ORCID

https://orcid.org/0009-0000-5908-1667

Date of Award

2025

Document Type

Thesis

Degree Name

MS in Biology

Department

Biological Sciences

First Advisor

Juan Santos

Second Advisor

Javier Juarez

Third Advisor

Dianella Howarth

Abstract

Chitinases are essential enzymes found in living organisms such as amphibians, and they ensure that amphibians survive in their varied ecosystems. They are crucial in the digestion and immunity of most organisms, including plants and animals. Chitinases’ diversity of functions is a testament to their evolutionary adaptability. The primary function of chitinases is the breakdown of chitin, a complex polymer of saccharides often found in the exoskeleton of insects and the walls of fungi. Amphibians that feed on insects make use of chitinases to hydrolyze chitin into simpler sugars that can be easily absorbed to extract the necessary nutrients from the prey. Most amphibians inhabit moist habitats and have thin skins, so their life history makes them susceptible to fungal infections. Again, this makes chitinases essential in protecting them against these pathogens by identifying them and degrading the chitin in fungal cell walls, leading to their quick elimination. In spite of chitinase relevance, only a few evolutionary studies exist in amphibians that have revealed gene duplication and specialization patterns. This functional diversity has led to the origin of different chitinase genes, each of which is designed to adapt to harsh adaptation conditions or dietary use. Several genomic findings indicate that chitinases in vertebrates are often well-conserved. In contrast, those in amphibians have new modifications in need of further characterization, such as their ability to prevent fungal infections and help in the digestion of a chitin-rich diet. Continued study and understanding of the diversity and activity of amphibian chitinases hold an immeasurable source for further discoveries on their evolution, amphibian health and conservation, and possible mechanisms to mitigate fungal pathogens.

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