Abstract
Metal ions are harmful to human health, causing multiple disruptions in the body as they accumulate over the years. While methods exist that extract heavy metal ions from drinking water, they create sludge as a by-product, require prior treatment or are not specific. Bioadsorption of metal ions through proteins is selective and non-polluting, and has been a promising field, but no protein has been studied in an immobilized state for water purification. The goal of the project was to test if immobilized metal ion binding transferrin could adsorb Fe3+ from solution. The results of the experiment show SOMS binds more Fe3+ (885 µg/g in total)than immobilized transferrin. Although large amounts of transferrin is bound into SOMS, immobilized transferrin does not appear to bind any Fe3+. The loss of iron binding affinity may be due to loss of conformation flexibility. FT-IR shows immobilized transferrin have the peaks at 1415 cm-1 and 1560 cm-1 present, which free transferrin with iron bound does not have. An interesting finding was that SOMS, which is hydrophobic, bound Fe3+ of 885 ug/g of which 64% could not be removed, despite an EDTA rinse which has a strong binding affinity.
Advisor
Edmiston, Paul
Department
Biochemistry and Molecular Biology
Recommended Citation
Shahreen, Shiropa, "Immobilization of Transferrin in Swellable Organically Modified Silica for Remediation of Heavy Metal Ions" (2023). Senior Independent Study Theses. Paper 10427.
https://openworks.wooster.edu/independentstudy/10427
Disciplines
Biochemistry | Molecular Biology
Keywords
Protein, Transferrin
Publication Date
2023
Degree Granted
Bachelor of Arts
Document Type
Senior Independent Study Thesis
© Copyright 2023 Shiropa Shahreen