Biochemical characterization of an extremely stable pH-versatile laccase from Sporothrix carnis CPF-05

Olajuyigbe, Folasade M.; Fatokun, Cornelius O.

doi:10.1016/j.ijbiomac.2016.10.037

Cited by 44 publications

(29 citation statements)

References 42 publications

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“…In addition, methanol at concentrations ranging from 1 to 5% (v/v) slightly lowered activity by 11.7-16.3%, and 10% ethanol (v/v) led to a 56.1% loss of activity. Similarly, the catalytic activity of laccase in S. carnis CPF-05 was almost lost when 10% of the organic solvents added (Olajuyigbe and Fatokun, 2017). In addition, the solvent tolerance of the enzyme is considered to be positively correlated with the thermal stability, which is also in line with the thermoactive and solvent tolerance of Lac 37 II in this study (Rasekh et al, 2014).…”

Section: Effect Of Organic Solvents On Activity Of Lac 37 IIsupporting

confidence: 74%

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

Yang

et al. 2020

Front. Microbiol.

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A thermo-activation and thermostable laccase isoenzyme (Lac 37 II) produced by Trametes trogii S0301 at 37 • C was purified to apparent homogeneity by anionic exchange chromatography and sephadex G-75 chromatography, with 12.3% of yeiled and a specific activity of 343.1 U mg −1 . The molecular weight of the purified Lac 37 II was estimated to be approximately 56 kDa in 12% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH and temperature for the protein was 2.7 and 60 • C, respectively. The purified Lac 37 II showed higher resistance to all tested metal ions and organic solvents except for Fe 2+ and Cd 2+ at 37 • C and the activity of the purified Lac 37 was significantly enhanced by Cu 2+ at 50 mM. The K cat , K m , and K cat /K m of Lac 37 II were 2.977 s −1 , 16.1 µM, and 184.9 s −1 µM −1 , respecively, in the condition of pH 2.7 and 60 • C using ABTS as a substrate. Peptide-mass fingerprinting analysis showed that the Lac 37 II matched to the gene-deduced sequences of lcc3 in T. trogii BAFC 463, other than Lcc1, Lcc 2, and Lcc 4. Compared with laccase prepared at 28 • C, the onset of thermo-activation of Lac 37 II activity occurred at 30 • C with an increase of 10%, and reached its maximum at the temperatures range of 40-60 • C with an increase of about 40% of their original activity. Furthermore, Lac 37 II showed the efficient decolorization ability toward triphenylmethane dyes at 60 • C, with decolorization rates of 100 and 99.1% for 25 mg L −1 malachite and crystal violet in 5 h, respectively, when hydroxybenzotriazole (HBT) was used as a mediator. In conclusion, it is the first time to report a thermoactivation laccase from a thermophilic T. trogii strain, which has a better enzyme property and higher decolorization ability among fungal laccases, and it also has a further application prospective in the field of biotechnology.

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Section: Effect Of Organic Solvents On Activity Of Lac 37 IIsupporting

confidence: 74%

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

Yang

et al. 2020

Front. Microbiol.

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“…An attempt has been made in the present study to express the laccase gene from S.commune in Pichia, whilst lowering application costs, which otherwise is a bottleneck in scaling up and sustainably use laccases for industrial applications. There is a continuous quest for isolating and screening laccase producers with desirable yields and properties [Olajuyigbe and Fatokun, 2017]. Hatomoto et al [1999] expressed S. commune laccase in Aspergillus sajae strain 1860 (with low protease levels) suggesting protein engineering strategies for improved production [Upadhyay et al, 2016].…”

Section: Discussionmentioning

confidence: 99%

Enhanced delignification of lignocellulosic substrates by <i>Pichia</i> GS115 expressed recombinant laccase

Kumar

Kolte

Dhali

et al. 2018

J. Gen. Appl. Microbiol.

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Utilization of energy-rich crop residues by ruminants is restricted by the presence of lignin, which is recalcitrant to digestion. Application of lignin degrading enzymes on the lignocellulosic biomass exposes the cellulose for easy digestion by ruminants. Laccases have been found to be considerably effective in improving the digestibility by way of delignification. However, laccase yields from natural hosts are not sufficient for industrial scale applications, which restricts their use. A viable option would be to express the laccase gene in compatible hosts to achieve higher production yields. A codon-optimized synthetic variant of Schizophyllum commune laccase gene was cloned into a pPIC9K vector and expressed in P. pastoris GS115 (his4) under the control of an alcohol oxidase promoter. Colonies were screened for G418 resistance and the methanol utilization phenotype was established. The transformant yielded a laccase activity of 344 U . mL -1 after 5 days of growth at 30 0 C (0.019 g . mL -1 wet cell weight). The laccase protein produced by the recombinant Pichia clone was detected as two bands with apparent molecular weights of 55 kDa and 70 kDa on SDS-PAGE. Activity staining on native PAGE confirmed the presence of bioactive laccase. Treatment of five common crop residues with recombinant laccase recorded a lignin loss ranging between 1.64% in sorghum stover, to 4.83% in finger millet, with an enhancement in digestibility ranging between 8.71% in maize straw to 24.61% in finger millet straw.Treatment with recombinant laccase was effective in enhancing the digestibility of lignocellulosic biomass for ruminant feeding through delignification. To date, a number of hosts have been adventured to produce laccase in large quantities, but, to our knowledge, there are no reports of the expression of laccase protein from Schizophyllum commune in Pichia pastoris, and also on the treatment of crop residues using recombinant laccase for ruminant feeding.

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“…Efforts are still being made to screen naturally-occurring laccase producers with desired laccase yields and properties (Chen et al, 2012; Si et al, 2013; Fang Z. et al, 2015; Iracheta-Cárdenas et al, 2016; Kandasamy et al, 2016; Olajuyigbe and Fatokun, 2017). Laccase yields are variable depending on the species and strain, but most naturally-occurring species appear to be poor laccase producers.…”

Section: Natural Laccase Producersmentioning

confidence: 99%

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

et al. 2017

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Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence, biochemical properties, and expression to immobilization and applications. This review is not intended to be all-encompassing; instead, we highlighted some of the latest developments in basic and applied laccase research with an emphasis on laccase-mediated bioremediation of pharmaceuticals, especially antibiotics. Pharmaceuticals are a broad class of emerging organic contaminants that are recalcitrant and prevalent. The recent surge in the relevant literature justifies a short review on the topic. Since low laccase yields in natural and genetically modified hosts constitute a bottleneck to industrial-scale applications, we also accentuated a genus of laccase-producing white-rot fungi, Cerrena, and included a discussion with regards to regulation of laccase expression.

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Biochemical characterization of an extremely stable pH-versatile laccase from Sporothrix carnis CPF-05

Cited by 44 publications

References 42 publications

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

A Thermo-Active Laccase Isoenzyme From Trametes trogii and Its Potential for Dye Decolorization at High Temperature

Enhanced delignification of lignocellulosic substrates by <i>Pichia</i> GS115 expressed recombinant laccase

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

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