Results 141 to 150 of about 165,484 (185)
Some of the next articles are maybe not open access.
Carbohydrate Research, 2013
We report the chemo-enzymatic synthesis of three cellobiono-1,5-lactone azido derivatives, designed as building blocks for biomedical polymer scaffolds. The synthesis is based on regioselective protection of cellobiose or 1,6-O-anhydro-β-d-cellobiose before azidation and subsequent deprotection.
Mulla, Dafina +9 more
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We report the chemo-enzymatic synthesis of three cellobiono-1,5-lactone azido derivatives, designed as building blocks for biomedical polymer scaffolds. The synthesis is based on regioselective protection of cellobiose or 1,6-O-anhydro-β-d-cellobiose before azidation and subsequent deprotection.
Mulla, Dafina +9 more
openaire +3 more sources
Substrate Specificity of Cellobiose Dehydrogenase From Phanerochaete chrysosporium
BBA - Proteins and Proteomics, 1998Substrate structural mapping suggests that the catalytic site of cellobiose dehydrogenase from Phanerochaete chrysosporium forms a narrow cave with two hexose binding subsites. Kinetic data also show that beta-di or oligosaccharides are favored electron donors with respect to both KM and kcat.
Gunnar Henriksson +2 more
exaly +3 more sources
Biosensor Based on Cellobiose Dehydrogenase for Detection of Catecholamines
Analytical Chemistry, 2004A cellobiose dehydrogenase (CDH)-modified graphite electrode was designed for amperometric detection of catecholamines in the flow injection mode, by their recycling between the graphite electrode (+300 mV vs Ag|AgCl) and the reduced FAD cofactor of adsorbed CDH, resulting in an amplified response signal. The high efficiency of the enzyme-catecholamine
Leonard, Stoica +3 more
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Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase
Gene, 1999We have cloned and sequenced a gene encoding cellobiose dehydrogenase (CDH) from Pycnoporus cinnabarinus (Pci). PCR primers that may recognize a homologous cdh were designed using regions of complete conservation of amino acid sequence within the known sequences of Trametes versicolor (Tv) and Phanerochaete chrysosporium (Pc) CDH.
Moukha, S.M. +3 more
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Biochemical Society Transactions, 2000
An important aspect of the cytochrome c electrochemistry is the possibility of coupling the ‘heterogeneous reactions’ with other redox enzymes. Cellobiose dehydrogenase, a 89170 Da glycoprotein that contains both FAD and a b-type haem as prosthetic groups, donates electrons to a number of acceptors, including cytochrome c.
Fridman, Vadim +7 more
openaire +3 more sources
An important aspect of the cytochrome c electrochemistry is the possibility of coupling the ‘heterogeneous reactions’ with other redox enzymes. Cellobiose dehydrogenase, a 89170 Da glycoprotein that contains both FAD and a b-type haem as prosthetic groups, donates electrons to a number of acceptors, including cytochrome c.
Fridman, Vadim +7 more
openaire +3 more sources
Cellobiose dehydrogenase-based biomedical applications
Process Biochemistry, 2017Abstract Cellobiose dehydrogenase (CDH) is an emerging enzyme that is being investigated for applications in many fields including biosensors, biofuels, bioremediation, and textile processing and recently for several biomedical applications. This review summarizes the recent advances in the application of CDH in the biomedical field, particularly as ...
Gibson S. Nyanhongo +2 more
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A cellulase assay coupled to cellobiose dehydrogenase
Analytical Biochemistry, 1985An assay for cellulase activity based on the oxidation of cellobiose, formed during the cellulase reaction, with ferricyanide and a cellobiose dehydrogenase derived from the cellulolytic fungus Sporotrichum (Chrysosporium) thermophile is presented. Due to the restricted specificity of this enzyme for cellobiose and cellodextrins, glucose, which may be ...
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Assay for cellobiose dehydrogenase in the presence of laccase
Biotechnology Techniques, 1997The currently used assay for cellobiose dehydrogenase (CDH), an enzyme produced by many wood degrading fungi, lacks specificity and can give false results. The presence of laccase interferes with the standard assay. We have developed an assay for CDH that is insensitive to the presence of both laccase and other phenoloxidases.
G. Henriksson, V. Polk, K.-E.L. Eriksson
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Journal of Basic Microbiology, 2018
This work investigated the regulatory role of the interaction between cellobiose dehydrogenase (CDH) and β‐glucosidase (β‐GLU) in the conversion of cellobiose into cellobionolactone or glucose in vitro. To study the regulation, the two enzymes were isolated from the culture medium of the fungus Cerrena unicolor grown on a medium with microcrystalline ...
Alexander V. Lisov +5 more
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This work investigated the regulatory role of the interaction between cellobiose dehydrogenase (CDH) and β‐glucosidase (β‐GLU) in the conversion of cellobiose into cellobionolactone or glucose in vitro. To study the regulation, the two enzymes were isolated from the culture medium of the fungus Cerrena unicolor grown on a medium with microcrystalline ...
Alexander V. Lisov +5 more
openaire +2 more sources
Journal of Biotechnology, 2006
The extracellular cellobiose dehydrogenase (CDH) obtained from Chaetomium sp. INBI 2-26(-) has a molecular mass of 95 kDa and an isoelectric point of 5. This novel CDH is highly specific for the oxidation of cellobiose (K(m,app) 4.5 microM) and lactose (K(m,app) 56 microM). With 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) (cyt c(3+)) as electron
K N, Karapetyan +5 more
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The extracellular cellobiose dehydrogenase (CDH) obtained from Chaetomium sp. INBI 2-26(-) has a molecular mass of 95 kDa and an isoelectric point of 5. This novel CDH is highly specific for the oxidation of cellobiose (K(m,app) 4.5 microM) and lactose (K(m,app) 56 microM). With 2,6-dichloroindophenol (DCIP) and cytochrome c(3+) (cyt c(3+)) as electron
K N, Karapetyan +5 more
openaire +2 more sources