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In situ generation of hydrogen peroxide by carbohydrate oxidase and cellobiose dehydrogenase for bleaching purposes
Author(s) -
Pricelius Sina,
Ludwig Roland,
Lant Neil J.,
Haltrich Dietmar,
Guebitz Georg M.
Publication year - 2011
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201000246
Subject(s) - cellobiose dehydrogenase , hydrogen peroxide , cellobiose , in situ , chemistry , glucose oxidase , biochemistry , dehydrogenase , carbohydrate , oxidase test , enzyme , organic chemistry , cellulase
The 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 H 2 O 2 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 H 2 O 2 . 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 H 2 O 2 sufficient to decolorize the pure anthocyanins within 2 h and showed significant cleaning benefits on the stains.