Biocatalytic characterization of free and immobilized laccase from Trametes versicolor in its activation zone

Saoudi, O.; Ghaouar, N.

doi:10.1016/j.ijbiomac.2019.01.199

Cited by 23 publications

(12 citation statements)

References 62 publications

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“…In addition, an industrial white-rot fungus was also found in this study. As a target of interest, Trametes versicolor was conducted under a free or immobilized laccase condition exploring its biocatalytic characterization in the activation zone [102]. Moreover, though these saprophytic species possess powerful enzymes, which can effectively degrade lignocellulose [103], Abundisporus quercicola, Bjerkandera adusta, Ceriporia lacerata, Cerrena zonata, C. albocinnamomea, Daedaleopsis confragosa, Fomes fomentarius and Gyrodontium sacchari are treated as forest pathogens contrarily [104].…”

Section: Discussionmentioning

confidence: 99%

Diversity of Wood-Decaying Fungi in Wuliangshan Area, Yunnan Province, P.R. China

Xiao

Zhao

2022

Diversity

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Five surveys were carried out in the Wuliangshan area, Yunnan Province, P.R. China, based on a combination of morphological features and molecular evidence. Around 2454 specimens of wood-decaying fungi were collected. The paper summarizes the obtained results on the wood-decaying fungi of this area, consisting in 95 species distributed in 59 genera, 23 families and 9 orders. Their hosts and substrates were also identified. A checklist of wood-decaying fungi is given. Sequences of the ITS nrRNA gene region of the studied specimens were generated and phylogenetic analysis was performed with maximum likelihood, maximum parsimony and Bayesian inference methods. The present list of wood-decaying fungi enriches the knowledge of fungal diversity worldwide and supplies the basic data for future applications.

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Section: Discussionmentioning

confidence: 99%

Diversity of Wood-Decaying Fungi in Wuliangshan Area, Yunnan Province, P.R. China

Xiao

Zhao

2022

Diversity

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“…An inhibitor is a compound that alters the catalytic action of an enzyme and thus slows down or stops catalysis. Inhibition studies are conducted to obtain information on the reaction mechanism of the enzyme [103]. Recently, Saoudi and Ghaouar (2019) conducted a study on biocatalytic characterisation of free and immobilised laccase in their activation zones [103].…”

Section: Effect Of Inhibitors On Enzyme Activitymentioning

confidence: 99%

“…Inhibition studies are conducted to obtain information on the reaction mechanism of the enzyme [103]. Recently, Saoudi and Ghaouar (2019) conducted a study on biocatalytic characterisation of free and immobilised laccase in their activation zones [103]. Sodium azide and ethylenediaminetetraacetic (EDTA), citric, sulphamic and oxalic acids were used to investigate inhibition of the laccase enzyme.…”

Section: Effect Of Inhibitors On Enzyme Activitymentioning

confidence: 99%

“…Laccase activity was entirely inhibited by oxalic acid and sulphamic acid at a concentration of 40 mM; however, citric acid and EDTA inhibited enzyme activity at even lower concentrations than the inhibitor concentration reported for oxalic acid and sulphamic acid. The inhibition of the enzyme at different concentrations was dependent on the nature of inhibitor interaction with the enzyme to form copper ion complexes [103].…”

Section: Effect Of Inhibitors On Enzyme Activitymentioning

confidence: 99%

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Overview of Recent Advances in Immobilisation Techniques for Phenol Oxidases in Solution

Ndlovu

Malinga

2020

Catalysts

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Over the past two decades, phenol oxidases, particularly laccases and tyrosinases, have been extensively used for the removal of numerous pollutants in wastewaters due to their broad substrate specificity and their ability to use readily accessible molecular oxygen as the essential cofactor. As for other enzymes, immobilisation of laccases and tyrosinases has been shown to improve the performance and efficiency of the biocatalysts in solution. Several reviews have addressed the enzyme immobilisation techniques and the application of phenol oxidases to decontaminate wastewaters. This paper offers an overview of the recent publications, mainly from 2012 onwards, on the various immobilisation techniques applied to laccases and tyrosinases to induce and/or increase the performance of the biocatalysts. In this paper, the emphasis is on the efficiencies achieved, in terms of structural modifications, stability and resistance to extreme conditions (pH, temperature, inhibitors, etc.), reactivity, reusability, and broad substrate specificity, particularly for application in bioremediation processes. The advantages and disadvantages of several enzyme immobilisation techniques are also discussed. The relevance and effectiveness of the immobilisation techniques with respect to wastewater decontamination are critically assessed. A perspective on the future directions for large-scale application of the phenol oxidases in immobilised forms is provided.

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“…Although laccases are highly active catalysts, they are not always useful for biotechnological applications because of their low stability. This can be increased through the immobilization of the enzyme on solid supports [1,3]. Enzyme-nanoparticles conjugates designed as industrial biocatalysts are poised to revolutionize many technological processes through ground-breaking new properties and applications.…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis, purification, characterization and immobilization of laccase from Lithothelium sp.

Radveikienė¹,

Pilotaitė²,

Dainytė³

et al. 2020

chemija

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Novel fungal laccase isoenzymes (namely L95-1 and L95-2) produced by the Ascomycete Lithothelium sp. isolated from the forest soil were purified. However, only one of them was characterized, because the other isoenzyme lost its activity during purification. Extracellular L95-1 laccase was purified 30-fold using ion-exchange and hydrophobic interaction chromatography, with an overall yield of 88%. The molecular mass of purified L95-1 was estimated to be 85 kDa by SDS-PAGE analysis. L95-1 laccase was stable at temperature 4–22°C and pH 6.0–6.5. The substrate specificity of L95-1 laccase was examined with various compounds. Determined affinity constants (KM) varied in a wide range of 3.7–2020.0 µM, whereas catalytic efficiency constants (kcat/KM) covered a range of 0.008–1.9 µM–1 s–1. The optimum pH for most substrates varied in a range from pH 5.0 to 6.0. Sodium azide and fluoride strongly inhibited L95-1 activity, whereas sulphate salts inhibited weakly. The laccase was immobilized on the Fe3O4 nanoparticles and characterized. Residual activity remained at 20% after ten cycles of ABTS oxidation reaction. The immobilized laccase showed higher tolerance to various metal salts. The properties of L95-1 laccase make it potentially useful in the biotechnological applications.

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Biocatalytic characterization of free and immobilized laccase from Trametes versicolor in its activation zone

Cited by 23 publications

References 62 publications

Diversity of Wood-Decaying Fungi in Wuliangshan Area, Yunnan Province, P.R. China

Diversity of Wood-Decaying Fungi in Wuliangshan Area, Yunnan Province, P.R. China

Overview of Recent Advances in Immobilisation Techniques for Phenol Oxidases in Solution

Biosynthesis, purification, characterization and immobilization of laccase from Lithothelium sp.

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