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- W2102022172 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." @default.
- W2102022172 created "2016-06-24" @default.
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- W2102022172 date "2015-05-24" @default.
- W2102022172 modified "2023-09-30" @default.
- W2102022172 title "Characterization of Cellobiose Dehydrogenase from a Biotechnologically Important Cerrena unicolor Strain" @default.
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- W2102022172 doi "https://doi.org/10.1007/s12010-015-1667-2" @default.
- W2102022172 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4515248" @default.
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