Substrate specificity of Myriococcum thermophilum cellobiose dehydrogenase on mono-, oligo-, and polysaccharides related to in situ production of H2O2

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...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2009-11, Vol.85 (1), p.75-83
Main Authors: Pricelius, S., Ludwig, R., Lant, N., Haltrich, D., Guebitz, G. M.
Format: Article
Language:English
Subjects:
Basidiomycota - enzymology
Biological and medical sciences
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Carbohydrate Dehydrogenases - metabolism
Cellulases - metabolism
Cellulose
Cotton
Cytochrome
Dehydrogenases
Detergents
Enzymes
Fundamental and applied biological sciences. Psychology
Fungi
Horseradish Peroxidase - metabolism
Hydrogen Peroxide - metabolism
Lactose
Life Sciences
Microbial Genetics and Genomics
Microbiology
Monosaccharides - metabolism
Oligosaccharides - metabolism
Oxidation
Polysaccharides - metabolism
Sodium
Studies
Substrate Specificity
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Summary: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 H 2 O 2 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 H 2 O 2 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 H 2 O 2 to decolorize the anthocyanins within 2 h.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-009-2062-0