Isolation and production of tandem collagen binding domain from clostridial collagenase ColG and developments in C1Q reagent production for future molecule characterization work

Author

Stephanie BeitleFollow

Date of Graduation

5-2022

Document Type

Thesis

Degree Name

Bachelor of Science in Chemical Engineering

Degree Level

Undergraduate

Department

Chemical Engineering

Advisor/Mentor

Sakon, Josh

Committee Member/Reader

Walker, Heather

Abstract

This thesis covers a two part project: the production methods to create a double collagen binding domain molecule with a growth factor for wound healing applications and the development of a new in-house production method for isolating C1q from bovine blood. The wound healing molecule was created using transformation, sonication, and purification before being tested via electrophoresis SDS page and Western blots to confirm the molecule’s presence. The C1q in-house production method utilizes an ultrafiltration flow cell rather than dialysis at a critical point in the process, allowing for researchers to not only be able to use a single small tank but also greatly reducing the amount of buffer needed for filtration.

Keywords

wound healing, biomolecular research, plasmid transformation, protein purification, ultrafiltration, C1q

Citation

Beitle, S. (2022). Isolation and production of tandem collagen binding domain from clostridial collagenase ColG and developments in C1Q reagent production for future molecule characterization work. Chemical Engineering Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/cheguht/187