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dc.contributor.authorBuchholz, Martina Irene
dc.date.accessioned2016-08-26T04:30:25Z
dc.date.available2016-08-26T04:30:25Z
dc.date.issued2016-08
dc.identifier.otherbuchholz_martina_i_201608_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/buchholz_martina_i_201608_ms
dc.identifier.urihttp://hdl.handle.net/10724/35570",
dc.description.abstractAlcohol oxidase (AOX), in the presence of oxygen, catalyzes the bioconversion of short-chained alcohols into their corresponding aldehydes and ketones. This enzyme has been used for electrochemical biosensors with applications in the food, medical, forensic and environmental industries. Alcohol oxidase has the potential to produce aldehydes that can serve as precursors of fine chemicals and flavour compounds naturally. However due to AOX’s poor stability, its practicality for biosensors is very limited. The application of high hydrostatic pressure (HHP) to stabilize and increase the activity of AOX at selected temperatures is reported. Intrinsic thermolabile and thermoresistant fractions of AOX were observed during thermal inactivation at atmospheric and high pressures. The slowest rates of inactivation were generally concentrated between 120 MPa and 160 MPa. A 3.2-fold increase in Vmax occurred at 160 MPa at 53.2 °C as compared to the AOX activity at 37 °C and atmospheric pressure.
dc.languageeng
dc.publisheruga
dc.rightsOn Campus Only Until 2018-08-01
dc.subjectHigh hydrostatic pressure
dc.subjectAlcohol oxidase
dc.subjectEnzyme kinetics
dc.subjectStabilization
dc.titleIncrease stability and activity of alcohol oxidase under high hydrostatic pressure
dc.typeThesis
dc.description.degreeMS
dc.description.departmentFood Science and Technology
dc.description.majorFood Science
dc.description.advisorJosé I. Reyes De Corcuera
dc.description.committeeJosé I. Reyes De Corcuera
dc.description.committeeRonald B. Pegg
dc.description.committeeWilliam L. Kerr


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