Premium
Iron Binding by Ovotransferrin from Ferric Nitrilotriacetate at pH 5 and pH 5.5
Author(s) -
THOMPSON DONALD B.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb08988.x
Subject(s) - chemistry , denaturation (fissile materials) , ovotransferrin , enthalpy , ferric , egg white , inorganic chemistry , chromatography , nuclear chemistry , biochemistry , physics , quantum mechanics
Binding of iron to ovotransferrin (OTf) in egg white at low pH was studied. At pH 5 iron as ferric nitrilotriacetate (FeNTA) bound to only 25% of the OTf iron‐binding sites. Although this binding caused a 1°C increase in OTf denaturation temperature, enthalpy of denaturation apparently decreased. At pH 5.5, the apo‐OTf denaturation temperature was about 4°C higher than at pH 5. FeNTA bound to 40% of the OTf iron‐binding sites; again a small increase in denaturation temperature and an apparent decrease in enthalpy was observed. Work with purified OTf suggests that the denaturation enthalpy decrease observed in egg white may be due to overlapping of the OTf and albumin endotherms.