Class
Article
College
College of Science
Faculty Mentor
Randy Lewis
Presentation Type
Poster Presentation
Abstract
Escherichia Coli is a widely used method of producing spider silk proteins, however the recovery and purification of silk proteins has proven problematic due to the nature of spider silk proteins to self-assemble. A genetic approach to solve downstream purification problems that has shown to be effective with other difficult proteins is coexpression of chaperone vectors. Coexpressed chaperone proteins have been shown to improve folding and increase solubility of proteins, resulting in an increased amount of protein recovered from the processing supernatant. Coexpressed chaperone proteins failed to significantly improve solubility in initial trials, however more should be done to study their value in improving recombinant spider silk protein solubility.
Location
The North Atrium
Start Date
4-12-2018 10:30 AM
End Date
4-12-2018 11:45 AM
Improving Purification Solubility of Recombinant Spider Silk Proteins (rSSP) With Coexpressed Chaperone Proteins
The North Atrium
Escherichia Coli is a widely used method of producing spider silk proteins, however the recovery and purification of silk proteins has proven problematic due to the nature of spider silk proteins to self-assemble. A genetic approach to solve downstream purification problems that has shown to be effective with other difficult proteins is coexpression of chaperone vectors. Coexpressed chaperone proteins have been shown to improve folding and increase solubility of proteins, resulting in an increased amount of protein recovered from the processing supernatant. Coexpressed chaperone proteins failed to significantly improve solubility in initial trials, however more should be done to study their value in improving recombinant spider silk protein solubility.