Precipitation of Porcine Hemoglobin by Nonionic Polymers
Department
Chemical and Biochemical Engineering
Major
Biochemical Engineering
Research Advisor
Forciniti, Daniel
Advisor's Department
Chemical and Biochemical Engineering
Abstract
Protein precipitation is a commonly used unit operation in the process of isolating and purifying proteins. This project focused on the use of nonionic polymers to precipitate porcine hemoglobin. Elements of experimental design were used to select meaningful sets of experiments. The effects of various factors and two-factor interactions on the solubility of the protein were examined. The data indicated that higher weight polymers and higher concentrations of polymer both decrease porcine hemoglobin solubility, but the two-factor interaction between polymer concentration and molecular weight was an inconsistent interaction, resulting in higher solubility than would be independently expected. The role played by EO/PO fraction in solubility was also studied.
Biography
Clayton Buback was born in St. Charles, Missouri. At age 16, he enrolled in the Missouri Academy of Science, Mathematics, and Computing, and graduated at the top of his class, earning an Associate of Science Degree and High School Diploma simultaneously. He now attends the Missouri University of Science and Technology, and is working on two Bachelor’s Degrees: one in Biology, and one in Biochemical Engineering. Clayton will graduate from Missouri S&T in May of 2014, and will start medical school at the University of Rochester the following fall.
Research Category
Engineering
Presentation Type
Oral Presentation
Document Type
Presentation
Award
Engineering oral presentation, Second place
Location
Gasconade Room
Presentation Date
16 Apr 2014, 9:00 am - 9:30 am
Precipitation of Porcine Hemoglobin by Nonionic Polymers
Gasconade Room
Protein precipitation is a commonly used unit operation in the process of isolating and purifying proteins. This project focused on the use of nonionic polymers to precipitate porcine hemoglobin. Elements of experimental design were used to select meaningful sets of experiments. The effects of various factors and two-factor interactions on the solubility of the protein were examined. The data indicated that higher weight polymers and higher concentrations of polymer both decrease porcine hemoglobin solubility, but the two-factor interaction between polymer concentration and molecular weight was an inconsistent interaction, resulting in higher solubility than would be independently expected. The role played by EO/PO fraction in solubility was also studied.
