Characterization of a Novel Laccase LAC-Yang1 from White-Rot Fungus Pleurotus ostreatus Strain Yang1 with a Strong Ability to Degrade and Detoxify Chlorophenols

Liu, Xinping; Deng, Wei; Yang, Yang

doi:10.3390/molecules26020473

Cited by 18 publications

(5 citation statements)

References 53 publications

(50 reference statements)

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“…Inorganic ions like fluoride-, chloride-, azide-can bind to Т2/Т3 active center of laccase and block the electron transfer from T1 copper center (Xu, 1996;Gianfreda, Xu & Bollag, 1999). Most of the three-domain fungal laccases are completely inhibited by 1 mM sodium azide (Liu, Deng & Yang, 2021;Nitheranont, Watanabe & Asada, 2011). LMCO, S. pristinaespiralis (Reiss et al, 2013;Ihssen et al, 2015) 38 But this inhibition effect of azide ions was not observed in case of CjSL (at alkaline pH).…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…Most bacterial laccases exhibit their highest activity below 40 °C. Most laccases have an activity of less than half of the highest level below 30 °C [ 12 , 22 , 23 , 24 , 25 , 26 , 27 ]. In contrast, L01 exhibits higher activity at 10 °C and 20 °C and relatively better thermostability compared to that of other laccases, which indicates that L01 is a typical cold-adapted laccase.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Jiang

Deng

Wang³

et al. 2023

Molecules

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Laccases have been widely used for fruit juice clarification, food modification, and paper pulp delignification. In addition, laccases exhibit remarkable performance in the degradation of toxic substances, including pesticides, organic synthetic dyes, antibiotics, and organic pollutants. Thus, the screening and development of robust laccases has attracted significant attention. In this study, Vibrio sp. LA is a strain capable of producing cold-adapted laccases. The laccase coding gene L01 was cloned from this strain and expressed in Yarrowia lipolytica, a host with good secretion ability. The secreted L01 (approximate MW of 56,000 Da) had the activity and specific activity of 18.6 U/mL and 98.6 U/mg toward ABTS, respectively. The highest activity occurred at 35 °C. At 20 °C, L01 activity was over 70% of the maximum activity in pH conditions ranging from 4.5–10.0. Several synthetic dyes were efficiently degraded by L01. Owing to its robustness, salt tolerance, and pH stability, L01 is a promising catalytic tool for potential industrial applications.

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“…As for TCP, the toxicity, persistence, and biodegradability depend on the number and position of chlorine substituents in the phenolic ring (Rubilar et al 2008 ). Çabuk et al revealed that TCP was dechlorinated by laccase (Çabuk et al 2012 ) and Liu et al demonstrated that laccase could achieve a good detoxification effect while degrading chlorophenols (Liu et al 2021 ). Also, the acute toxicity test pointed out that the detected metabolites of NP were less toxic than the parent compound after laccase treatment (Mtibaà et al 2020 ).…”

Section: Resultsmentioning

confidence: 99%

Efficient biodegradation of straw and persistent organic pollutants by a novel strategy using recombinant Trichoderma reesei

Xia

Lin

2022

Bioresour. Bioprocess.

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Efficient biodegradation of lignocellulosic biomass needs a battery of enzymes targeting cellulose, hemicellulose, and lignin. In this study, recombinant Trichoderma reesei ZJ-09 with Pycnoporus sanguineus laccase gene was used to degrade rice straw by in situ production of laccase, xylanase, and cellulases under solid-state fermentation (SSF). Effects of parameters on key enzymes (cellulase, xylanase, and laccase) in biodegradation during SSF were investigated. Under the optimized SSF conditions, the FPA, xylanase activity, and laccase activity reached 110.47 FPU/g, 5787.59 IU/g, and 24.45 IU/g, respectively, on day 12. The obtained recombinant T. reesei SSF system achieved efficient degradation of rice straw with the final mass loss up to 51.16% which was 1.4-fold higher than the host strain. Further, bioconversion of rice straw into a novel laccase-enriched koji for persistent organic pollutants bioremediation (LKPB) was conducted by the optimized SSF system. LKPB was found to degrade persistent organic pollutants (POPs) effectively without the addition of mediators. 4-h removal rates of three POPs mediated by LKPB (87.21% for 2,4,5-trichlorophenol, 92.45% for nonylphenol, and 90.73% for oxytetracycline) were comparable to those achieved by laccase-co-mediator system. The newly established recombinant T. reesei SSF system could be potential to effectively degrade lignocellulosic wastes as well as organic pollutants. Graphical abstract

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Characterization of a Novel Laccase LAC-Yang1 from White-Rot Fungus Pleurotus ostreatus Strain Yang1 with a Strong Ability to Degrade and Detoxify Chlorophenols

Cited by 18 publications

References 53 publications

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

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

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Efficient biodegradation of straw and persistent organic pollutants by a novel strategy using recombinant Trichoderma reesei

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