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Author: Raymond Moody | Major: Biochemistry, Biology, Psychology | Semester: Fall 2024
My name is Raymond Moody, a triple major in Biochemistry, Biology, and Psychology at the Fulbright College of Arts and Sciences. This Fall 2024 semester, I have been conducting research under the mentorship of Professor Susanne Striegler in the Department of Chemistry & Biochemistry. My future plans include attending medical school, with a particular interest in Plastic Surgery. Over the past several months, my research has centered on developing a cost-effective method to extract and purify alpha-galactosidase from cantaloupe (Cucumis melo). This enzyme is crucial for breaking down complex sugars into simpler monosaccharides, making it significant for treating conditions like Fabry’s disease and improving various food industry processes. Through refining extraction protocols, employing precipitation techniques with PEG-6000, and using advanced analytical tools such as high-performance liquid chromatography (HPLC), I aim to confirm the enzyme’s purity and molecular weight. Ultimately, my work seeks to produce a more reliable and accessible enzyme protocol, benefiting both healthcare and industry.
I chose this research topic because it bridges fundamental biochemical knowledge with practical real-world applications. Drawing on my mentor’s expertise—Professor Striegler’s work in carbohydrate chemistry and enzymatic catalysis—I was able to develop protocols suited to isolating this enzyme. At first, I focused on homogenizing cantaloupe tissue and creating buffers that stabilized the protein before attempting protein precipitation at various concentrations of PEG-6000. This helped me concentrate the enzyme from a crude solution, laying a foundation for further analysis. While these initial steps were productive, they soon highlighted the need for more robust analytical methods.
To confirm the identity and purity of the enzyme, I turned to HPLC, using a Yarra™ 3 µm SEC-3000 LC Column. By uploading both standard proteins with known molecular weights and my sample, I could correlate retention times to molecular mass, providing a calibration curve that let me estimate the size of the proteins in my sample. From these comparisons, I identified peaks around 82 kDa and 46 kDa, numbers that aligned closely with subunits previously reported for related enzymes in watermelon, being 45 kDa. Since 82 kDa is close to twice 46 kDa, it is likely that this peak represents a dimer. The evolutionary link between cantaloupe and watermelon, separated by approximately 10 million years, suggests that these enzyme isoforms share structural and functional similarities. This strengthened my confidence that I was capturing the intended enzyme and not some unrelated contaminant.
The research process itself taught me invaluable lessons. When I initially struggled with protein precipitation, I learned to modify conditions—such as increasing centrifugation force—to achieve better yields. Throughout these challenges, I realized that scientific research is rarely straightforward and demands resilience, creativity, and iterative problem-solving. Working closely with Professor Striegler and other members offered a supportive environment. By sharing ideas, seeking help from peers familiar with biochemical technqiues, and testing out new strategies, I appreciated how communal knowledge accelerates scientific progress.
While my work this semester was confined to the lab (no travels to archives, archaeological sites, or conferences), the foundational data and methods I have produced open the door for future presentations and discussions at student research conferences. Such venues would give me the opportunity to share results, refine protocols based on feedback, and network with others who are engaged in similar endeavors. Beyond the immediate scope, the skills I’ve gained—experimental design, analytical reasoning, and resilience—are all qualities I will carry into my medical career. Understanding biochemical processes at the molecular level will also support my future work as a physician, potentially guiding me toward innovations that improve patient care.
In the coming steps, I will focus on further purifying the enzyme and conducting substrate-specific assays using compounds like p-nitrophenyl α-galactopyranoside to confirm the enzyme’s activity. As I approach medical school applications, I see these experiences as crucial stepping stones. They not only show me how biochemical research can evolve into tangible improvements in healthcare and industry, but they also ensure that I enter medical training with an enriched perspective—one that blends molecular understanding, analytical problem-solving, and clinical vision.