubility in water caused by the oxidation of ben
zo[a]pyrene, can stimulate the subsequent miner
alization. Jun Zeng suggests that the soil contami
nated with benzo[a]pyrene can be detoxified by
laccase mainly by forming a bound residue for the
organic matter of the soil by covalent binding. Lac
case contributed to the dissociation of benzo[a]
pyrene (15.6 %) from the soil, followed by trace
mineralization (<0.58 ± 0.02 %) and the forma
tion of a substantial bound residue (~ 80 %). In
crease ~ 15 % in the related residual fraction was
observed when the action of laccase, which was
mainly due to covalent binding residues humic
fraction. In contrast, benzo[a]pyrene, treated with
laccase, led to a smaller shift in the composition of
the bacterial community, which indicates a de
crease in the disturbance of soil microbial com
munities [38]. Navada reports that the addition of
mediators (syringaldehyde, vanillin, ABTS and 9 naphthol) accelerated the decomposition of chlo
ramphenicol from 10 % to 100 % within 48 hours [28].
Despite the fact that enzymes have a unique
and unprecedented catalytic activity and selectivity
over a wide range of substances, problems related
to their stability often hinder their use in real envi
ronmental conditions. Interest in the practical use
of oxidases increased in the mid1990s, after the
discovery of the possibility of enhancing the ac
tion of these enzymes using various redox media
tors [7], which made it possible to significantly
expand the scope of their practical application.
MSO mediators are substrates of these enzymes,
in the process of oxidation of which highly redox
potential and chemically active products are formed.
The latter can react with compounds that are not
subjected to oxidation by oxide alone or partici
pate in electron transfer in electrochemical reac
tions, accelerating electrochemical processes in
volving these enzymes. In addition, during the
oxidation of organic substrates, free radicals are
formed, which can modify other compounds [19].
Biocatalytic systems created with the help of
nanotechnology have attracted attention for many
applications, since nanoscale carriers for immobi
lizing enzymes can improve the factors that deter
mine efficiency, for example, increasing surface area
and loading capacity and reducing mass transfer
resistance. Laccases, which play an important role
in the degradation of soil phenol or phenollike
substances, can be potentially used to restore the
soil through immobilization through physical ad
sorption or covalent binding. So Mitra Naghdi found
that immobilized laccase has a higher stability with
respect to temperature and pH changes. compared
to free laccase. In addition, the immobilized lac
case retained its catalytic cha racteristics for up to
seven recycling cycles and shows more than 50 %
of the initial activity after two months of storage at
room temperature [27]. There is evidence that Fe
and Alcontaining mi nerals can adsorb extracel
lular enzymes in the soil environment [35]. This is
consistent with the results of Wendy Hernandez
Mo niaras, which suggests that laccase activity in
the intracellular fraction of Fusarium oxyspo
rum f. sp. lycopersici wildtype and mutant strains
increases with the addition of iron chelator (53.4
and 114.32 %, respectively) [16].
However, the efficiency of immobilization strongly
depends on the conditions of immobilization and
the properties of the enzyme and the material of
the carrier. So, on the basis of a comprehensive
92 ISSN 16056574. Plant introduction, 2019, № 4
A.V. Zakrasov
study of the biochemical, spectral and electro
chemical characteristics of blue coppercontain
ing oxidases with different values of the redox po
tential of T1 centers, Shleev established a clear
correlation between the substrate redox potential
and the effectiveness of homogeneous catalysis and
suggested the presence of an endodermic stage in
the process of intramolecular electron transfer
with T1 center on T2/TZ copper cluster of highly
redoxpotential coppercontaining oxidases. Ac
cording to the model proposed by him, the mech
anism and efficiency of bioelectrocatalysis depend
on the orientation of enzyme molecules on the
electrode surface. The orientation of the T1 enzy
mes center to the electrode surface determines the
effective bioelectrocatalytic reduction of molecu
lar oxygen by the mechanism of direct electron
transfer [4].
Haibin Yuan, who conducted a comparative
analysis of the process of immobilizing laccase
on bacterial nanocellulose (BNC), produced by
four different strains, showed that different types
of BNCimmobilized laccase had different affini
ty for the substrate, while all of them showed high
operational stability after ten consecutive biocata
lytic reaction cycles. The results show that the
structural diversity of BNC from different strains
can directly lead to different efficiencies in the im
mobilization of laccase, with the white fiber net
work in the BNC with high porosity particularly
effectively promotes the immobilization of the en
zyme [36]. Monica Bansal found that the activity
of laccase immobilized on nanocellulose fibers re
mained at 60.5 % even after 15 repeated uses,
while the enzyme remained immobilized stable
with a relative activity of 75 % after 45 days [6].
Among nanomaterials, carbon nanotubes (CNTs)
have unique features as support for the immobili
zation of the enzyme, that is, with a high surface
to volume ratio, a porous structure, and the pres
ence of functional groups on its surface. Linson Lo
nappan in his research, shows that laccase immo
bilized on CNTs has a shelf life of three times
higher than that of the free enzyme, and notes that
regardless of the origin of the substrate, when the
initial concentration of laccase in the raw solution
increased, the binding capacity and the result, the
immobilization efficiency also increased. The
same author proposes, in order to increase the ef
ficiency of immobilization, the preliminary func
tionalization of the substrate with citric acid [22].
Everton Skoronski, using the example of CNTim
mobilized laccase from Aspergillus oryzae, demon
strated that under stable conditions, the enzyme
quickly loses its activity after the second reaction
cycle during immobilization using physical adsor p
tion, while using the covalent bond method, about
80 % of the activity remains after six cycles [33].
Meihua Fu, who studied the issues of biodegra
dation of bisphenol A (BPA), proposes to use the
socalled immobilization substrate. Magnetic na
noflowers (MNF) — spherical, porous and hierar
chical structures with an average diameter of 15 µm,
filled with laccase, by attaching amino functional
magnetic nanoparticles to a hybrid laccaseinor
ganic base. He reports that under optimal condi
tions in the presence of ABTS, MNF reached 100 %
BPA degradation in just 5 minutes. In addition,
after 60 days of storage at 4 °C, more than 92 % of
the initial activity of the laccase remained. After
processing the MNF and their reuse for 5 cycles,
only a 5 % decrease in the efficiency of degrada
tion of BFA was observed [11]. Significant results
in the field of bisphenol biodegradation are re
ported by Jakub Zdart, who used the new material
based on the sponge Hippospongia communis as a
biopolymer basis for immobilizing laccase from
Trametes versicolor. He has shown that under op
timal conditions, almost 100 % of BPA and BPF
and more than 40 % of BPS are removed from the
solution at a concentration of 2 mg/ml. Laccase
immobilized in this way has a high reusability and
storage stability, retaining more than 80 % of its
initial activity after 50 days of storage. In addition,
they identified the main biodegradation products
BPA and BPF. It was shown that after the oxida
tion of bisphenols by immobilized laccase, mainly
dimers and trimers are formed [37]. Osikoya re
ports that the adsorption capacity increases sig
nificantly with doping of graphene nanosheets
with O, N and Cl atoms. [29] .
Special attention should be paid to the participa
tion of laccase in the soil emission of CO
2
and other
greenhouse gases. To mitigate climate change, it is
93ISSN 16056574. Інтродукція рослин, 2019, № 4
Researches of soil laccases in the 21st century: main directions and prospects
necessary to reduce or slow down the accumula
tion of greenhouse gases in the atmosphere by in
creasing sequestration and storing C in the soil.
Carbon sequestration usually refers to medium
and longterm (15—50 years) storage of C in ter
restrial ecosystems, in underground conditions,
mainly in the form of carbonates or in the oceans.
The net amount of sequestered C is a longterm
balance between absorption and release of C.
Soils have the ability to adapt to the addition of
significant amounts of C from the atmosphere
through photosynthesis and to isolate it for a suf
ficiently long time to substantially reduce the ac
cumulation of atmospheric CO
2
.
Unlike theories of humic substances (HS) as
high molecular weight polymers, recent theories
have suggested that HS are supramolecules con
sisting of associations of small heterogeneous mo
lecules held together not by covalent bonds, but by
weak forces, such as dispersive hydrophobic inter
actions (Van der Waals, : ; : , CH: binding) and
hydrogen bonds in the adjacent hydrophilic and
hydrophobic domains, apparently, of high molec
ular size. This unstable conformation is stabilized
by an increase in intermolecular covalent bonds
by oxidation enzymes, such as phenol oxidase. It
was found that the coppercontaining phenol oxi
dase enzyme, laccase, is produced by soil fungi
and mycorrhiza. Laccases are probably the largest
class of ligninolytic enzymes in the soil and per
form various oxidative and polymeric functions.
The enzymes of the first group are mainly involved
in the breakdown of lignin, while the latter are
mainly involved in the polymerization of soluble
phenols, thereby promoting humification and [12].
The data collected in this study suggest a rela
tionship between the amount and expression of
the bacterial LMCO (laccaselike multicopper oxi
dases) genes on the one hand, and the amount and
stability of HA with the other. The soils under the ve
getation cover are processed by mechanical methods,
where, after 30 years of experiments, the highest
levels of HA were obtained, showed the maximum
population of bacteria rich in laccase genes. In ad
dition, environmental conditions con tributed to a
corresponding higher level of gene expression in
these soils compared to other modes. The structure
of the bacterial community based on the LMCO
genes also indicates a phylogenetic difference in
the SM soils because of the farming system used.
Kwan Meng Go suggests that hydrophilic com
ponents, released from the microbial degradation
of plant tissues or formed as a result of microbial
synthesis, should be gradually sequestered in the hyd
r ophobic humus domains to protect against fur th er
degradation. Persistent humic fractions con tain main
ly aliphatic or alkyl (lipid structures) compounds.
Hydrophobic protection is most effective for frac
tions of silt and clay. However, hydrophobic C se
questration can also occur with larger soil particles.
The stability of the soil as a whole increased and
was maintained with time by hydrophobic, but not
by hydrophilic components of organic matter. This
implies that the total soil stability or stabilization
of C can be improved by increasing the hydropho
bicity of the native humus or by adding materials,
such as organic waste or lignite, with high hydro
phobic components.
Several biological mechanisms and processes
have also been proposed, but the extent and rela
tive significance of these mechanisms are still un
clear. These include the classical model of the for
mation and organization of aggregates, in which
microaggregates are interconnected by roots and
fungal hyphae and temporary (polysaccharides)
agents, the role of residues of roots and rhizomes
of plants, the production of laccase enzymes by
white rot and mycorrhiza, a variety of microbial
communities and the formation of organic refrac
tory compounds microbiota soil anthropodes. Most
of these proposals are at the experimental stage,
and there is currently insufficient data to verify and
confirm the proposed mechanisms [14].
Asrin Partavian, based on the fact that laccases
are central to the decomposition of an inaccessi
ble SOM, suggested that plants and elevated levels
of CO
2
stimulate laccase activity. Increased CO
2
levels have amplified the yield of Deschampsia
flexuosa and underground respiration. Plants sti
mulated microbial soil biomass, respiration un
derground and laccase activity, and laccase stimu
lation caused by plants was particularly noticeable
in the soil subjected to prolonged exposure to in
creased CO
2
in the field, while laccase activity did
94 ISSN 16056574. Plant introduction, 2019, № 4
A.V. Zakrasov
not affect the shortterm increase in CO
2
. There
fore, actively growing plants can stimulate laccase
activity, but the potential for plantinduced lac
case production seems to depend on the potential
for laccase production in the soil. In addition, the
initial differences in laccase production potential
prevailed during the sixmonth experimental period
regardless of the current level of CO
2
, although dur
ing this period the productivity of plants increased
with an increased level of CO
2
. Thus, although lac
case activity depends on the presence of a plant,
the potential for laccase production does not respond
quickly to an increase in plant production [30].
The given data show that the soil laccase — im
portant factor of soil functionality, but they should
be investigated in more detail to understand the
mechanisms that regulate their activities.
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Recommended by N.V. Zaimenko
Received 30.05.2019
Закрасов А.В.
Национальный ботанический сад
имени Н.Н. Гришко НАН Украины,
Украина, г. Киев
ИССЛЕДОВАНИЯ ПОЧВЕННЫХ ЛАККАЗ В XXI в.:
ОСНОВНЫЕ НАПРАВЛЕНИЯ И ПЕРСПЕКТИВЫ
Лакказы относятся к синемедным оксидазам, являясь
Cuсодержащими ферментами, катализирующими
окисление соединений молекулярным кислородом,
включая о и wдифенолы, аминофенолы, полифено
лы, полиамины, арилдиамины, фенольные подструк
туры лигнина и некоторые неорганические ионы.
Физиологические функции лакказ разнообразны: учас
тие в формировании пигментов и образовании пло
довых тел грибов, детоксификация фенолов, катализ
окисления нефенольных лигниновых единиц (С
4
эте
рифицированных) до радикалов.
Активность лакказы возрастает за счет введения
Cu2+, Mg2+ и Na+, но сильно ингибируется Fe2+, Ag+,
lцистеином, дитиотреитолом и NaN
3
. В нижних сло
ях почвы активность лакказы значительное увеличи
вается при снабжении минеральным азотом. Добав
ление компоста приводит к повышенной активности
в поверхностном слое.
96 ISSN 16056574. Plant introduction, 2019, № 4
A.V. Zakrasov
Перспективы практического использования оксидаз
расширились после открытия возможности усиления
их действия с использованием редоксме диа торов,
представляющих собой субстраты этих фермен тов, в
процессе окисления которых образуются вы сокоре
докспотенциальные и химически активные продук
ты. Биокаталитические системы, создаваемые путем
нанотехнологий (бактериальная наноцеллюлоза, уг
ле родные нанотрубки, магнитные нанобукеты и др.),
повышают эффективность реакции за счет увеличе
ния площади поверхности и загрузочной способности
и уменьшения сопротивления массо переноса. Эффек
тивность иммобилизации в значительной степени за
висит от условий процесса, свойств фермента и мате
риала носителя. В частности, установлена четкая кор
реляция между редокспо тен циа лом субстрата и эф
фективностью гомо генного катализа.
Отдельного внимания заслуживает влияние лак
казы на почвенную эмиссию СО
2
и других парнико
вых газов. Участвуя в полимеризации растворимых
фенолов, они способствуют гумификации, образуя
стойкие гуминовые фракции, связывающие почвен
ный углерод.
Приведенные данные свидетельствуют о том, что
почвенные лакказы — важный фактор функциональ
ности почвы, но необходимо провести дополнитель
ные исследования, чтобы понять механизмы, регу
лирующие их деятельность.
Ключевые слова: лакказа, ферментативная активность,
иммобилизация, эмиссия парниковых газов.
Закрасов О.В.
Національний ботанічний сад
імені М.М. Гришка НАН України,
Україна, м. Київ
ДОСЛІДЖЕННЯ ҐРУНТОВИХ ЛАКАЗ У ХХІ ст. :
ОСНОВНІ НАПРЯМИ ТА ПЕРСПЕКТИВИ
Лакази належать до синьомідних оксидаз, будучи
Cuвмісними ферментами, котрі каталізують окиснен
ня сполук молекулярним киснем, зокрема о і wди
феноли, амінофеноли, поліфеноли, поліаміни, арил
діаміни, фенольні підструктури лігніну та деякі неор
ганічні іони. Фізіологічні функції лаказ різноманітні:
участь у формуванні пігментів і створенні плодових
тіл грибів, детоксикація фенолів, каталіз окиснення
нефенольних лігнінових одиниць (С
4
етерифікова них)
до радикалів.
Активність лаказ значно зростає за рахунок вве
дення Cu2+, Mg2+ і Na+, але сильно інгібується Fe2+,
Ag+, lцистеїном, дітіотреїтолом та NaNО
3
. У нижніх
шарах ґрунту активність лакази значно збільшується
при постачанні мінерального азоту. Додавання ком
посту спричиняє підвищену активність у поверхне
вому шарі.
Перспективи практичного застосування оксидаз
розширилися після відкриття можливості посилення
їх дії з використанням редоксмедіаторів, котрі явля
ють собою субстрати цих ферментів, у процесі окис
нення яких утворюються високоредокспо тен ційні
та хімічно активні продукти. Біокаталітичні системи,
створені шляхом нанотехнологій (бактеріальна на
ноцелюлоза, вуглецеві нанотрубки, магнітні нанобу
кети тощо), підвищують ефективність реакції завдя
ки збільшенню поверхні та завантажувальної здат
ності та зменшенню опору масопереносу. Ефектив
ність іммобілізації значною мірою залежить від умов
процесу, властивостей ферменту та матеріалу носія.
Зокрема встановлено чітку кореляцію між ре докс
потенціалом субстрату та ефективністю гомогенного
каталізу.
На окрему увагу заслуговує вплив лакази на ґрунто
ву емісію СО
2
та інших парникових газів. Беручи
участь у полі меризації розчинних фенолів, вони спри
яють гуміфікації, створюючи стійкі гумінові фракції,
які зв’я зу ють ґрунтовий вуглець.
Наведені дані свідчать про те, що ґрунтові лакази —
важливий чинник функціональності ґрунту, але необ
хідно провести додаткові дослідження, щоб зрозуміти
механізми, котрі регулюють їх діяльність.
Ключові слова: лаказа, ферментативна активність, ім
мобілізація, емісія парникових газів.
|
| id | oai:ojs2.plantintroduction.org:article-1534 |
| institution | Plant Introduction |
| keywords_txt_mv | keywords |
| language | English |
| last_indexed | 2025-07-17T12:53:29Z |
| publishDate | 2019 |
| publisher | M.M. Gryshko National Botanical Garden of the NAS of Ukraine |
| record_format | ojs |
| resource_txt_mv | wwwplantintroductionorg/8a/26a58d47e2eb9ac17fa666bf4167e18a.pdf |
| spelling | oai:ojs2.plantintroduction.org:article-15342019-12-14T18:51:01Z Researches of soil laccases in the 21st century: main directions and prospects Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи Zakrasov, A.V. Laccases (benzodiol: oxygen oxidoreductases, EC 1.10.3.2) belong to the so-called blue-copper oxidase family and are coppercontaining enzymes that are involved in oxidative processes by catalyzing the oxidation of various compounds with molecular oxygen, including o- and w-diphenols, aminophenols, polyphenols, polyamines, aryl diamines, phenolic substructures of lignin, and also some inorganic ions. The physiological functions of laccases are diverse: participation in the formation of pigments and the formation of fruiting bodies of fungi, detoxification of phenols, catalysis of the oxidation of non-phenolic lignin units (C4-esterified) to radicals. Laccase activity increases due to the introduction of Cu2+, Mg2+ and Na+, but is strongly inhibited by Fe2+, Ag+, l-cysteine, dithiothreitol and NaN3. In the lower soil layers, the activity of laccase shows a significant increase when supplied with mineral N, the addition of compost leads to increased activity in the surface layer. The prospects for the practical use of oxidases increased after the discovery of the possibility of enhancing their action using redox mediators, which are substrates of these enzymes, during the oxidation of which highly redox potential and chemically active products are formed. Biocatalytic systems created by nano-technologies (bacterial nanocellulose, carbon nanotubes, magnetic nanoflowers etc.) increase the reaction efficiency by increasing the surface area and loading capacity, and reducing the mass transfer resistance. The effectiveness of immobilization is highly dependent on the process conditions, the properties of the enzyme and the material of the carrier. In particular, a clear correlation was established between the redox potential of the substrate and the efficiency of homogeneous catalysis. Of particular note is the effect of laccase on soil emissions of CO2 and other greenhouse gases. Participating in the polymerization of soluble phenols, they thereby contribute to humification, forming stable humic fractions that bind soil carbon. The data presented indicate that soil laccase is an important factor in the functionality of soil, but they need to be studied in more detail in order to understand the mechanisms that regulate their activity. Лакази належать до синьо-мідних оксидаз, будучи Cu-вмісними ферментами, котрі каталізують окиснення сполук молекулярним киснем, зокрема о- і w-дифеноли, амінофеноли, поліфеноли, поліаміни, арилдіаміни, фенольні підструктури лігніну та деякі неорганічні іони. Фізіологічні функції лаказ різноманітні: участь у формуванні пігментів і створенні плодових тіл грибів, детоксикація фенолів, каталіз окиснення нефенольних лігнінових одиниць (С4-етерифікова них) до радикалів. Активність лаказ значно зростає за рахунок введення Cu2+, Mg2+ і Na+, але сильно інгібується Fe2+, Ag+, l-цистеїном, дітіотреїтолом та NaNО3. У нижніх шарах ґрунту активність лакази значно збільшується при постачанні мінерального азоту. Додавання компосту спричиняє підвищену активність у поверхневому шарі. Перспективи практичного застосування оксидаз розширилися після відкриття можливості посилення їх дії з використанням редокс-медіаторів, котрі являють собою субстрати цих ферментів, у процесі окиснення яких утворюються високо-редокс-потенційні та хімічно активні продукти. Біокаталітичні системи, створені шляхом нанотехнологій (бактеріальна наноцелюлоза, вуглецеві нанотрубки, магнітні нанобукети тощо), підвищують ефективність реакції завдяки збільшенню поверхні та завантажувальної здатності та зменшенню опору масо-переносу. Ефективність іммобілізації значною мірою залежить від умов процесу, властивостей ферменту та матеріалу носія. Зокрема встановлено чітку кореляцію між редокспотенціалом субстрату та ефективністю гомогенного каталізу. На окрему увагу заслуговує вплив лакази на ґрунтову емісію СО2 та інших парникових газів. Беручи участь у полі меризації розчинних фенолів, вони сприяють гуміфікації, створюючи стійкі гумінові фракції, які зв’язують ґрунтовий вуглець. Наведені дані свідчать про те, що ґрунтові лакази – важливий чинник функціональності ґрунту, але необхідно провести додаткові дослідження, щоб зрозуміти механізми, котрі регулюють їх діяльність. M.M. Gryshko National Botanical Garden of the NAS of Ukraine 2019-12-01 Article Article application/pdf https://www.plantintroduction.org/index.php/pi/article/view/1534 10.5281/zenodo.3566632 Plant Introduction; Vol 84 (2019); 89-96 Інтродукція Рослин; Том 84 (2019); 89-96 2663-290X 1605-6574 10.5281/zenodo.3572674 en https://www.plantintroduction.org/index.php/pi/article/view/1534/1477 http://creativecommons.org/licenses/by/4.0 |
| spellingShingle | Zakrasov, A.V. Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи |
| title | Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи |
| title_alt | Researches of soil laccases in the 21st century: main directions and prospects |
| title_full | Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи |
| title_fullStr | Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи |
| title_full_unstemmed | Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи |
| title_short | Дослідження ґрунтових лаказ у ХХІ ст.: основні напрями та перспективи |
| title_sort | дослідження ґрунтових лаказ у ххі ст.: основні напрями та перспективи |
| url | https://www.plantintroduction.org/index.php/pi/article/view/1534 |
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