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Cellobiose-oxidizing enzymes from the lignocellulose-degrading basidiomycete Phanerochaete chrysosporium: interaction with microcrystalline cellulose by V. Renganathan; S. N. Usha; Flordeliz Lindenburg is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Cellobiose-oxidizing enzymes from the lignocellulose-degrading basidiomycete Phanerochaete chrysosporium: interaction with microcrystalline cellulose about?

Cellulose-degrading cultures of the white-rot fungus Phanerochaete chrysosporium produce two extracellular cellobiose-oxidizing enzymes, cellobiose oxidase and cellobiose:quinone oxidoreductase. These two enzymes bind strongly to microcrystalline cellulose (MCC) in the pH range 4-7; above neutral pH their affinity for MCC decreases. Cellulose-bound enzymes could not be eluted with phosphate buffer (20 mM, pH 6) containing polyols (10%), KC1 (1 M), urea (1 M) or 1% ionic or non-ionic detergent. TRIS or borate buffer at pH 9 eluted 30%-35% of the cellobiose-oxidizing enzyme activity. The celluloseimmobilized enzymes oxidized cellobiose actively, suggesting that the catalytic sites are not involved in cellulose binding. These results suggest that the cellobiose-oxidizing enzymes of P. chrysosporium may be organized into two domains: a cellulose-binding domain and a catalytic domain.

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Author

V. Renganathan; S. N. Usha; Flordeliz Lindenburg

Publisher

Springer; Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc. (ISSN 1432-0614)

Published

1990

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)