Major
Forensic Science
Anticipated Graduation Year
2024
Access Type
Open Access
Abstract
We performed this experiment to contribute data to the D2D Project, which seeks to determine if enzymatic function can be predicted based on primary structure of an enzyme (Beta-glucosidase B/BglB). To make this prediction, we created a T352V mutation for BglB. We hypothesized that BglB T352V mutation will demonstrate decreased catalytic efficiency and/or thermal stability compared to wild-type because increased local and overall scores signify that BglB has become less stable. In this experiment, we prepared and purified plasmid containing mutated Bgl-B gene, expressed and purified BglB, and performed enzymatic assays to determine catalytic efficiency of the mutant T352V Bgl-B.
Community Partners
Justin Seigel Lab at the University of California - Davis
Faculty Mentors & Instructors
Dr. Emma Feeney
Supported By
National Science Foundation
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Characterizing the T352V Mutation of Beta-Glucosidase B
We performed this experiment to contribute data to the D2D Project, which seeks to determine if enzymatic function can be predicted based on primary structure of an enzyme (Beta-glucosidase B/BglB). To make this prediction, we created a T352V mutation for BglB. We hypothesized that BglB T352V mutation will demonstrate decreased catalytic efficiency and/or thermal stability compared to wild-type because increased local and overall scores signify that BglB has become less stable. In this experiment, we prepared and purified plasmid containing mutated Bgl-B gene, expressed and purified BglB, and performed enzymatic assays to determine catalytic efficiency of the mutant T352V Bgl-B.