Properties of bacterial laccases and their application in bioremediation of industrial wastes

Chandra, Ram; Chowdhary, Pankaj

doi:10.1039/c4em00627e

Cited by 192 publications

(121 citation statements)

References 136 publications

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“…Various oxidases are being tested for the action on lignin aiming at deriving added value chemicals [36,37]. Heterogeneity of lignin is a major obstacle for detailed study of the enzyme activity and model compounds are used instead.…”

Section: Discussionmentioning

confidence: 99%

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Lončar

Božić

Vujčić

2016

Journal of Molecular Catalysis B: Enzymatic

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Please cite this article as: Nikola Lončar, Nataša Božić, Zoran Vujčić, Expression and characterization of a thermostable organic solevent-tolerant laccase from Bacillus licheniformis ATCC 9945a, Journal of Molecular Catalysis B: Enzymatic http://dx.Abstract Highlights  Bacillus licheniformis 9945a laccase is overexpressed in E. coli with yield 50 mg/L.  Temperature optimum of laccase is 90⁰C and pH optimum is 7.0. Enzyme is thermostable with a melting temperature of 79⁰C at pH 7.0. Presence of organic solvents reduces melting temperature but activity remains impaired. Lignin model compounds are dimerized after one electron oxidation of phenolic group. AbstractBacterial laccases have proven advantages over fungal and plant counterparts in terms of wider pH optimum, higher stability and broader biocatalytic scope. In this work, Bacillus licheniformis ATCC 9945a laccase is produced heterologously in Escherichia coli. Produced laccase exhibits remarkably high temperature optimum at 90⁰C and possess significant thermostability and resistance to inactivation by organic solvents. Laccase has an apparent melting temperature of 79⁰C at pH 7.0 and above 70⁰C in range of pH 5.0-8.0, while having half-life of 50 min at 70⁰C. Presence of 10% organic solvents such as acetonitrile, dimethylformamide, dimethylsulfoxide or methanol reduces melting temperature to 45-52ᴼC but activity remains practically unimpaired. With 50% of acetonitrile and methanol laccase retained 3 ~40% of initial activity. EDTA and 300 mM sodium-chloride have positive effect on activity.Enzyme is active on syringaldazine, ABTS, phenols, amines, naphthol, lignin and lignin model compounds and mediates C-C bond formation via oxidative coupling after one electron oxidation of phenolic group. Successful polymerization of 2-naphthol was achieved with 77% conversion of 250 mg/L 2-naphtol in only 15 min which may further expand substrate scope of this enzyme towards polymer production and/or xenobiotics removal for environmental applications.

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Section: Discussionmentioning

confidence: 99%

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Lončar

Božić

Vujčić

2016

Journal of Molecular Catalysis B: Enzymatic

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“…Fungal laccases are used in the decolorization and detoxifications of effluents discharged from industries (Chandra and Chowdhary 2015) like food, textile, pulp/ paper, and plastic (Viswanath et al 2014) which pollute water due to the release of colored effluents and by the Fig. 4 List of advantages associated with the usage of bio-fuel cell over conventional fuel cell formation of carcinogenic intermediates such as aromatic amines from azo dyes (Mahmoodi et al 2009).…”

Section: Bioremediation Of the Environment And Detoxification Of Efflmentioning

confidence: 99%

Fungal laccase discovered but yet undiscovered

Agrawal

Chaturvedi

Verma

2018

Bioresour. Bioprocess.

180

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Laccases belongs to multinuclear copper-containing oxidase and can act on a variety of aromatic and non-aromatic compounds. Due to their broad substrate specificity, they are considered as a promising candidate in various industrial and biotechnological sectors. They are regarded as a "Green Tool"/"Green Catalyst" in biotechnology. The present review focuses on structure, reaction mechanism, categories, applications, economic feasibility, limitations, and future prospects of fungal laccases. Thus, this review would help in understanding laccases along with the areas, which has not been focused and requires attention. Since past, immense work has been carried out on laccases: yet, new discoveries and application are ever increasing which includes bio-fuel, bio-sensor, fiber board synthesis, bioremediation, clinical, textile industry, food, cosmetics, and many more. Hence, it can be stated that fungal laccase is an enzyme which is "discovered but yet undiscovered".

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“…These enzymes (EC 1.10.3.2) are multicopper-containing oxidases catalyzing monoelectronic oxidation of diverse substrates by reducing oxygen to water (Riva, 2006;Giardina et al, 2010;Chandra and Chowdhary, 2015;Wang et al, 2015). Owing to their broad substrate spectrum in biodegradation ability, laccases became desired biocatalysts in many industrial processes including diagnosis and bioremediation approaches and the detoxification of industrial effluents of paper, pulp, textile, and petrochemical industries.…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression and characterization of a high redox potential laccase from Coriolopsis polyzona MUCL 38443

Pinar¹,

Tamerler²,

Karataş³

2017

Turk J Biol

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In this study, a novel laccase gene, named as Cplcc1, and its corresponding cDNA were isolated and characterized from the Coriolopsis polyzona MUCL 38443 strain. The Cplcc1 gene consists of a 1563-bp open reading frame encoding a protein of 520 amino acids with a 20-residue putative signal peptide. The size of the Cplcc1 gene is 2106 bp and it contains ten introns and five potential N-glycosylation sites. Additionally, the isolated full-length Cplcc1 cDNA was successfully expressed in Pichia pastoris. The heterologous expression conditions were also optimized and the highest activity value increased to 800 U L -1 with 1.5% methanol, 0.8 mM CuSO 4 , and 0.6% L-alanine supplementation. The recombinant laccase was partially purified and the molecular weight was found as approximately 54 kDa. The maximum oxidation activity was observed for 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) at pH 3.0. The optimal temperature was found as 70 °C. On the other hand, at 30 °C, the enzyme was stable for more than a week and its half-life was longer than 8 h. The K m , V max , k cat , and k cat K m -1 values of the recombinant laccase were identified as 0.137 mM, 288.6 µmol min -1 L -1 , 5.73 × 10 5 min -1 , and 4.18 × 10 6 min -1 mM -1 , respectively. Sodium azide, L-cysteine, and SDS were found as usual inhibitors.

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Properties of bacterial laccases and their application in bioremediation of industrial wastes

Cited by 192 publications

References 136 publications

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Expression and characterization of a thermostable organic solvent-tolerant laccase from Bacillus licheniformis ATCC 9945a

Fungal laccase discovered but yet undiscovered

Heterologous expression and characterization of a high redox potential laccase from Coriolopsis polyzona MUCL 38443

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