Title of Oral/Poster Presentation

Improving purification solubility of recombinant spider silk proteins (rSSP) with coexpressed chaperone proteins

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

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Apr 12th, 10:30 AM Apr 12th, 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.