Inhibition of metal ions on Cerrena sp. laccase: Kinetic, decolorization and fluorescence studies

Xu, Xinqi; Huang, Xinhua; Liú, Dan; Lin, Juan; Ye, Xiuyun; Yang, Jie

doi:10.1016/j.jtice.2017.12.028

Cited by 20 publications

(9 citation statements)

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“…A similar observation was made for laccase from P. ferulae (Ding, et al, 2014) while More et al (2011) reported that the activity of laccase from Pleurotus sp was notably inhibited by metal ions. In contrast to P. tuber-regium laccase, the activity of laccase from other species has been reported to be inhibited by Hg 2+ in previous studies (Bagewadi et al, 2017;Mtibaa et al, 2018;Xu et al, 2018) in addition to K + and Na + ions (Lu et al, 2012;Atalla et al, 2013). This suggests that P. tuber-regium laccase has desirable qualities for industrial applications.…”

Section: Discussionmentioning

confidence: 89%

“…In comparison to other fungal laccases, laccases from Sclerotium rolfsii and Pleurotus sp were reported to have a K m of 0.087 and 250 mM, respectively, using ABTS as a substrate (Ryan et al, 2003;More et al, 2011). Like most industrial effluents, textile dye wastewater usually contains high amounts of different metal ions (Lu et al, 2012;Mtibaa et al, 2018), and laccases, in real bioremediation applications, are inactivated in the presence of these metals (Xu et al, 2018). Therefore, enzymes used for biodegradation of toxic industrial effluents are desired to function effectively in the presence of various metal ions.…”

Section: Discussionmentioning

confidence: 99%

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Purification and characterization of laccase from Pleurotus tuber-regium and its application in dye decolourization

Bamigboye¹,

Oloke²,

Olaogun³

et al. 2019

bta

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Pleurotus tuber-regium is a unique sclerotium-forming white rot fungus. It is edible and has medicinal value and a high potentials of application in various industries. However, to date, there is no information on the production of laccase by this fungus, the purification and determination of decolourization potential of laccase have also not been reported. In this study, purification of laccase from P. tuber-regium is demonstrated for the first time. Laccase was purified from the submerged culture of P. tuber-regium using ammonium sulfate precipitation, ion-exchange chromatography and gel filtration chromatography. The molecular weight of laccase was determined using sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified laccase was characterized to determine its optimum pH and temperature, substrate specificity, Michaelis-Menten constant, and inhibitors. The decolourization potential of the crude laccase was evaluated using Congo red, trypan blue, textile dyes and textile effluent. The purified laccase had a molecular weight of 52 kDa, optimum pH and temperature were 4 and 60EC, respectively. The best substrate for laccase was found to be 2,2N-azino-bis (3-ethylbenzothiazoline-6-sulfonate), with a Michaelis-Menten constant (K m ) of 7.82 μM. Laccase activity was mildly inhibited by ethylenediamine tetraacetic acid (EDTA) and L-cysteine, but strongly inhibited by sodium azide. The activity of the purified laccase was enhanced by more than two fold by Na + , Ca 2+ and Ba 2+ , and slightly enhanced by Hg 2+ and Mn 2+ . The crude laccase was able to efficiently decolourize trypan blue and Congo red dyes and red and blue textile dyes. Notably, on solid agar, trypan blue was completely degraded by intracellular laccase.

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Purification and characterization of laccase from Pleurotus tuber-regium and its application in dye decolourization

Bamigboye¹,

Oloke²,

Olaogun³

et al. 2019

bta

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“…On the other hand, the optimal reacting temperature of Lac2 was higher than that of Lac7. Hg 2+ , Fe 2+ , and Ce 3+ inhibit activity of both CGMCC 5.1011 Lac2 and HYB07 Lac7; however, Pb 2+ and Li + did not suppress Lac2 activity as they do to Lac7 (Xu et al 2018 ; Yang et al 2014 ). Lac2 was more tolerant of organic solvents compared with a thermo-active and thermostable laccase, Lac37 II, from Trametes trogii .…”

Section: Discussionmentioning

confidence: 99%

A highly thermotolerant laccase produced by Cerrena unicolor strain CGMCC 5.1011 for complete and stable malachite green decolorization

et al. 2020

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Laccases are a class of multi-copper oxidases with important industrial values. A thermotolerant laccase produced by a basidiomycete fungal strain Cerrena unicolor CGMCC 5.1011 was studied. With glycerin and peptone as the carbon and nitrogen sources, respectively, a maximal laccase activity of 121.7 U/mL was attained after cultivation in the shaking flask for 15 days. Transcriptomics analysis revealed an expressed laccase gene family of 12 members in C. unicolor strain CGMCC 5.1011, and the gene and cDNA sequences were cloned. A glycosylated laccase was purified from the fermentation broth of Cerrena unicolor CGMCC 5.1011 and corresponded to Lac2 based on MALDI-TOF MS/MS identification. Lac2 was stable at pH 5.0 and above, and was resistant to organic solvents. Lac2 displayed remarkable thermostability, with half-life time of 1.67 h at 70 ºC. Consistently, Lac2 was able to completely decolorize malachite green (MG) at high temperatures, whereas Lac7 from Cerrena sp. HYB07 resulted in accumulation of colored MG transformation intermediates. Molecular dynamics simulation of Lac2 was conducted, and possible mechanisms underlying Lac2 thermostability were discussed. The robustness of C. unicolor CGMCC 5.1011 laccase would not only be useful for industrial applications, but also provide a template for future work to develop thermostable laccases.

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“…reversibly. Hg + was shown to reduce pH and thermal stability, and dynamic simulation showed the presence of binding sites for Hg close to copper binding sites on the laccase molecule [43]. For T. mangrovei, the effect of metal ions was analysed at 1 mM, and only Fe 2+ showed a complete inactivation of its activity, whereas Cu 2+ was not tested [29].…”

Section: Discussionmentioning

confidence: 99%

Enzyme Properties of a Laccase Obtained from the Transcriptome of the Marine-Derived Fungus Stemphylium lucomagnoense

Ali

Ayed

Turbé-Doan

et al. 2020

IJMS

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Only a few studies have examined how marine-derived fungi and their enzymes adapt to salinity and plant biomass degradation. This work concerns the production and characterisation of an oxidative enzyme identified from the transcriptome of marine-derived fungus Stemphylium lucomagnoense. The laccase-encoding gene SlLac2 from S. lucomagnoense was cloned for heterologous expression in Aspergillus niger D15#26 for protein production in the extracellular medium of around 30 mg L−1. The extracellular recombinant enzyme SlLac2 was successfully produced and purified in three steps protocol: ultrafiltration, anion-exchange chromatography, and size exclusion chromatography, with a final recovery yield of 24%. SlLac2 was characterised by physicochemical properties, kinetic parameters, and ability to oxidise diverse phenolic substrates. We also studied its activity in the presence and absence of sea salt. The molecular mass of SlLac2 was about 75 kDa, consistent with that of most ascomycete fungal laccases. With syringaldazine as substrate, SlLac2 showed an optimal activity at pH 6 and retained nearly 100% of its activity when incubated at 50°C for 180 min. SlLac2 exhibited more than 50% of its activity with 5% wt/vol of sea salt.

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Inhibition of metal ions on Cerrena sp. laccase: Kinetic, decolorization and fluorescence studies

Cited by 20 publications

References 47 publications

Purification and characterization of laccase from Pleurotus tuber-regium and its application in dye decolourization

Purification and characterization of laccase from Pleurotus tuber-regium and its application in dye decolourization

A highly thermotolerant laccase produced by Cerrena unicolor strain CGMCC 5.1011 for complete and stable malachite green decolorization

Enzyme Properties of a Laccase Obtained from the Transcriptome of the Marine-Derived Fungus Stemphylium lucomagnoense

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