Major
Forensic Science
Anticipated Graduation Year
2023
Access Type
Open Access
Abstract
This study aimed to produce data to improve protein modeling software for B-glucosidase (BglB), a crucial enzyme in producing glucose from cellulose. It was hypothesized that BglB mutant T352V would demonstrate decreased catalytic efficiency and thermal stability compared to the wild type. The T352V mutation was first observed using Foldit Standalone modeling software. DNA sequencing and SDS-PAGE analysis confirmed mutation expression and purity. The kinetic assay indicated a decrease in catalytic efficiency in the T352V mutant. The thermostability assay showed no activity for the T352V mutant, suggesting an error occurred or the temperature range was too high.
Community Partners
Ashely Vater and the Siegel Lab at UC 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.
B-glucosidase Mutation T352V Catalytic Efficiency and Thermal Stability
This study aimed to produce data to improve protein modeling software for B-glucosidase (BglB), a crucial enzyme in producing glucose from cellulose. It was hypothesized that BglB mutant T352V would demonstrate decreased catalytic efficiency and thermal stability compared to the wild type. The T352V mutation was first observed using Foldit Standalone modeling software. DNA sequencing and SDS-PAGE analysis confirmed mutation expression and purity. The kinetic assay indicated a decrease in catalytic efficiency in the T352V mutant. The thermostability assay showed no activity for the T352V mutant, suggesting an error occurred or the temperature range was too high.