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

Disciplines

Biochemistry | Molecular Biology

Keywords

Protein, Transferrin

Publication Date

2023

Degree Granted

Bachelor of Arts

Document Type

Senior Independent Study Thesis

Available for download on Sunday, January 01, 2073

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