Optimization of flavin oxidase enzymes for human health monitoring
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Issue Date
2021-05-31Author
Deay, Dwight O'Dell
Publisher
University of Kansas
Format
163 pages
Type
Dissertation
Degree Level
Ph.D.
Discipline
Molecular Biosciences
Rights
Copyright held by the author.
Metadata
Show full item recordAbstract
Biosensors are an analytic modality able to quantify, in real time, the abundance of specific analytes in complex biological mixtures such as blood, the brain, and in a variety of organs. However, the use of biosensors has been limited to analytes for which suitable oxidase enzyme exists. Flavin dependent peroxide producing oxidase enzymes serve as the highly specific biorecognition elements in the fabrication of amperometric biosensors. While many enzymes have been evaluated for the purposes of in vivo sensing, most of these studies have failed because these enzymes are inherently unsuitable for in vivo biosensing applications because of low stability, low substrate affinity, and/or slow rates of turnover. The common thread that ties together these diverse studies performed as part of my dissertation work is the focus on improving enzymes for in vivo biosensing and human health monitoring applications. My goal has been to improve the toolbox available to the electrochemists and developers of biosensors by engineering oxidase enzymes with improved performance in vivo and in vitro biosensing applications. Specifically, my dissertation work focuses primarily on two critical aspects of biosensor design: (1) the structure-informed rational improvement of three FDPGOs as potential nicotine oxidases and (2) the successful use of a gold binding peptide fusion sequence for the orientation-controlled immobilization of a putrescine oxidase on gold surfaces.
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