Abstract
This study is a contribution to the identification and characterization, at a molecular level, of the enzymic machinery utilized by Trametes versicolor to effect ligninolysis. Emphasis has been given to lignin peroxidase and the genes encoding this enzyme. The characterization of genes contributes to the knowledge of the primary structure of fungal peroxidases. Although much has been gained from studies of complex systems, such as fungal cultures or crude enzyme preparations, a final characterization cannot be reached without the use of defined reaction components. Enzyme purification, studies of the action of pure enzyme preparations on well defined substrates, and characterization of enzyme structure have therefore been given attention. Since ligninolytic peroxidases appear to be produced by T.versicolor during secondary metabolism, the time required for enzyme production tends to be rather long. Adequate supply of enzyme, preferably in the form of pure isozymes, would be helpful for further studies of the structure, action, and mechanism of ligninolytic peroxidases. Molecular genetic approaches, such as heterologous expression of overproduction of isolated genes, are usually valuable tools in this regard, especially for detailed studies of structure and function by use of site-directed mutagenesis
Citation Formats
Joensson, Leif.
Lignin peroxidase from the wood-degrading basidiomycete Trametes versicolor. Studies of enzymic properties and gene structure.
Sweden: N. p.,
1994.
Web.
Joensson, Leif.
Lignin peroxidase from the wood-degrading basidiomycete Trametes versicolor. Studies of enzymic properties and gene structure.
Sweden.
Joensson, Leif.
1994.
"Lignin peroxidase from the wood-degrading basidiomycete Trametes versicolor. Studies of enzymic properties and gene structure."
Sweden.
@misc{etde_10142887,
title = {Lignin peroxidase from the wood-degrading basidiomycete Trametes versicolor. Studies of enzymic properties and gene structure}
author = {Joensson, Leif}
abstractNote = {This study is a contribution to the identification and characterization, at a molecular level, of the enzymic machinery utilized by Trametes versicolor to effect ligninolysis. Emphasis has been given to lignin peroxidase and the genes encoding this enzyme. The characterization of genes contributes to the knowledge of the primary structure of fungal peroxidases. Although much has been gained from studies of complex systems, such as fungal cultures or crude enzyme preparations, a final characterization cannot be reached without the use of defined reaction components. Enzyme purification, studies of the action of pure enzyme preparations on well defined substrates, and characterization of enzyme structure have therefore been given attention. Since ligninolytic peroxidases appear to be produced by T.versicolor during secondary metabolism, the time required for enzyme production tends to be rather long. Adequate supply of enzyme, preferably in the form of pure isozymes, would be helpful for further studies of the structure, action, and mechanism of ligninolytic peroxidases. Molecular genetic approaches, such as heterologous expression of overproduction of isolated genes, are usually valuable tools in this regard, especially for detailed studies of structure and function by use of site-directed mutagenesis}
place = {Sweden}
year = {1994}
month = {Jan}
}
title = {Lignin peroxidase from the wood-degrading basidiomycete Trametes versicolor. Studies of enzymic properties and gene structure}
author = {Joensson, Leif}
abstractNote = {This study is a contribution to the identification and characterization, at a molecular level, of the enzymic machinery utilized by Trametes versicolor to effect ligninolysis. Emphasis has been given to lignin peroxidase and the genes encoding this enzyme. The characterization of genes contributes to the knowledge of the primary structure of fungal peroxidases. Although much has been gained from studies of complex systems, such as fungal cultures or crude enzyme preparations, a final characterization cannot be reached without the use of defined reaction components. Enzyme purification, studies of the action of pure enzyme preparations on well defined substrates, and characterization of enzyme structure have therefore been given attention. Since ligninolytic peroxidases appear to be produced by T.versicolor during secondary metabolism, the time required for enzyme production tends to be rather long. Adequate supply of enzyme, preferably in the form of pure isozymes, would be helpful for further studies of the structure, action, and mechanism of ligninolytic peroxidases. Molecular genetic approaches, such as heterologous expression of overproduction of isolated genes, are usually valuable tools in this regard, especially for detailed studies of structure and function by use of site-directed mutagenesis}
place = {Sweden}
year = {1994}
month = {Jan}
}