Ferritin,
a distinctive iron-storage protein, possesses a unique
cage-like nanoscale structure that enables it to encapsulate and deliver
a wide range of biomolecules. Recent advances prove that ferritin
can serve as an efficient 8 nm diameter carrier for various bioinorganic
nutrients, such as minerals, bioactive polyphenols, and enzymes. This
review offers a comprehensive summary of ferritin’s structural
features from different sources and emphasizes its functions in iron
supplementation, calcium delivery, single- and coencapsulation of
polyphenols, and enzyme package. Additionally, the influence of innovative
food processing technologies, including manothermosonication, pulsed
electric field, and atmospheric cold plasma, on the structure and
function of ferritin are examined. Furthermore, the limitations and
prospects of ferritin in food and nutritional applications are discussed.
The exploration of ferritin as a multifunctional protein with the
capacity to load various biomolecules is crucial to fully harnessing
its potential in food applications.