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Temp, Ulrike; Meyrahn, H.; Eggert, Claudia

doi:10.1023/a:1005491818192

Cited by 30 publications

(6 citation statements)

References 20 publications

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“…Therefore, only the nearest surrounding of the laccase active center was supposed to be affected by toluene. In this study, coal HA did not have a negative effect on laccase activity (Figure 5), what was in agreement with recently published data [44]. The finding, nevertheless, contradicted the reported data on the inhibitory effect of coal HA on laccase [29].…”

Section: Dynamic Of Laccase Activity In the Presence And Absence Of Csupporting

confidence: 91%

Interaction of Coal Humic Acids with Fungal Laccase

Куликова¹,

Davidchik²,

Цветкова³

et al. 2013

AiM

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Humic acids (HA) are one of the main environmental factors controlling the fate and behavior of the compounds released into the environment. In particular, they are universally considered of great importance in determining soil extracellular enzyme activity and stability via association with essential soil enzymes. The objective of this study was to investigate the interaction of coal HA with an extracellular multicopper oxidase laccase (EC 1.10.3.2) that catalyze the oxidation of a wide range of reducing substances in the environment. Using size-exclusion chromatography analysis and monitoring laccase activity, the formation of a stable and an enzymatically active complex between HA and laccase was shown. Basing the data obtained by isoelectric focusing of HA-laccase complex, non-covalent character of laccase association with HA was considered and binding of laccase to HA by weak dispersive forces such as van der Waals, hydrophobic, π-π, CH-π and others was hypothesized.

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Section: Dynamic Of Laccase Activity In the Presence And Absence Of Csupporting

confidence: 91%

Interaction of Coal Humic Acids with Fungal Laccase

Куликова¹,

Davidchik²,

Цветкова³

et al. 2013

AiM

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“…The best investigated example is the production of CDH by P. chrysosporium, in which under cellulolytic conditions this oxidoreductase represents about 0.5% of the extracellular protein [19]. Further examples of white-rot CDH producers are represented by Irpex lacteus [20] and Pycnoporus cinnabarinus [21] both of which possess two different CDHs when grown on cellulose as a carbon source. Notably, CDH from Py.…”

Section: Production Of Cdh In Basidiomycetesmentioning

confidence: 99%

“…Purified, characterized, sequenced [41,138] Flammulina velutipes DCIP and cyt c activity [139] Ganoderma gibbosum DCIP and cyt c activity [139] Grifola frondosa Sequenced [30] Hericium erinaceum DCIP and cyt c activity [139] Heterobasidion annosum DCIP activity [42] Irpex lacteus Purified, characterized, sequenced [20] Phanerochaete chrysosporium Purified, characterized, sequenced, crystallized [11][12][13][14] Pycnoporus cinnabarinus Purified, characterized, sequenced [21,46] Schizophyllum commune Purified, characterized [132,140] Sclerotium coffeicola DCIP and cyt c activity [35] Sclerotium delphinii DCIP and cyt c activity [35] Sclerotium rolfsii Purified, characterized, sequenced [34,47] Trametes pubescens Purified, characterized [18] Trametes versicolor Purified, characterized, sequenced [17,44] Trametes villosa Purified, characterized [18] respectively, in cdh transcript levels [32]. In P. chrysosporium it was also shown by RT-PCR that the cdh gene is differentially regulated compared to the bgl (β-glucosidase) gene.…”

Section: Coniophora Puteanamentioning

confidence: 99%

Cellobiose Dehydrogenase – A Flavocytochrome from Wood-Degrading, Phytopathogenic and Saprotropic Fungi

Zámocký¹,

Ludwig

Peterbauer

et al. 2006

CPPS

221

230

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Cellobiose dehydrogenase, the only currently known extracellular flavocytochrome, is formed not only by a number of wood-degrading but also by various phytopathogenic fungi. This inducible enzyme participates in early events of lignocellulose degradation, as investigated in several basidiomycete fungi at the transcriptional and translational level. However, its role in the ascomycete fungi is not yet obvious. Comprehensive sequence analysis of CDH-encoding genes and their translational products reveals significant sequence similarities along the entire sequences and also a common domain architecture. All known cellobiose dehydrogenases fall into two related subgroups. Class-I members are represented by sequences from basidiomycetes whereas class-II comprises longer, more complex sequences from ascomycete fungi. Cellobiose dehydrogenase is typically a monomeric protein consisting of two domains joined by a protease-sensitive linker region. Each larger (dehydrogenase) domain is flavin-associated while the smaller (cytochrome) domains are haem-binding. The latter shorter domains are unique sequence motifs for all currently known flavocytochromes. Each cytochrome domain of CDH can bind a single haem b as prosthetic group. The larger dehydrogenase domain belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily - a widespread flavoprotein evolutionary line. The larger domains can be further divided into a flavin-binding subdomain and a substrate-binding subdomain. In addition, the class-II (but not class-I) proteins can possess a short cellulose-binding module of type 1 at their C-termini. All the cellobiose dehydrogenases oxidise cellobiose, cellodextrins, and lactose to the corresponding lactones using a wide spectrum of different electron acceptors. Their flexible specificity serves as a base for the development of possible biotechnological applications.

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“…Kelompok dari genus Polyporus sp. juga pernah dilaporkan oleh Temp et al (1999) bahwa hasil pengujian aktivitas enzim isolat Polyporus ciliates mampu menghasilkan enzim Lac dan MnP di dalam media yang ditambahkan asam humat dari batu bara. Sedangkan dari genus Coriolopsis sp.…”

Section: Aktivitas Enzim Ekstraselulerunclassified

Fungi Dekomposer Penghasil Enzim Ekstraseluler Lakase, Mangan Peroksidase, dan Lignin Peroksidase dari Kawasan Kebun Raya Bogor: Isolasi, Seleksi, Identifikasi dan Kajian Aktivitas Enzimnya

Ruhimat¹,

Djajakirana²,

Antonius³

2022

JBI

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This study aimed to obtain the candidate isolates of superior decomposer from several plant block areas in the Bogor Botanic Gardens (KRB). Those candidates were expected to be able to utilize in the fermentation process of solid organic waste. The superior decomposer fungi candidates were selected based on their abilities to produce extracellular enzymes (laccase - Lac, manganese peroxidase - MnP, and lignin peroxidase - LiP) using 0.05% guaiacol as a substrate. The highest abundance of decomposer population was found in the block 4 with 9.9 x 106 CFU ml-1, and the lowest in block 6 with 1.9 x 106 CFU ml-1 density. Three superior decomposer isolates were obtained, namely KRB 3.1 (from block area 3), KRB 4.6 (from block area 4), KRB 6.7 isolate (from block area 7). The KRB 6.7 isolate has the highest Lac and MnP enzyme activities, as the following 24.10 U ml-1 and 186.3 U ml-1, while KRB 3.1 isolate from block area 3 has the highest LiP activity with the value 598.57 U ml-1. According to the molecular analysis, those candidate isolates of superior decomposers were identified as Coriolopsis hainanensis (KRB 3.1 isolate), Polyporus thailandensis (KRB 4.6 isolate), and Cerrena aurantiopora (KRB 6.7 isolate). Those are potentially used as the decomposers in solid organic waste fermentation.

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Untitled

Cited by 30 publications

References 20 publications

Interaction of Coal Humic Acids with Fungal Laccase

Interaction of Coal Humic Acids with Fungal Laccase

Cellobiose Dehydrogenase – A Flavocytochrome from Wood-Degrading, Phytopathogenic and Saprotropic Fungi

Fungi Dekomposer Penghasil Enzim Ekstraseluler Lakase, Mangan Peroksidase, dan Lignin Peroksidase dari Kawasan Kebun Raya Bogor: Isolasi, Seleksi, Identifikasi dan Kajian Aktivitas Enzimnya

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