
pmid: 21298807
AbstractThe carbohydrate oxidase from Microdochium nivale (CAOX), heterologously expressed in Aspergillus oryzae, and cellobiose dehydrogenase from Myriococcum thermophilum (MtCDH), were assessed for their ability to generate bleaching species at a pH suitable for liquid detergents. The substrate specificities of CAOX and MtCDH were analyzed on a large variety of soluble and insoluble substrates, using oxygen as an electron receptor. Even insoluble substrates like cellulose were oxidized from both CAOX and MtCDH, but only MtCDH produced H2O2 on cotton as the sole substrate. To enhance the amount of cello‐oligosaccharides formed from cotton as substrates for CAOX and MtCDH, various cellulases were used in combination with MtCDH or CAOX, leading to a 10‐fold increase in H2O2. As model substrates for colored stains, the degradation of pure anthocyanins and stain removal of blueberry stains by CAOX and MtCDH was examined in the absence and presence of a horseradish peroxidase. Both enzymes were able to produce an amount of H2O2 sufficient to decolorize the pure anthocyanins within 2 h and showed significant cleaning benefits on the stains.
Industrial Microbiology, Aspergillus oryzae, Basidiomycota, Detergents, Carbohydrate Dehydrogenases, Hydrogen Peroxide, Oxidoreductases, Horseradish Peroxidase, Substrate Specificity
Industrial Microbiology, Aspergillus oryzae, Basidiomycota, Detergents, Carbohydrate Dehydrogenases, Hydrogen Peroxide, Oxidoreductases, Horseradish Peroxidase, Substrate Specificity
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