Selective Induction, Purification and Characterization of a Laccase Isozyme from the Basidiomycete Trametes sp. AH28-2

Xiao, Yazhong; Chen, Q.; Hang, J.; Shi, Yongpeng; Wu, J.; Hong, Y. Z.; Wang, Y. P.

doi:10.2307/3761984

Cited by 47 publications

(31 citation statements)

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“…pubescens growth. This suggests a synergistic effect of Lac1 and Lac2, as have been reported for laccases obtained from Trametes and Pleurotus strains [17,52,53]. …”

Section: Discussionsupporting

confidence: 74%

Production of Trametes pubescens Laccase under Submerged and Semi-Solid Culture Conditions on Agro-Industrial Wastes

et al. 2013

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Laccases are copper-containing enzymes involved in the degradation of lignocellulosic materials and used in the treatment of phenol-containing wastewater. In this study we investigated the effect of culture conditions, i.e. submerged or semi-solid, and copper supplementation on laccase production by Trametes pubescens grown on coffee husk, soybean pod husk, or cedar sawdust. The highest specific laccase activity was achieved when the culture was conducted under submerged conditions supplemented with copper (5 mM), and using coffee husk as substrate. The crude extracts presented two laccase isoforms with molecular mass of 120 (Lac1) and 60 kDa (Lac2). Regardless of the substrate, enzymatic crude extract and purified fractions behaved similarly at different temperatures and pHs, most of them presented the maximum activity at 55 °C and a pH range between 2 and 3. In addition, they showed similar stability and electro-chemical properties. At optimal culture conditions laccase activity was 7.69±0.28 U mg-1 of protein for the crude extract, and 0.08±0.001 and 2.86±0.05 U mg-1 of protein for Lac1 and Lac2, respectively. In summary, these results show the potential of coffee husk as an important and economical growth medium to produce laccase, offering a new alternative use for this common agro-industrial byproduct.

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“…pubescens growth. This suggests a synergistic effect of Lac1 and Lac2, as have been reported for laccases obtained from Trametes and Pleurotus strains [17,52,53]. …”

Section: Discussionsupporting

confidence: 74%

Production of Trametes pubescens Laccase under Submerged and Semi-Solid Culture Conditions on Agro-Industrial Wastes

et al. 2013

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“…Increase in activity does not seem to be caused by specific structure/ substituent group. Xiao et al (29) reported that compounds with different chemical structures affect composition of laccase isozymes in Trametes sp. AH28–2.…”

Section: Discussionmentioning

confidence: 99%

“…They are members of the multicopper protein family that has developed from small sized prokaryotic azurins to eukaryotic ceruloplasmin. Laccases are widely distributed in plants and fungi (4), where their involvement in melanin formation and in a variety of different, and sometimes contradictory, physiological functions like fungal morphogenesis, plant pathogenesis and fungal virulence has been frequently proposed (29). They also occur in prokaryotes e.g.…”

Section: Introductionmentioning

confidence: 99%

“…Filazzola et al (10) reported the influence of xenobiotics on catalytic activity of constitutive forms of laccases. Metal ions and several organic molecules have also been assayed for their ability to enhance activity of inducible form of laccases (25,29). Gallic and ferulic acids were used, mainly because of their structural analogy with lignin model compounds (11).…”

Section: Introductionmentioning

confidence: 99%

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Xenobiotics enhance laccase activity in alkali-tolerant γ-proteobacterium JB

Singh

Batish

Sharma

et al. 2009

Braz. J. Microbiol.

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Various genotoxic textile dyes, xenobiotics, substrates (10 µM) and agrochemicals (100 µg/ml) were tested for enhancement of alkalophilic laccase activity in γ-proteobacterium JB. Neutral Red, Indigo Carmine, Naphthol Base Bordears and Sulphast Ruby dyes increased the activity by 3.7, 2.7, 2.6 and 2.3 fold respectively. Xenobiotics/substrates like p-toluidine, 8-hydroxyquinoline and anthracine increased it by 3.4, 2.8 and 2.3 fold respectively. Atrazine and trycyclozole pesticides enhanced the activity by 1.95 and 1.5 fold respectively.

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“…Laccases (EC 1.10.3.2, p -diphenol: oxygen oxidoreductase) are blue copper-containing oxidases, catalyzing the oxidation of ortho - and para - diphenols, polyphenols, arylamines, aminophenols, and some inorganic ions, while simultaneously reducing molecular dioxygen to water [50, 51, 53]. Laccases are classified into two groups depending on their source: plant and fungal.…”

Section: Introductionmentioning

confidence: 99%

Chemical Modifications of Laccase from White-Rot Basidiomycete Cerrena unicolor

Kucharzyk

Janusz

Karczmarczyk

et al. 2012

Appl Biochem Biotechnol

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Laccases belong to the group of phenol oxidizes and constitute one of the most promising classes of enzymes for future use in various fields. For industrial and biotechnological purposes, laccases were among the first enzymes providing larger-scale applications such as removal of polyphenols or conversion of toxic compounds. The wood-degrading basidiomycete Cerrena unicolor C-139, reported in this study, is one of the high-laccase producers. In order to facilitate novel and more efficient biocatalytic process applications, there is a need for laccases with improved biochemical properties, such as thermostability or stability in broad ranges of pH. In this work, modifications of laccase isoforms by hydrophobization, hydrophilization, and polymerization were performed. The hydrophobized and hydrophilized enzyme showed enhanced surface activity and higher ranges of pH and temperatures in comparison to its native form. However, performed modifications did not appear to noticeably alter enzyme’s native structure possibly due to the formation of coating by particles of saccharides around the molecule. Additionally, surface charge of modified laccase shifted towards the negative charge for the hydrophobized laccase forms. In all tested modifications, the size exclusion method led to average 80 % inhibition removal for hydrophilized samples after an hour of incubation with fluoride ions. Samples that were hydrophilized with lactose and cellobiose showed an additional 90 % reversibility of inhibition by fluoride ions after an hour of concluding the reaction and 40 % after 24 h. The hydrophobized laccase showed higher level of the reversibility after 1 h (above 80 %) and 24 h (above 70 %) incubation with fluoride ions. The addition of ascorbate to laccase solution before a fluoride spike resulted in more efficient reversibility of fluoride inhibitory effect in comparison to the treatments with reagents used in the reversed sequence.

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Selective Induction, Purification and Characterization of a Laccase Isozyme from the Basidiomycete Trametes sp. AH28-2

Cited by 47 publications

References 0 publications

Production of Trametes pubescens Laccase under Submerged and Semi-Solid Culture Conditions on Agro-Industrial Wastes

Production of Trametes pubescens Laccase under Submerged and Semi-Solid Culture Conditions on Agro-Industrial Wastes

Xenobiotics enhance laccase activity in alkali-tolerant γ-proteobacterium JB

Chemical Modifications of Laccase from White-Rot Basidiomycete Cerrena unicolor

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