Copper induction and differential expression of laccase in Aspergillus flavus

Gomaa, Ola M.; Momtaz, Osama A.

doi:10.1590/s1517-838246120120118

Cited by 33 publications

(17 citation statements)

References 38 publications

(54 reference statements)

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“…After cultivating N. pironii IM 6443 in media containing these additives for 96 and 72 h, the enzyme activity reached 1,412 and 1,405 U/L, respectively, and was almost five fold higher than in the control sample cultivated in Sabuoraud medium. Copper has been reported to be a strong inducer of laccase in many fungal species, including Aspergillus flavus [43], M. roridum [44], and Peniophora sp. [45].…”

Section: Optimization Of the Laccase Productionmentioning

confidence: 99%

Laccase activity of the ascomycete fungus Nectriella pironii and innovative strategies for its production on leaf litter of an urban park

et al. 2020

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A laccase-producing ascomycete fungus was isolated from soil collected around the premises of a textile dye factory and identified as Nectriella pironii. Efficient laccase production was achieved via the synergistic action of 1 mM copper sulfate and ferulic acid. Extracts of rapeseed oil cake, grass hay, and leaf litter collected in a pocket urban park were used for enzyme production. The highest laccase activity (3,330 U/L) was observed in the culture grown on the leaf litter extract. This is the first report on biosynthesis of laccase by N. pironii. This is also the first study on utilization of naturally fallen park leaves as a substrate for fungal laccase production. The extracellular enzyme possessing laccase activity was purified to homogeneity by ion-exchange and gel filtration chromatographic techniques. The amino acid sequence of the protein revealed highest similarity to the laccase enzyme produced by Stachybotrys chartarum-and considerable homology to those produced by other fungal species. The purified laccase possessed a molecular mass of 50 kDa. The enzyme had an optimum pH of 2.0 or 6.0 and retained more than 50% of residual activity after 3 hours of incubation at pH 3.0-10.6 or 4.0-9.0 when 2,2 0-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid or 2,6-dimethoxyphenol, respectively, were used. Dithiothreitol, β-mercaptoethanol, and sodium azide at 1 mM concentration strongly inhibited the laccase activity, while in the presence of 50 mM urea, the enzyme was found to retain 25% of its activity. The laccase was able to decolorize more than 80% of Indigo Carmine, Remazol Brilliant Blue R, Reactive Orange 16, and Acid Red 27 dyes within 1 h. The possibility of leaf litter use for the production of the laccase enzyme from N. pironii (IM 6443), exhibiting high pH stability and degradative potential, makes it a promising tool for use in different environmental and industrial operations.

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Section: Optimization Of the Laccase Productionmentioning

confidence: 99%

Laccase activity of the ascomycete fungus Nectriella pironii and innovative strategies for its production on leaf litter of an urban park

et al. 2020

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“…Enhanced laccase activity in presence of CuSO 4 is due to the fact that copper acts as a strong inducer of laccase in white-rot fungi. Laccases belong to the group of blue copper oxidases, and are the most abundant members of the multicopper protein family (Gomaa and Momtaz 2015). Isolation of laccase producing Aspergillus sp.…”

Section: Discussionmentioning

confidence: 99%

Statistical optimization for enhanced production of extracellular laccase from Aspergillus sp. HB_RZ4 isolated from bark scrapping

Bhamare

Jadhav

Sayyed

2018

Environmental Sustainability

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Laccase enzyme has gained tremendous demand in various industries, waste water treatment, bioremediation and nanobiotechnology. This compels the availability of enzyme in greater yields that can be achieved by employing potential laccase producing cultures and statistical optimization. Use of Plackett-Burman design (PBD) that evaluates various medium components and having two level factorial design help to determine the factor and its level to increase the yield of product. Present paper reports the screening of laccase producting fungus identified as Aspergillus sp. by 18S rDNA of internal transcribed spacer regions and the large subunit. Aspergillus sp. HB_RZ4 isolated from tree bark scrapping showed enhanced production of laccase in minimal medium by applying two-stage statistical approach, as PBD and Response Surface Methodology using central composite design (CCD). In the first stage of optimization, out of 8 variables of minimal medium, glucose, yeast extract, CuSO 4 and temperature were found as significant components that influenced laccase production. Aspergillus sp. HB_RZ4 produced highest amount (7.27 Uml −1 ) of extracellular laccase. Further optimization using CCD revealed that 34 °C temperature, 2.1 gL −1 of glucose (carbon source), 2.5 gL −1 of yeast extract (nitrogen source) and 0.0025 gLCuSO 4 (inducer) were the optimum values that yielded maximum laccase. The optimization by PBD statistical design studies revealed optimum laccase yield with conditions being; pH, 6.0; temperature, 34 °C; incubation, 9 days; glucose, 2.1 gL −1 ; yeast extract, 2.5 gL −1 and CuSO 4 ., 0.0025 gL −1 .

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“…Genes encoding laccase enzymes have been studied in different filamentous fungi like Aspergillus niger, A. oryzae and Trichoderma reesei (Hoffmeister and Keller, 2007;Gomaa and Momtaz, 2015). Fungal species belong to Ascomycota have different laccase encoding genes which are involved in the oxidization of syringaldazine dye (Dedeyan et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Biochemical and Molecular Analysis of Laccase Enzyme in Saprobic Fungus; Sordaria fimicola

Ishfaq¹,

Mahmood²,

Nasir³

et al. 2017

IJAB

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To cite this paper: Ishfaq, M., N. Mahmood, I.A. Nasir and M. Saleem, 2017 AbstractSaprobic fungi play an important role in decomposition and thus contributing to the global carbon cycle. Sordaria fimicola strains collected from diverse environment were evaluated for their laccase enzyme activity, while Aspergillus niger was used as control fungus. In laccase assay, S. fimicola strain N6 collected from the station 6 located at the Northern Facing Slope (NFS) of the Evolution Canyon 1 (EC 1), showed the maximum laccase enzyme activity (1

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Copper induction and differential expression of laccase in Aspergillus flavus

Cited by 33 publications

References 38 publications

Laccase activity of the ascomycete fungus Nectriella pironii and innovative strategies for its production on leaf litter of an urban park

Laccase activity of the ascomycete fungus Nectriella pironii and innovative strategies for its production on leaf litter of an urban park

Statistical optimization for enhanced production of extracellular laccase from Aspergillus sp. HB_RZ4 isolated from bark scrapping

Biochemical and Molecular Analysis of Laccase Enzyme in Saprobic Fungus; Sordaria fimicola

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