Novel biocatalyst from Microthielavia ovispora VKM F-1735 for industrial dye decolorization in the absence of mediators

Shebanova, Anna D.; Chernykh, A.M.; Баскунов, Б. П.; Gaidina, Anastasya S.; Myasoedova, N. M.; Renfeld, Zhanna V.; Понаморева, О. Н.; Kolomytseva, M. P.

doi:10.1016/j.procbio.2021.07.009

Cited by 2 publications

(1 citation statement)

References 60 publications

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“…Because of insufficient stability of fungal oxidases, though, it may be difficult to use them for analytical purposes. On the other hand, this is an incentive to research aimed at finding new species of higher fungi for producing oxidoreductases [13,14], studying the ways to increase the production of enzymes with oxidative properties in fungal biomass during the cultivation stage, and discovering fungal oxidases with new properties [15,16]. Studies are conducted to develop and improve the methods of isolating these enzymes from the biomass and immobilizing them on various carriers in order to enhance their resistance to negative factors and enable them to retain their catalytic function when reused multiple times [17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

On the Substrate Specificity and Some Properties of the Extracellular Oxidase from the Neonothopanus nambi Basidiomycete

Mogilnaya,

Ronzhin,

Posokhina

et al. 2024

AJBGMB

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The present study reports experimental data on substrate specificity and some properties of the extracellular enzyme with oxidase activity isolated from the mycelium of the higher fungus Neonothopanus nambi IBSO 2391 by treating the biomass with \(\beta\) -glucosidase. Gel-filtration chromatography showed that molecular weight of the isolated enzyme was 80 kDa. Spectral analysis did not reveal any chromophore components in the enzyme. The extracellular oxidase of the basidiomycete N. nambi IBSO 2391 was active with most of the aromatic compounds chosen as model substrates. An important fact is that the enzyme exhibited catalytic activity with no hydrogen peroxide or any other mediators added to the reaction mixture. The highest activity of the enzyme was observed in reactions with veratryl alcohol and hydroquinone. In reactions with guaiacol and aromatic amines (diaminobenzidine, o-dianisidine), the level of activity of the extracellular oxidase was considerably lower – by a factor of 2.5–3.5. In reactions with resorcinol, phenol, and caffeic acid, the catalytic efficiency of the enzyme was no greater than 6% of its activity with veratryl alcohol. Kinetic parameters of enzymatic reactions were determined for the most efficiently oxidized substrates. The addition of the chelating agent of divalent metal ions (EDTA) did not affect the activity of the extracellular oxidase from the fungus N. nambi IBSO 2391, indicating the absence of divalent metal ions in the molecule of the enzyme. At the same time, addition of the SH reagent (DTT) increased catalytic efficiency of the enzyme. The study showed that the extracellular oxidase of the fungus N. nambi IBSO 2391 functions in wide ranges of temperature and pH of the reaction medium, showing the highest catalytic activity at temperatures between 22 and 35 °C and pH 6.0. Results obtained in the current study provide the basis for studying potential uses of the isolated enzyme in biomedical analytics and bioremediation.

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Section: Introductionmentioning

confidence: 99%

On the Substrate Specificity and Some Properties of the Extracellular Oxidase from the Neonothopanus nambi Basidiomycete

Mogilnaya,

Ronzhin,

Posokhina

et al. 2024

AJBGMB

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show abstract

On the Substrate Specificity and Some Properties of the Extracellular Oxidase From the Neonothopanus Nambi Basidiomycete

Mogilnaya,

Ronzhin,

Posokhina

et al. 2024

Russian Journal of Biological Physics and Chemisrty

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An extracellular enzyme with oxidase activity was isolated from the mycelium of the higher fungus Neonothopanus nambi by mild treatment of the biomass with β-glucosidase. A substrate specificity and some properties of the isolated extracellular oxidase were studied in the present work. Experiments revealed that the extracellular oxidase exhibited activity with most phenolic compounds chosen as model substrates. It is important to note that the enzyme exhibited a catalytic function in the reactions without the addition of exogenous hydrogen peroxide and other mediators. The highest catalytic activity of the enzyme was observed with veratryl alcohol and dihydric phenols, hydroquinone and guaiacol. The enzyme showed lower activity with aromatic azo compounds (ABTS, DAB, o-dianisidine). In reactions with dihydric phenol resorcinol and monophenol, the enzyme efficiency was extremely low. The kinetic parameters of the enzymatic reactions with actively oxidized substrates were determined. The addition of a divalent metal ion chelator (EDTA) did not affect the activity of the enzyme, while the addition of the SH reagent (DTT) increased the catalytic efficiency of the studied oxidase. The totality of the data obtained indicates that the extracellular oxidase of the N. nambi fungus catalyzes the oxidation of a wide range of aromatic compounds under slightly acidic and neutral conditions without the addition of additional mediators (in particular, hydrogen peroxide). This creates the prerequisites for studying the applicability of the enzyme in biomedical analytics.

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Novel biocatalyst from Microthielavia ovispora VKM F-1735 for industrial dye decolorization in the absence of mediators

Cited by 2 publications

References 60 publications

On the Substrate Specificity and Some Properties of the Extracellular Oxidase from the Neonothopanus nambi Basidiomycete

On the Substrate Specificity and Some Properties of the Extracellular Oxidase from the Neonothopanus nambi Basidiomycete

On the Substrate Specificity and Some Properties of the Extracellular Oxidase From the Neonothopanus Nambi Basidiomycete

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