Strategies in disulfide bond formations to stabilize X-prolyl amino dipeptidases for hydrolysis of proline-rich amino acid sequences
Faculty Sponsor
Dr. Deanna Ojennus
dojennus@whitworth.edu
Session Type
Poster Presentation
Research Project Abstract
Gluten proteins typically have a large proline content in their amino acid sequences which yields high resistivity to hydrolysis from regular digestive enzymes within humans. As a result, Celiac disease exists in genetically predisposed individuals as a disorder that ultimately leads to pain, inflammation and malnutrition when gluten is ingested. X-prolyl amino dipeptidases (PEPX) are enzymes that have potential to more effectively hydrolyze the high-proline sequences of gluten and other food allergens. The goals of this study were to further discover how disulfide bonding within PEPX mutant species may stabilize the enzyme against hydrolysis by other digestive enzymes. Two mutant constructs V669C-A759C and G232C-S442C were expressed and purified and compared to wild type mutant activity. Disulfide bond formation was examined by gel shift assay.
Session Number
PS3
Location
HUB Multipurpose Room
Abstract Number
PS3-k
Strategies in disulfide bond formations to stabilize X-prolyl amino dipeptidases for hydrolysis of proline-rich amino acid sequences
HUB Multipurpose Room
Gluten proteins typically have a large proline content in their amino acid sequences which yields high resistivity to hydrolysis from regular digestive enzymes within humans. As a result, Celiac disease exists in genetically predisposed individuals as a disorder that ultimately leads to pain, inflammation and malnutrition when gluten is ingested. X-prolyl amino dipeptidases (PEPX) are enzymes that have potential to more effectively hydrolyze the high-proline sequences of gluten and other food allergens. The goals of this study were to further discover how disulfide bonding within PEPX mutant species may stabilize the enzyme against hydrolysis by other digestive enzymes. Two mutant constructs V669C-A759C and G232C-S442C were expressed and purified and compared to wild type mutant activity. Disulfide bond formation was examined by gel shift assay.
