Abstract
Ferritin is a cage-like carrier protein with multiple interfaces, allowing for the encapsulation and delivery of biologically active molecules. In this study, hesperetin was covalently conjugated to the outer surface of ferritin to fabricate hesperetin covalently modified ferritin (HFRT) at pH 9.0. This conjugation resulted in a binding equivalent of hesperetin to ferritin of 12.33 ± 0.56 nmol/mg. After covalent binding, the free amino content of HFRT decreased and the secondary and tertiary structures of HFRT were changed relative to the structure of control ferritin. In addition, HFRT successfully retained the cage-like structure of ferritin and exhibited reversible self-assembly property regulated by pH shifts. Taking advantage of this property, quercetin was encapsulated into the inner surface of HFRT with an encapsulation ratio of 14.0 ± 1.36% (w/w). The modification with hesperetin improved the digestive stability of ferritin and enhanced the stability of encapsulated quercetin against thermal treatment compared to unmodified ferritin. This study explored the functions of the double interfaces of ferritin by covalent and non-covalent binding of two different bioactive compounds. The results can help guide the functionalization of the ferritin cage as a nanocarrier in food application.
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