ArticleApplied biochemistry and biotechnology2015
Characterization of Cellobiose Dehydrogenase from a Biotechnologically Important Cerrena unicolor Strain.
Article in Applied biochemistry and biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 26 citations in OpenAlex.
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- Chitosan as a Promising Support of a CDH Activity Preservation System for Biomedical and Industrial Applications.International journal of molecular sciences · 2023Article
- Drimane-Type Sesquiterpenoids Derived from the Tropical BasidiomycetesMolecules (Basel, Switzerland) · 2022Article
- Genomic Studies of White-Rot FungusJournal of fungi (Basel, Switzerland) · 2021Article
- Natural microbial polysaccharides as effective factors for modification of the catalytic properties of fungal cellobiose dehydrogenase.Archives of microbiology · 2021Article
- The wood decay fungus Cerrena unicolor adjusts its metabolism to grow on various types of wood and light conditions.PloS one · 2019Article
- Inactivation of Cellobiose Dehydrogenases Modifies the Cellulose Degradation Mechanism of Podospora anserina.Applied and environmental microbiology · 2017Article
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8 authors at 1 institution in 1 country.
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Abstract
Cellobiose dehydrogenase (CDH), a secreted flavocytochrome produced by a number of wood-degrading fungi, was detected in the culture supernatant of a biotechnologically important strain of Cerrena unicolor grown in a modified cellulose-based liquid medium. The enzyme was purified as two active fractions: CuCDH-FAD (flavin domain) (1.51-fold) with recovery of 8.35 % and CuCDH (flavo-heme enzyme) (21.21-fold) with recovery of 73.41 %. As CDH from other wood-rotting fungi, the intact form of cellobiose dehydrogenase of C. unicolor is a monomeric protein containing one flavin and one heme b with molecular mass 97 kDa and pI = 4.55. The enzyme is glycosylated (8.2 %) mainly with mannose and glucosamine residues. Moreover, the cellobiose dehydrogenase gene cdh1 and its corresponding cDNA from the fungus C. unicolor were isolated, cloned, and characterized. The 2316-bp full-length cDNA of cdh1 encoded a mature CDH protein containing 771 amino acids preceded by a signal peptide consisting of 18 amino acids. Moreover, both active fractions were characterized in terms of kinetics, temperature and pH optima, and antioxidant properties.
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