Characterization of the thermostability and kinetics of Acremonium strictum glucooligosaccharide oxidase

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1999
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Fan, Zhiliang
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Reilly, Peter J.
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Abstract
The kinetics and thermostability properties of a glucooligosaccharide oxidase (GO) from Acremonium strictum were determined. The crude enzyme does not contain free mono- or disaccharides or any other enzymes that interfere with the main GO-catalyzed oxidation reaction. GO converts maltose and oxygen to only maltobionic acid and H202. This enzyme is most active at pH 9-10.5 and most stable at pH 6.5. The highest values of K[Subscript m] and V[Subscript max] occur with glucose, maltopentose, and maltoheptose, while the highest values of K[Subscript m] and V[Subscript max] with maltose occur at pH 10. Activation energies for catalysis and inactivation are 25 kJ/mol and 387 kJ/mol, respectively. The N-terminal sequence is not homologous with any other oxidase but has some homology with other proteins having different functions.
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