Literature DB >> 3322681

Properties of ligninase from Phanerochaete chrysosporium and their possible applications.

M Tien1.   

Abstract

The wood-degrading fungus Phanerochaete chrysosporium Burds produces a family of enzymes which degrade lignin and lignin-like substrates. These ligninases exhibit a high degree of homology in being hemeprotein peroxidases, in Mr, in cross reactivity to polyclonal antibodies, in being glycosylated, and in catalytic properties. The predominant ligninase is able to generate cation radicals in its aromatic substrates. These radicals can undergo a variety of reactions thus explaining the nonspecific nature of the enzyme. A similar mechanism is suggested for the other isoenzymes. There are numerous potential applications for ligninases. These include: biopulping, waste treatment of byproduct lignins, detoxification of environmental pollutants, and modification of lignins to produce small molecular weight organics.

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Year:  1987        PMID: 3322681     DOI: 10.3109/10408418709104456

Source DB:  PubMed          Journal:  Crit Rev Microbiol        ISSN: 1040-841X            Impact factor:   7.624


  27 in total

Review 1.  P450 monooxygenases (P450ome) of the model white rot fungus Phanerochaete chrysosporium.

Authors:  Khajamohiddin Syed; Jagjit S Yadav
Journal:  Crit Rev Microbiol       Date:  2012-05-25       Impact factor: 7.624

2.  Intra- and Extracellular Localization of Lignin Peroxidase during the Degradation of Solid Wood and Wood Fragments by Phanerochaete chrysosporium by Using Transmission Electron Microscopy and Immuno-Gold Labeling.

Authors:  G Daniel; T Nilsson; B Pettersson
Journal:  Appl Environ Microbiol       Date:  1989-04       Impact factor: 4.792

3.  Protease-mediated degradation of lignin peroxidase in liquid cultures of Phanerochaete chrysosporium.

Authors:  C G Dosoretz; S B Dass; C A Reddy; H E Grethlein
Journal:  Appl Environ Microbiol       Date:  1990-11       Impact factor: 4.792

4.  Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay.

Authors:  A Datta; A Bettermann; T K Kirk
Journal:  Appl Environ Microbiol       Date:  1991-05       Impact factor: 4.792

5.  Degradation of environmental pollutants byPhanerochaete chrysosporium.

Authors:  S D Aust
Journal:  Microb Ecol       Date:  1990-12       Impact factor: 4.552

6.  2-chloro-1,4-dimethoxybenzene as a novel catalytic cofactor for oxidation of anisyl alcohol by lignin peroxidase.

Authors:  P J Teunissen; J A Field
Journal:  Appl Environ Microbiol       Date:  1998-03       Impact factor: 4.792

7.  Lignin-Degrading Enzymes of the Commercial Button Mushroom, Agaricus bisporus.

Authors:  A M Bonnen; L H Anton; A B Orth
Journal:  Appl Environ Microbiol       Date:  1994-03       Impact factor: 4.792

8.  Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase.

Authors:  P J Kersten
Journal:  Proc Natl Acad Sci U S A       Date:  1990-04       Impact factor: 11.205

9.  Overproduction of lignin peroxidase by Phanerochaete chrysosporium (BKM-F-1767) under nonlimiting nutrient conditions.

Authors:  C G Dosoretz; N Rothschild; Y Hadar
Journal:  Appl Environ Microbiol       Date:  1993-06       Impact factor: 4.792

10.  Manganese regulates expression of manganese peroxidase by Phanerochaete chrysosporium.

Authors:  J A Brown; J K Glenn; M H Gold
Journal:  J Bacteriol       Date:  1990-06       Impact factor: 3.490

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