Casein phosphopeptide interferes the interactions between ferritin and ion irons.

Ferritin, a vital protein required to store iron in a cage-like structure, is critical for maintaining iron balance. Ferritin can be attacked by free radicals during iron reduction and release, thereby leading to oxidative damage. Whether other biomacromolecules such as casein phosphopeptides (CPP) could influence the ferritin's function in iron oxidation and release and affect the ferritin stability remains unclear. This study aims to investigate the effect of CPP on the ferritin­iron ion interaction, thereby focusing on role of CPP on ferritin stability. Results showed that CPP weakened the iron oxidation activity of ferritin but promoted iron release. Moreover, CPP could effectively chelate iron, capture hydroxyl radicals, and reduce the degradation of ferritin. This study highlights the role of CPP in the ferritin­iron relationship, and lays a foundation for understanding the interaction between ferritin, peptides, and metal ions.

Dual Decoration of Ferritin Nanocages by Caffeic Acid and Betanin with Covalent and Noncovalent Approaches: Structure and Stability Analyses.

Ferritin is a cage-like protein with modifiable outer and inner surfaces. To functionalize ferritin with preferable carrier applications, caffeic acid was first covalently bound to the soybean ferritin outer surface to fabricate a caffeic acid-ferritin complex (CFRT) by alkali treatment (pH 9.0). A decreased content of free amino acid (0.34 µmol/mg) and increased polyphenol binding equivalent (63.76 nmol/mg) indicated the formation of CFRT (ferritin/caffeic acid, 1:80). Fluorescence and infrared spectra verified the binding of caffeic acids to the ferritin structure. DSC indicated that the covalent modification enhanced the thermal stability of CFRT. Besides, CFRT maintained the typically spherical shape of ferritin (12 nm) and a hydration radius of 7.58 nm. Moreover, the bioactive colorant betanin was encapsulated in CFRT to form betanin-loaded CFRT (CFRTB), with an encapsulation rate of 15.5% (w/w). The betanin stabilities in CFRTB were significantly improved after heat, light, and Fe3+ treatments, and its red color retention was enhanced relative to the free betanin. This study delves into the modifiable ferritin application as nanocarriers of dual molecules and gives guidelines for betanin as a food colorant.

The application of ferritin in transporting and binding diverse metal ions.

The ferritin cage can not only load iron ions in its inner cavity, but also has the capacity to carry other metal ions, thus constructing a new biological nano-transport system. The nanoparticles formed by ferritin and minerals can be used as ingredients of mineral supplements, which overcome the shortcomings of traditional mineral ingredients such as low bioavailability. Moreover, ferritin can be used to remove heavy metal ions from contaminated food. Silver and palladium nanoparticles formed by ferritin are also applied as anticancer agents. Ferritin combined with metal ions can be also used to detect harmful substances. This review aims to provide a comprehensive overview of ferritin's function in transporting and binding metal ions, and discusses the limitations and future prospects, which offers valuable insights for the application of ferritin in mineral supplements, food detoxifiers, anticancer agents, and food detections.

Multifaceted Applications of Ferritin Nanocages in Delivering Metal Ions, Bioactive Compounds, and Enzymes: A Comprehensive Review.

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.

Phytoferritin functions in two interface-loading of natural pigment betanin and caffeic acid with enhanced color stability and the sustained release of betanin.

Betanin, a natural red pigment, is sensitive and prone to fading and discoloration, affecting its stability and bioavailability. Phytoferritin is a nano-diameter protein with unique interior-/exterior-interfaces. By the unique interfaces and pH-induced self-assembly of ferritin, a ferritin-betanin complex (FB) with an encapsulation efficiency of 17.66 ± 1.24% was prepared. The caffeic acid-FB (CFB) was further fabricated by attaching ferritin with caffeic acid, and the binding number n of caffeic acid was 88.47 ± 9.49, with a binding constant K of (1.63 ± 0.33) × 104 M-1. Fluorescence and Fourier transform infrared analysis indicated that the encapsulation of betanin and the binding of caffeic acid influenced the ferritin structure. The interaction between caffeic acid and ferritin was mainly through van der Waals forces and hydrogen bonds. TEM and DLS showed that the globular structure and diameter (12 nm) remained in CFB. Furthermore, the ferritin and caffeic acid exhibited a synergistic effect in enhancing thermal, light, and ferric ion stabilities, and controlled the betanin release in a more sustained manner in the simulated gastrointestinal tract. In addition, the antioxidant capacity of CFB was enhanced compared with free betanin. This study promotes the bioavailability of betanin by two interface-loading of ferritin, and guides the use of ferritin nanoparticles as a nanocarrier for pigment stabilization.

Phycobiliproteins, the pigment-protein complex form of natural food colorants and bioactive ingredients.

Currently, the use of synthetic pigments in foods is restricted since synthetic pigments are proven and suspected to be harmful to human health. Phycobiliproteins (PBPs), existed in phycobilisomes (PBSs) of algae, are a kind of pigment-proteins with intense color. The specific color of PBPs (red and blue) is given by the water-soluble open-chained tetrapyrrole chromophore (phycobilin) that covalently attaches to the apo-protein via thioether linkages to cysteine residues. According to the spectral characteristics of PBPs, they can be categorized as phycoerythrins (PEs), phycocyanins (PCs), allophycocyanins (APCs), and phycoerythrocyanins (PECs). PBPs can be used as natural food colorants, fluorescent substances, and bioactive ingredients in food applications owing to their color characteristics and physiological activities. This paper mainly summarizes the extraction and purification methods of the PBPs and reviews their characteristics and applications. Moreover, the use of several strategies such as additives, microencapsulation, electrospray, and cross-linking to improve the stability and bioavailability of PBPs as well as the future outlooks of PBPs as natural colorants in food commercialization are elucidated.