Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 2 of 2
Full-Text Articles in Entire DC Network
Electrochemical And Spectroscopic Study Of Peptide-Template Melanins, Daniel Courter, Olivia Rossi, Zhen Tian
Electrochemical And Spectroscopic Study Of Peptide-Template Melanins, Daniel Courter, Olivia Rossi, Zhen Tian
Honors Theses and Capstones
Melanins are organic polymers made up of 5,6-dihydroxyindole carboxylic acid (DHICA) and 5,6-dihydroxyindole (DHI). Biochemical systems synthesize melanins through a complex reaction pathway. Previous research exhibited that naturally-occurring melanins (NatMel) and their synthetic analogues (SynMel) can potentially serve as electrode materials for aqueous charge storage devices. Small surface area creates technical challenges for these melanins as charge storage materials. This research herein demonstrates that the structure of melanins can affect the charge storage capacities of monovalent Na+cations and divalent Mg2+ cations. 2-D sheet-like peptide melanins (PepMel) were synthesized into tripeptides consisting of aspartic acid (D), phenylalanine (F), …
Enzyme-Catalyzed Reactions Using Enzymes Immobilized On Non-Spherical Particles, Alexander D. Redfearn
Enzyme-Catalyzed Reactions Using Enzymes Immobilized On Non-Spherical Particles, Alexander D. Redfearn
Honors Theses and Capstones
Modern and industrial chemical reactions often utilize enzyme-catalyzed reactions to increase product yields. Given the high cost of enzymes it is desirable to preserve the activity of the enzymes and reuse them several times. In this study, I explored the possibility of immobilizing enzymes on custom-made non-spherical SU-8 microparticles to conduct enzyme-catalyzed reactions in flow reactors. The decomposition of hydrogen peroxide using bovine liver catalase was studied due to its well-understood enzyme kinetics. Soft lithography techniques were used to synthesize prismatic SU-8 microparticles. I will discuss the progress that has been made in immobilizing the enzyme on the particle surface …