Ligninases production by Basidiomycetes strains on lignocellulosic agricultural residues and their application in the decolorization of synthetic dyes

Gomes, Eleni; Aguiar, Ana Paula; Carvalho, Carlos Alberto Machado; Bonfá, Maricy Raquel B.; Silva, Roberto da; Boscolo, Maurício

doi:10.1590/s1517-83822009000100005

Cited by 80 publications

(55 citation statements)

References 33 publications

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“…Basidiomycetes fungi are the most efficient lignin-degrading organisms that produce mainly laccases, manganese peroxidase, and lignin peroxidase [9]. These enzymes present a non-specific biocatalyst mechanism and have been used for bioremediation process due to their ability to degrade azo, heterocyclic, reactive and polymeric dyes [1,6].…”

Section: Resultsmentioning

confidence: 99%

“…The optimum temperature obtained for laccase production by mutant and hybrid strains of P. pulmonarius is 30 O C whereas Okamoto et al [17] reported 50℃ as active optimum temperature for laccase production from P. ostreatus. Gomes et al [9] reported the optimum temperature for laccase production by the following organisms; Lentinus strigellus (55-60℃), Picnoporus sanguineus (60-70℃), Phenllinus rimosus (60℃). The optimum pH for laccase enzyme for mutant strain of P. pulmonarius is pH 5, due to highest yield of laccase enzyme obtained at pH 5 for mutant strain (Figure 3).…”

Section: Figure 1 Laccase Activity Of Wild and Mutant Strains Of Plementioning

confidence: 99%

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Improvement of Laccase Production in Pluerotus pulmonarius-LAU 09 by Mutation

Adebayo¹,

Kola²,

Yadav³

et al. 2012

MICROBIOLOGY

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The strain improvement of P. pulmonarius LAU 09 for laccase production was carried out by UV-light exposure at 210nm (UV-sterilizer, Millipore xx63 70000) for 90minutes. The highest laccase activity of 2.5 Uml-1 was produced by LAU 90 (mutant) in comparison with obtained yield by wild type LAU 09 (1.75 Uml-1). The optimal physiological parameters for optimum laccase production by LAU 90 are 30OC of temperature, pH of 5.0 and incubation of 168hours. The mutant strain gave the highest total enzyme activity and enzyme specific activity of 71.7 x 10-4 mol/min and 89.63X 10-4 IU/mg of purified laccase enzyme respectively, with molecular weight of 97KDa. The activity of the purified enzyme was strongly inhibited by Sodium azide and EDTA at 1ml/0.1mM and 0.5ml/100mM respectively. The result obtained shown an improved performance of the mutant (LAU 90) strain of P. pulmonarius in laccase production over the wild (LAU 09) type.

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Section: Resultsmentioning

confidence: 99%

Section: Figure 1 Laccase Activity Of Wild and Mutant Strains Of Plementioning

confidence: 99%

Improvement of Laccase Production in Pluerotus pulmonarius-LAU 09 by Mutation

Adebayo¹,

Kola²,

Yadav³

et al. 2012

MICROBIOLOGY

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“…Supplementation of nitrogen in rice straw increased the production of laccase 3-4 times in lignocellulolytic fungus (9).…”

Section: Lignocellulolytic Enzyme Production Of P Ostreatusmentioning

confidence: 98%

Lignocellulolytic enzyme production of Pleurotus ostreatus growth in agroindustrial wastes

Luz¹,

Nunes²,

Paes³

et al. 2012

Braz. J. Microbiol.

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The mushroom Pleurotus ostreatus has nutritional and medicinal characteristics that depend on the growth substrate. In nature, this fungus grows on dead wood, but it can be artificially cultivated on agricultural wastes (coffee husks, eucalyptus sawdust, corncobs and sugar cane bagasse). The degradation of agricultural wastes involves some enzyme complexes made up of oxidative (laccase, manganese peroxidase and lignin peroxidase) and hydrolytic enzymes (cellulases, xylanases and tanases). Understanding how these enzymes work will help to improve the productivity of mushroom cultures and decrease the potential pollution that can be caused by inadequate discharge of the agroindustrial residues. The objective of this work was to assess the activity of the lignocellulolytic enzymes produced by two P. ostreatus strains (PLO 2 and PLO 6). These strains were used to inoculate samples of coffee husks, eucalyptus sawdust or eucalyptus bark add with or without 20 % rice bran. Every five days after substrate inoculation, the enzyme activity and soluble protein concentration were evaluated. The maximum activity of oxidative enzymes was observed at day 10 after inoculation, and the activity of the hydrolytic enzymes increased during the entire period of the experiment. The results show that substrate composition and colonization time influenced the activity of the lignocellulolytic enzymes.

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“…The lignocellulolytic enzymes include lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase (Lac), which are involved in lignin degradation (Gomes et al 2009). Also included are hydrolytic enzymes, cellulases, and hemicellulases (Membrillo et al 2008;Isikhuemhen and Mikiashvilli 2009), which are involved in cellulose and hemicellulose degradation, respectively.…”

Section: Introductionmentioning

confidence: 99%

Sequential Solid-State and Submerged Cultivation of the White Rot Fungus Pleurotus ostreatus on Biomass and the Activity of Lignocellulolytic Enzymes

An¹,

Wu²,

Han³

et al. 2016

BioResources

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Sequential solid-state and submerged cultivation with various lignocellulosic biomasses as a substrate for lignocellulolytic enzyme production by Pleurotus ostreatus were assessed by measuring endoglucanase, xylanase, and laccase activities. An unconventional preculture method was established by cultivating the P. ostreatus mycelia in a solid substrate medium for an initial fungal growth phase, followed by a transition to submerged fermentation through adding a liquid culture medium. The lignocellulolytic enzymes of P. ostreatus in different fermentation methods revealed wide differences. The higher yields of endoglucanase (3152 ± 139 U/L), xylanase (3064 ± 40 U/L), and laccase (543 ± 21 U/L) were achieved by using the sequential solid-state submerged method compared to conventional solid-state and submerged cultivation. Generally speaking, sequential solid-state and submerged fermentation of cottonseed hull is favorable for laccase secretion, whereas sequential solid-state and submerged fermentation of corncob provides better production of hydrolytic enzymes. These results revealed that the nature of the lignocellulosic biomass and the fermentation method play an important role in the expression of lignocellulolytic enzymes. This indication would be helpful in optimizing the production of integrated industrial lignocellulolytic enzymes.

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Ligninases production by Basidiomycetes strains on lignocellulosic agricultural residues and their application in the decolorization of synthetic dyes

Cited by 80 publications

References 33 publications

Improvement of Laccase Production in Pluerotus pulmonarius-LAU 09 by Mutation

Improvement of Laccase Production in Pluerotus pulmonarius-LAU 09 by Mutation

Lignocellulolytic enzyme production of Pleurotus ostreatus growth in agroindustrial wastes

Sequential Solid-State and Submerged Cultivation of the White Rot Fungus Pleurotus ostreatus on Biomass and the Activity of Lignocellulolytic Enzymes

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