Date of Graduation

5-2026

Document Type

Thesis

Degree Name

Bachelor of Science in Chemistry

Degree Level

Undergraduate

Department

Chemistry & Biochemistry

Advisor/Mentor

Striegler, Susanne

Committee Member

Hershberger, Margaret

Second Committee Member

Coridan, Robert

Third Committee Member

Chen, Jingyi

Abstract

The enzyme α-galactosidase is a type of glycosidase that removes galactose sugar units from larger molecules in cells. Compounds that inhibit glycosidases have been useful for understanding the structure and function of the enzymes they inhibit, and some have been used to treat certain diseases. Using inhibitors of α-galactosidase to study its characteristics and mechanisms may provide insights into its role in disease and its general utility. Advances in fields such as agriculture, sustainable fuels, and biomedicine may be facilitated by inhibition studies of α-galactosidase, but the current library of known inhibitors is relatively lacking. Obtaining α-galactosidase enzymes from chemical suppliers is often difficult, which provides an obstacle to the development of new inhibitors. The goal of this project, therefore, is to develop a method by which active, pure α-galactosidase may be reliably obtained from an accessible source. Watermelon (Citrullus lanatus) fruit has been shown to produce an α-galactosidase. Ammonium sulfate and PEG precipitation methods were used to extract protein solutions from watermelon, and both methods yielded α-galactosidase activity in solution when assayed with an artificial substrate. Gel permeation chromatography was used to estimate the molecular weight.

Keywords

alpha-galactosidase; enzyme purification; glycosidase inhibition; protein precipitation; gel permeation chromatography

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