Honors Theses
Advisor
Dr. Matthew Lopper and Dr. Justin Biffinger
Department
Chemistry
Publication Date
4-22-2026
Document Type
Honors Thesis
Abstract
Fungal degradation of polymer coatings on military aircraft causes accelerated damage and corrosion and results in expensive repairs to affected aircraft, especially in warm and humid environments. This project aims to identify and characterize the fungal enzymes responsible for degrading these coatings and give us a better understanding of their mechanisms of degradation. The focus is specifically on hydrolytic cutinase enzymes, which are secreted by fungi to degrade plant cutin and similar natural polymers. We hypothesize that these enzymes can also break down synthetic polymers, such as the polyester-based coatings used on aircraft, by catalyzing hydrolysis of their ester bonds. In order to explore their role in polymer coating breakdown, the genes encoding two putative cutinase enzymes were cloned from Naganishia albida into a yeast overexpression vector, pPICZalpha-A. The His-tagged recombinant proteins were overexpressed in Pichia pastoris strain KM71H and the resulting proteins were purified by nickel affinity chromatography and ion exchange chromatography. The future direction of this work will involve studying how the enzymes interact with polymer substrates and break them down. This will provide insights into the mechanism of action for degradation and it will help identify alternative polymer coatings that can resist this degradation. The outcomes of this project can be applied to mitigate the impact of fungal degradation and help develop long-term solutions to protect military aircraft.
Permission Statement
This item is protected by copyright law (Title 17, U.S. Code) and may only be used for noncommercial, educational, and scholarly purposes.
Keywords
Undergraduate research
eCommons Citation
Bair, Allison, "Molecular Cloning and Purification of Recombinant Cutinase Enzymes to study Enzymatic Degradation of Aircraft Polymer Coatings" (2026). Honors Theses. 495.
https://ecommons.udayton.edu/uhp_theses/495
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