Occurrence and biocatalytic potential of carbohydrate oxidases
Autor: | van Hellemond, Erik W., Leferink, Nicole G. H., Heuts, Dominic P. H. M., Fraaije, Marco W., van Berkel, Willem J. H., Laskin, AI, Sariaslani, S, Gadd, GM |
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Jazyk: | angličtina |
Rok vydání: | 2006 |
Předmět: |
chemistry.chemical_classification
L-GULONOLACTONE-OXIDASE biology Carbohydrate synthesis L-ASCORBIC-ACID BERBERINE BRIDGE ENZYME Carbohydrate Berberine bridge enzyme CORYNEBACTERIUM SP 2-4-1 Cofactor Enzyme Biochemistry chemistry biology.protein L-Galactonolactone oxidase L-GALACTONOLACTONE OXIDASE Molecular oxygen AMINO-ACID OXIDASE TUBULAR MEMBRANE SYSTEM FLOW-INJECTION ANALYSIS COVALENTLY-BOUND FLAVIN GAMMA-LACTONE OXIDASE |
Zdroj: | Advances in Applied Microbiology, 60, 17-54 |
ISSN: | 0065-2164 |
Popis: | Publisher Summary Carbohydrate oxidases are found in all kingdoms of life but are mostly found in fungi. Their natural role is not always clear. Usage of molecular oxygen as electron acceptor is not a logical choice when the enzyme is part of a catabolic pathway. This chapter provides an overview of the occurrence and properties of carbohydrate oxidases. The physiological role of the different enzymes is discussed in relation to their origin, and the catalytic and structural properties are discussed in relation to their family background. It also provides a summary of the biocatalytic applications of carbohydrate oxidases. Carbohydrate oxidases are valuable enzymes for several applications. They are relatively stable and do not need expensive coenzymes. Carbohydrate oxidases are widely used in diagnostic applications, in the food and drinks industry, and for carbohydrate synthesis. They are also used for bleaching (production of H2O2) and as oxygen scavenger. |
Databáze: | OpenAIRE |
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