Transformation of humic acids by two-domain laccase from Streptomyces anulatus

Lisov, A. V.; Трубицина, Л.И.; Lisova, Zoya A.; Trubitsin, Ivan Vasilyevich; Заварзина, А. Г.; Leontievsky, A. A.

doi:10.1016/j.procbio.2018.11.001

Cited by 19 publications

(12 citation statements)

References 52 publications

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“…3.4-Dimethoxybenzoic alcohol and p-hydroxybenzoic acid were not oxidized by two-domain laccase alone. Humic acids are polymerized by two-domain laccase [33], which was also the result of the present study (Fig 3). Three-domain fungal laccases can depolymerize HA at acidic pH-both directly [4,31,50] and in the presence of mediators [51].…”

Section: Interaction Of Spsl With Low Molecular Weight Substrates Andsupporting

confidence: 87%

“…Secretion is characteristic of both two-domain and three-domain laccase [ 48 , 49 ]. SpSL is a trimeric protein like other two-domain laccases reported previously [ 17 , 48 ], although there is a report on the octameric enzyme [ 33 ]. The absorption maximum at 600 nm in the SpSL spectrum is due to the presence of the T1-copper center, while a shoulder at 340 nm is due to the presence of the T3-copper center in the enzyme.…”

Section: Discussionmentioning

confidence: 99%

“…Gel-filtration. The molecular weight distributions of the HA and phenolic acids and the products of their reaction with two-domain laccase were obtained in conditions similar to those previously described [33]. The column filled with Sephadex G-75 gel was used.…”

Section: Reactions Of Two-domain Laccase With Humic Acid In the Presementioning

confidence: 99%

“…It has been shown that three-domain fungal laccase can polymerize and depolymerize humic acids (HA) both in vivo and in vitro [ 4 , 31 , 32 ]. Two-domain bacterial laccase polymerized humic acids and their low- and high-molecular weight fractions [ 33 ]. Thus, both forms of laccase play a potentially important role in the transformation of components of soil organic matter (SOM).…”

Section: Introductionmentioning

confidence: 99%

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Transformation of low molecular compounds and soil humic acid by two domain laccase of Streptomyces puniceus in the presence of ferulic and caffeic acids

et al. 2020

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The two-domain bacterial laccases oxidize substrates at alkaline pH. The role of natural phenolic compounds in the oxidation of substrates by the enzyme is poorly understood. We have studied the role of ferulic and caffeic acids in the transformation of low molecular weight substrates and of soil humic acid (HA) by two-domain laccase of Streptomyces puniceus (SpSL, previously undescribed). A gene encoding a two-domain laccase was cloned from S. puniceus and over-expressed in Escherichia coli. The recombinant protein was purified by affinity chromatography to an electrophoretically homogeneous state. The enzyme showed high thermal stability, alkaline pH optimum for the oxidation of phenolic substrates and an acidic pH optimum for the oxidation of K 4 [Fe(CN) 6 ] (potassium ferrocyanide) and ABTS (2,2 0-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt). Phenolic compounds were oxidized with lower efficiency than K 4 [Fe(CN) 6 ] and ABTS. The SpSL did not oxidize 3.4-dimethoxybenzoic alcohol and p-hydroxybenzoic acid neither in the absence of phenolic acids nor in their presence. The enzyme polymerized HA-the amount of its high molecular weight fraction (>80 kDa) increased at the expense of low MW fraction (10 kDa). The addition of phenolic acids as potential mediators did not cause the destruction of HA by SpSL. In the absence of the HA, the enzyme polymerized caffeic and ferulic acids to macromolecular fractions (>80 kDa and 10-12 kDa). The interaction of SpSL with HA in the presence of phenolic acids caused an increase in the amount of HA high MW fraction and a twofold increase in the molecular weight of its low MW fraction (from 10 to 20 kDa), suggesting a cross-coupling reaction. Infrared and solution-state 1 H-NMR spectroscopy revealed an increase in the aromaticity of HA after its interaction with phenolic acids. The results of the study expand our knowledge on the transformation of natural substrates by two-domain bacterial laccases and indicate a potentially important role of the enzyme in the formation of soil organic matter (SOM) at alkaline pH values.

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Section: Interaction Of Spsl With Low Molecular Weight Substrates Andsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Reactions Of Two-domain Laccase With Humic Acid In the Presementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Transformation of low molecular compounds and soil humic acid by two domain laccase of Streptomyces puniceus in the presence of ferulic and caffeic acids

et al. 2020

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“…Bacterial laccases can contain two or three structural and functional domains. Contrary to the three-domain laccases, which are active in monomeric form, two-domain laccases are active in multimeric forms (homotrimers, homohexamers) (Lisov et al, 2019). All the 12 two-domain laccases characterized to date were found in bacteria belonging to the phylum Actinobacteria, the majority of them were isolated from Streptomyces.…”

Section: Introductionmentioning

confidence: 99%

Expression of thermophilic two-domain laccase from Catenuloplanes japonicus in Escherichia coli and its activity against triarylmethane and azo dyes

Трубицина

Abdullatypov

Larionova

et al. 2021

PeerJ

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Background Two-domain laccases are copper-containing oxidases found in bacteria in the beginning of 2000ths. Two-domain laccases are known for their thermal stability, wide substrate specificity and, the most important of all, their resistance to so-called «strong inhibitors» of classical fungal laccases (azides, fluorides). Low redox potential was found to be specific for all the two-domain laccases, due to which these enzymes lost the researchers’ interest as potentially applicable for various biotechnological purposes, such as bioremediation. Searching, obtaining and studying the properties of novel two-domain laccases will help to obtain an enzyme with high redox-potential allowing its practical application. Methods A gene encoding two-domain laccase was identified in Catenuloplanes japonicus genome, cloned and expressed in an Echerichia coli strain. The protein was purified to homogeneity by immobilized metal ion affinity chromatography. Its molecular properties were studied using electrophoresis in native and denaturing conditions. Physico-chemical properties, kinetic characteristics, substrate specificity and decolorization ability of laccase towards triphenylmethane dyes were measured spectrophotometrically. Results A novel two-domain recombinant laccase CjSL appeared to be a multimer with a subunit molecular mass of 37 kDa. It oxidized a wide range of phenolic substrates (ferulic acid, caffeic acid, hydroquinone, catechol, etc.) at alkaline pH, while oxidizing of non phenolic substrates (K4[Fe(CN)6], ABTS) was optimal at acidic pH. The UV-visible absorption spectrum of the purified enzyme was specific for all two-domain laccases with peak of absorption at 600 nm and shoulder at 340 nm. The pH optima of CjSL for oxidation of ABTS and 2, 6-DMP substrates were 3.6 and 9.2 respectively. The temperature optimum was 70 °C. The enzyme was most stable in neutral-alkaline conditions. CjSL retained 53% activity after pre-incubation at 90 °C for 60 min. The enzyme retained 26% activity even after 60 min of boiling. The effects of NaF, NaN3, NaCl, EDTA and 1,10-phenanthroline on enzymatic activity were investigated. Only 1,10-phenanthroline reduced laccase activity under both acidic and alkaline conditions. Laccase was able to decolorize triphenylmethane dyes and azo-dyes. ABTS and syringaldehyde were effective mediators for decolorization. The efficacy of dye decolorization depended on pH of the reaction medium.

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Laccases for Soil Bioremediation

Guauque-Torres

Bustos

2019

Microorganisms for Sustainability

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Transformation of humic acids by two-domain laccase from Streptomyces anulatus

Cited by 19 publications

References 52 publications

Transformation of low molecular compounds and soil humic acid by two domain laccase of Streptomyces puniceus in the presence of ferulic and caffeic acids

Transformation of low molecular compounds and soil humic acid by two domain laccase of Streptomyces puniceus in the presence of ferulic and caffeic acids

Expression of thermophilic two-domain laccase from Catenuloplanes japonicus in Escherichia coli and its activity against triarylmethane and azo dyes

Laccases for Soil Bioremediation

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