Cellobiose dehydrogenase. Possible roles and importance for pulp and paper biotechnology

Duarte, Júlio César; Costa‐Ferreira, Maria; Sena-Martins, G.

doi:10.1016/s0960-8524(98)00080-7

Cited by 14 publications

(6 citation statements)

References 17 publications

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“…The first and only report on the production of this enzyme in the Aspergillus niger species of was reported by Duarte et al in 1999. The researcher showed that by using the zymogram method, different isolates of different fungal species, including different species of Aspergillus niger, could be studied in terms of the production of CDH enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…The researcher showed that by using the zymogram method, different isolates of different fungal species, including different species of Aspergillus niger, could be studied in terms of the production of CDH enzymes. They showed that the CDH enzyme in the Aspergillus niger fungus is an extracellular enzyme and is secreted into the culture medium (31).…”

Section: Discussionmentioning

confidence: 99%

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Antibiofilm Activity of Cellobiose Dehydrogenase Enzyme (CDH) Isolated from Aspergillus niger on Biofilm of Clinical Staphylococcus epidermidis and Pseudomonas aeruginosa Isolates

Rasouli

Navidinia

Shams-Ghahfarokhi

et al. 2020

Arch Clin Infect Dis

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Background: It is estimated that more than 80% of cases of human infections are related to biofilm formation by invasive bacteria. So, in this study, we considered the activity of cellobiose dehydrogenase enzyme (CDH) isolated from Aspergillus niger, as an antibiofilm agent, on biofilm of clinical Staphylococcus epidermidis and Pseudomonas aeruginosa isolates. Methods: In this study, five standard strains of Aspergillus niger were purchased for CDH production. Of the 42 isolated bacterial strains, 24 strains were Staphylococcus epidermidis and 18 strains were Pseudomonas aeruginosa. Zymogram method was used for screening of CDH. The CDH activity was measured by monitoring the decrease in absorbance of 2, 6-dichlorophenolindophenol (DCPIP) spectrophotometrically. After cultivation and production of bacterial biofilms, 7 concentrations of the cellobiose prepared and CDH enzyme with a final concentration of 364 U/mL were considered on bacterial biofilms by microbroth dilution method. Results: Out of five standard strains of Aspergillus niger, only 1 strain have the highest production of CDH. The most effective dilution of cellobiose on growth inhibition of Staphylococcus epidermidis and Pseudomonas aeruginosa in liquid cultures as a function of cellobiose concentration in the presence of cellobiose dehydrogenase was in 12.5 µg/mL. Conclusions: Based on the results of this study, it can be concluded that the CDH enzyme had a high potential for use as an antimicrobial agent. As shown, this enzyme had a high potential for eliminating bacterial biofilms. So, these results may provide a basis for alternative therapies for the treatment of infections related to clinical biofilm producing bacteria.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Antibiofilm Activity of Cellobiose Dehydrogenase Enzyme (CDH) Isolated from Aspergillus niger on Biofilm of Clinical Staphylococcus epidermidis and Pseudomonas aeruginosa Isolates

Rasouli

Navidinia

Shams-Ghahfarokhi

et al. 2020

Arch Clin Infect Dis

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“…In lignin biodegradation, the two enzymes CDH and MnP have the potential to degrade the most common linkages between lignin monomers, both in phenolic and in non‐phenolic lignin, by the generation of the reactive species OH and Mn(III). However, it remains to be demonstrated that a real depolymerisation of lignin takes place under these conditions even though some data already connect CDH to lignin degradation [17,21]. In addition to ether linkages, lignin also contains condensed structures with carbon–carbon bonds between the monomers [1].…”

Section: Discussionmentioning

confidence: 99%

“…This protein is secreted by P. chrysosporium under cellulolytic conditions [16], that is, different growth conditions from those resulting in MnP and LP production. In vivo, however, the enzymes are probably present simultaneously [17,18]. CDH oxidises cellodextrins and mannodextrins (preferably cellobiose) to their corresponding lactones.…”

Section: Introductionmentioning

confidence: 99%

Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?

et al. 2000

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The extracellular enzyme manganese peroxidase is believed to degrade lignin by a hydrogen peroxide-dependent oxidation of Mn(II) to the reactive species Mn(III) that attacks the lignin. However, Mn(III) is not able to directly oxidise the non-phenolic lignin structures that predominate in native lignin. We show here that pretreatment of a non-phenolic lignin model compound with another extracellular fungal enzyme, cellobiose dehydrogenase, allows the manganese peroxidase system to oxidise this molecule. The mechanism behind this effect is demethoxylation and/or hydroxylation, i.e. conversion of a nonphenolic structure to a phenolic one, mediated by hydroxyl radicals generated by cellobiose dehydrogenase. This suggests that cellobiose dehydrogenase and manganese peroxidase may act in an extracellular pathway in fungal lignin biodegradation. Analytical techniques used in this paper are reverse-phase highpressure liquid chromatography, gas chromatography connected to mass spectroscopy and UV-visible spectroscopy. ß

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“…However, it has been proposed that CDH has a direct role in lignin degradation [7], and together with manganese peroxidase may form an extracellular pathway in fungal lignin biodegradation [8], while the Archibald group has shown that a CDH‐deficient strain of Trametes versicolor grows poorly on wood, indicating an important role for the enzyme in delignification [9]. Besides the interest being shown by many groups in the catalytic properties of CDH, with respect to lignocellulose degradation it is also of interest from a biotechnological standpoint, given its potential use both as a biosensor [10,11] and in the pulp and paper industry [12].…”

Section: Introductionmentioning

confidence: 99%

Carbon repression of cellobiose dehydrogenase production in the white rot fungusTrametes versicoloris mediated at the level of gene transcription

Stapleton

Dobson

2003

FEMS Microbiology Letters

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Cellobiose dehydrogenase (CDH) production in Trametes versicolor is induced in the presence of cellulose, but decreases when additional carbon sources such as glucose and maltose are added to the fungal cultures. Using T. versicolor-specific cdh primers in a reverse transcription-polymerase chain reaction-based approach, it appears that this repression in CDH production is being mediated at the level of gene transcription. When a 1.6-kb upstream region of the T. versicolor cdh gene was cloned and sequenced, a number of putative CreA-like binding sites were observed. We propose that these sites may be involved in mediating this repressive effect, based on their similarity to the consensus [5'-SYGGRGG-3'] site for binding of the CreA and Cre1 repressor proteins.

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Cellobiose dehydrogenase. Possible roles and importance for pulp and paper biotechnology

Cited by 14 publications

References 17 publications

Antibiofilm Activity of Cellobiose Dehydrogenase Enzyme (CDH) Isolated from Aspergillus niger on Biofilm of Clinical Staphylococcus epidermidis and Pseudomonas aeruginosa Isolates

Antibiofilm Activity of Cellobiose Dehydrogenase Enzyme (CDH) Isolated from Aspergillus niger on Biofilm of Clinical Staphylococcus epidermidis and Pseudomonas aeruginosa Isolates

Do the extracellular enzymes cellobiose dehydrogenase and manganese peroxidase form a pathway in lignin biodegradation?

Carbon repression of cellobiose dehydrogenase production in the white rot fungusTrametes versicoloris mediated at the level of gene transcription

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