Cellobiose Dehydrogenase

Renganathan, V.; Bao, Wenjun

doi:10.1021/bk-1994-0566.ch008

ACS Symposium Series

1994

DOI: 10.1021/bk-1994-0566.ch008

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Cellobiose Dehydrogenase

V. Renganathan

Wenjun Bao

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2001

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“…The reduced enzyme is reoxidized by different electron acceptors, such as 2,6-dichloro-indophenol (DCIP), 1,2-or 1,4-benzoquinone and some of their derivatives, cytochrome c (cyt c), metal ions, including Fe(III), and even oxygen, although the latter is only a very poor electron acceptor (27). The natural electron acceptor of the enzyme is presently not known (29,34,37,42,44).…”

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confidence: 99%

Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

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121

108

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Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by several wood-degrading fungi. In the presence of a suitable electron acceptor, e.g., 2,6-dichloro-indophenol (DCIP), cytochrome c, or metal ions, CDH oxidizes cellobiose to cellobionolactone. The phytopathogenic fungus Sclerotium rolfsii (teleomorph: Athelia rolfsii) strain CBS 191.62 produces remarkably high levels of CDH activity when grown on a cellulose-containing medium. Of the 7,500 U of extracellular enzyme activity formed per liter, less than 10% can be attributed to the proteolytic product cellobiose:quinone oxidoreductase. As with CDH from wood-rotting fungi, the intact, monomeric enzyme from S. rolfsii contains one heme b and one flavin adenine dinucleotide cofactor per molecule. It has a molecular size of 101 kDa, of which 15% is glycosylation, and a pI value of 4.2. The preferred substrates are cellobiose and cellooligosaccharides; additionally, ␤-lactose, thiocellobiose, and xylobiose are efficiently oxidized. Cytochrome c (equine) and the azino-di-(3-ethyl-benzthiazolin-6-sulfonic acid) cation radical were the best electron acceptors, while DCIP, 1,4-benzoquinone, phenothiazine dyes such as methylene blue, phenoxazine dyes such as Meldola's blue, and ferricyanide were also excellent acceptors. In addition, electrons can be transferred to oxygen. Limited in vitro proteolysis with papain resulted in the formation of several protein fragments that are active with DCIP but not with cytochrome c. Such a flavin-containing fragment, with a mass of 75 kDa and a pI of 5.1 and lacking the heme domain, was isolated and partially characterized.

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mentioning

confidence: 99%

Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

Self Cite

121

108

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show abstract

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Cellobiose Dehydrogenase

Cited by 1 publication

References 20 publications

Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

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