Characterization of the thermostability and kinetics of Acremonium strictum glucooligosaccharide oxidase

dc.contributor.advisor Reilly, Peter J.
dc.contributor.author Fan, Zhiliang
dc.date.accessioned 2024-03-22T15:53:03Z
dc.date.available 2024-03-22T15:53:03Z
dc.date.issued 1999
dc.description.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.
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/dvmqQy3v
dc.language.iso en
dc.title Characterization of the thermostability and kinetics of Acremonium strictum glucooligosaccharide oxidase
dc.type Thesis
dc.type.genre Thesis
dspace.entity.type Publication
relation.isDegreeOrgUnitOfPublication 86545861-382c-4c15-8c52-eb8e9afe6b75
thesis.degree.department Chemical and Biological Engineering
thesis.degree.discipline Chemical Engineering
thesis.degree.level Masters
thesis.degree.name Master of Science
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