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Full-Text Articles in Physical Sciences and Mathematics
A Biophysical Investigation Of Stability, Ligand Binding, And Iron State Of Cyp102a1, Catherine A. Denning-Jannace
A Biophysical Investigation Of Stability, Ligand Binding, And Iron State Of Cyp102a1, Catherine A. Denning-Jannace
Theses and Dissertations--Chemistry
Cytochrome P450s (CYPs) are cysteine ligated Fe-heme monooxygenases that are found in all domains of life. In mammals, they have a role in xenobiotic metabolism and steroid synthesis, making them a fundamental requirement for survival. In addition, their ability to perform a variety of chemical reactions on an array of substrates makes CYPs highly sought for biotechnical applications such as wastewater remediation, production of potential drug candidates, and creation of drug metabolites. By mutating specific amino acids, these enzymes can be engineered to change their substrate binding profiles and achieve stereo- and regio-specific chemistry. While these mutations are essential to …
Stability Improvement By Crosslinking Of Previously Immobilized Glucose Oxidase On Carbon Nanotube-Based Bioanode, Tahsi̇n Bahar
Stability Improvement By Crosslinking Of Previously Immobilized Glucose Oxidase On Carbon Nanotube-Based Bioanode, Tahsi̇n Bahar
Turkish Journal of Chemistry
Bioanode stability with glucose oxidase was enhanced significantly by covalent crosslinking without substantial enzymatic activity and affinity loss. Initially, glucose oxidase was immobilized by aldehyde groups on the electrode that was developed using ferrocenecarboxaldehyde, polyethyleneimine, multiwall carbon nanotubes, and carbon cloth for biofuel cell applications. The glucose oxidase half-life was extended by more than 4 times, from 27.2 to 124.7 h, after the electrode was crosslinked. Enzymatic kinetic parameters were determined for the crosslinked enzyme and they were compared to the noncrosslinked immobilized enzyme parameters on the electrode. The apparent substrate affinity of the crosslinked enzyme electrode was decreased (i.e. …