Substrate specificity of Myriococcum thermophilum cellobiose dehydrogenase on mono-, oligo-, and polysaccharides related to in situ production of H sub(2)O sub(2)

• Published in: Applied microbiology and biotechnology 2009-01, Vol.85 (1), p.75-83
• Main Authors: Pricelius, S, Ludwig, R, Lant, N, Haltrich, D, Guebitz, G M
• Format: Article
• Language: English
• Subjects: Ascomycetes
• ISSN: 0175-7598; 1432-0614
• DOI: 10.1007/s00253-009-2062-0

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 sub(2)O sub(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 sub(2)O sub(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 sub(2)O sub(2) to decolorize the anthocyanins within 2h.