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Gewählte Publikation:

Pricelius, S; Ludwig, R; Lant, N; Haltrich, D; Guebitz, GM.
(2009): Substrate specificity of Myriococcum thermophilum cellobiose dehydrogenase on mono-, oligo-, and polysaccharides related to in situ production of H2O2
APPL MICROBIOL BIOTECHNOL. 2009; 85(1): 75-83. FullText FullText_BOKU

Abstract:
Cellobiose dehydrogenase from the ascomycete fungus Myriococcum thermophilum (MtCDH) was tested for the ability to generate bleaching species at a pH suitable for liquid detergents. The catalytic properties of MtCDH were investigated for a large variety of carbohydrate substrates using oxygen as an electron receptor. MtCDH produces H2O2 with all substrates tested (except fructose) but only in the presence of a chelant. Insoluble substrates like cellulose and cotton could as well be oxidized by MtCDH. To enhance the amount of cello-oligosaccharides in solution, different cellulases on cotton were used and in combination with MtCDH an increased H2O2 concentration could be measured. Additionally, the degradation of pure anthocyanins in solution (as model substrates for bleaching) was investigated in the absence and presence of a horseradish peroxidase. MtCDH was able to produce a sufficient amount of H2O2 to decolorize the anthocyanins within 2 h.
Autor/innen der BOKU Wien:
Gübitz Georg
Haltrich Dietmar
Ludwig Roland
BOKU Gendermonitor:


Find related publications in this database (Keywords)
Carbohydrate oxidation
Cellobiose dehydrogenase
Destaining
Hydrogen peroxide
Myriococcum thermophilum


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