Characterization of Cellobiose Dehydrogenase from a Biotechnologically Important Cerrena unicolor Strain.
Appl Biochem Biotechnol
; 176(6): 1638-58, 2015 Jul.
Article
en En
| MEDLINE
| ID: mdl-26003328
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Fúngicas
/
Deshidrogenasas de Carbohidratos
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Celulosa
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Polyporales
Idioma:
En
Revista:
Appl Biochem Biotechnol
Año:
2015
Tipo del documento:
Article
País de afiliación:
Polonia
Pais de publicación:
Estados Unidos